P98164 · LRP2_HUMAN
- ProteinLow-density lipoprotein receptor-related protein 2
- GeneLRP2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids4655 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Multiligand endocytic receptor (By similarity).
Acts together with CUBN to mediate endocytosis of high-density lipoproteins (By similarity).
Mediates receptor-mediated uptake of polybasic drugs such as aprotinin, aminoglycosides and polymyxin B (By similarity).
In the kidney, mediates the tubular uptake and clearance of leptin (By similarity).
Also mediates transport of leptin across the blood-brain barrier through endocytosis at the choroid plexus epithelium (By similarity).
Endocytosis of leptin in neuronal cells is required for hypothalamic leptin signaling and leptin-mediated regulation of feeding and body weight (By similarity).
Mediates endocytosis and subsequent lysosomal degradation of CST3 in kidney proximal tubule cells (By similarity).
Mediates renal uptake of 25-hydroxyvitamin D3 in complex with the vitamin D3 transporter GC/DBP (By similarity).
Mediates renal uptake of metallothionein-bound heavy metals (PubMed:15126248).
Together with CUBN, mediates renal reabsorption of myoglobin (By similarity).
Mediates renal uptake and subsequent lysosomal degradation of APOM (By similarity).
Plays a role in kidney selenium homeostasis by mediating renal endocytosis of selenoprotein SEPP1 (By similarity).
Mediates renal uptake of the antiapoptotic protein BIRC5/survivin which may be important for functional integrity of the kidney (PubMed:23825075).
Mediates renal uptake of matrix metalloproteinase MMP2 in complex with metalloproteinase inhibitor TIMP1 (By similarity).
Mediates endocytosis of Sonic hedgehog protein N-product (ShhN), the active product of SHH (By similarity).
Also mediates ShhN transcytosis (By similarity).
In the embryonic neuroepithelium, mediates endocytic uptake and degradation of BMP4, is required for correct SHH localization in the ventral neural tube and plays a role in patterning of the ventral telencephalon (By similarity).
Required at the onset of neurulation to sequester SHH on the apical surface of neuroepithelial cells of the rostral diencephalon ventral midline and to control PTCH1-dependent uptake and intracellular trafficking of SHH (By similarity).
During neurulation, required in neuroepithelial cells for uptake of folate bound to the folate receptor FOLR1 which is necessary for neural tube closure (By similarity).
In the adult brain, negatively regulates BMP signaling in the subependymal zone which enables neurogenesis to proceed (By similarity).
In astrocytes, mediates endocytosis of ALB which is required for the synthesis of the neurotrophic factor oleic acid (By similarity).
Involved in neurite branching (By similarity).
During optic nerve development, required for SHH-mediated migration and proliferation of oligodendrocyte precursor cells (By similarity).
Mediates endocytic uptake and clearance of SHH in the retinal margin which protects retinal progenitor cells from mitogenic stimuli and keeps them quiescent (By similarity).
Plays a role in reproductive organ development by mediating uptake in reproductive tissues of androgen and estrogen bound to the sex hormone binding protein SHBG (By similarity).
Mediates endocytosis of angiotensin-2 (By similarity).
Also mediates endocytosis of angiotensis 1-7 (By similarity).
Binds to the complex composed of beta-amyloid protein 40 and CLU/APOJ and mediates its endocytosis and lysosomal degradation (By similarity).
Required for embryonic heart development (By similarity).
Required for normal hearing, possibly through interaction with estrogen in the inner ear (By similarity).
Acts together with CUBN to mediate endocytosis of high-density lipoproteins (By similarity).
Mediates receptor-mediated uptake of polybasic drugs such as aprotinin, aminoglycosides and polymyxin B (By similarity).
In the kidney, mediates the tubular uptake and clearance of leptin (By similarity).
Also mediates transport of leptin across the blood-brain barrier through endocytosis at the choroid plexus epithelium (By similarity).
Endocytosis of leptin in neuronal cells is required for hypothalamic leptin signaling and leptin-mediated regulation of feeding and body weight (By similarity).
Mediates endocytosis and subsequent lysosomal degradation of CST3 in kidney proximal tubule cells (By similarity).
Mediates renal uptake of 25-hydroxyvitamin D3 in complex with the vitamin D3 transporter GC/DBP (By similarity).
Mediates renal uptake of metallothionein-bound heavy metals (PubMed:15126248).
Together with CUBN, mediates renal reabsorption of myoglobin (By similarity).
Mediates renal uptake and subsequent lysosomal degradation of APOM (By similarity).
Plays a role in kidney selenium homeostasis by mediating renal endocytosis of selenoprotein SEPP1 (By similarity).
Mediates renal uptake of the antiapoptotic protein BIRC5/survivin which may be important for functional integrity of the kidney (PubMed:23825075).
Mediates renal uptake of matrix metalloproteinase MMP2 in complex with metalloproteinase inhibitor TIMP1 (By similarity).
Mediates endocytosis of Sonic hedgehog protein N-product (ShhN), the active product of SHH (By similarity).
Also mediates ShhN transcytosis (By similarity).
In the embryonic neuroepithelium, mediates endocytic uptake and degradation of BMP4, is required for correct SHH localization in the ventral neural tube and plays a role in patterning of the ventral telencephalon (By similarity).
Required at the onset of neurulation to sequester SHH on the apical surface of neuroepithelial cells of the rostral diencephalon ventral midline and to control PTCH1-dependent uptake and intracellular trafficking of SHH (By similarity).
During neurulation, required in neuroepithelial cells for uptake of folate bound to the folate receptor FOLR1 which is necessary for neural tube closure (By similarity).
In the adult brain, negatively regulates BMP signaling in the subependymal zone which enables neurogenesis to proceed (By similarity).
In astrocytes, mediates endocytosis of ALB which is required for the synthesis of the neurotrophic factor oleic acid (By similarity).
Involved in neurite branching (By similarity).
During optic nerve development, required for SHH-mediated migration and proliferation of oligodendrocyte precursor cells (By similarity).
Mediates endocytic uptake and clearance of SHH in the retinal margin which protects retinal progenitor cells from mitogenic stimuli and keeps them quiescent (By similarity).
Plays a role in reproductive organ development by mediating uptake in reproductive tissues of androgen and estrogen bound to the sex hormone binding protein SHBG (By similarity).
Mediates endocytosis of angiotensin-2 (By similarity).
Also mediates endocytosis of angiotensis 1-7 (By similarity).
Binds to the complex composed of beta-amyloid protein 40 and CLU/APOJ and mediates its endocytosis and lysosomal degradation (By similarity).
Required for embryonic heart development (By similarity).
Required for normal hearing, possibly through interaction with estrogen in the inner ear (By similarity).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 1126 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 1129 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 1131 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 1133 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 1139 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 1140 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 1208 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 1210 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 1212 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 1218 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 1219 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameLow-density lipoprotein receptor-related protein 2
- Short namesLRP-2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP98164
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Apical cell membrane ; Single-pass type I membrane protein
Note: Localizes to brush border membranes in the kidney. In the endolymphatic sac of the inner ear, located in the lumen of endosomes as a soluble form.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 26-4423 | Extracellular | ||||
Sequence: QECDSAHFRCGSGHCIPADWRCDGTKDCSDDADEIGCAVVTCQQGYFKCQSEGQCIPNSWVCDQDQDCDDGSDERQDCSQSTCSSHQITCSNGQCIPSEYRCDHVRDCPDGADENDCQYPTCEQLTCDNGACYNTSQKCDWKVDCRDSSDEINCTEICLHNEFSCGNGECIPRAYVCDHDNDCQDGSDEHACNYPTCGGYQFTCPSGRCIYQNWVCDGEDDCKDNGDEDGCESGPHDVHKCSPREWSCPESGRCISIYKVCDGILDCPGREDENNTSTGKYCSMTLCSALNCQYQCHETPYGGACFCPPGYIINHNDSRTCVEFDDCQIWGICDQKCESRPGRHLCHCEEGYILERGQYCKANDSFGEASIIFSNGRDLLIGDIHGRSFRILVESQNRGVAVGVAFHYHLQRVFWTDTVQNKVFSVDINGLNIQEVLNVSVETPENLAVDWVNNKIYLVETKVNRIDMVNLDGSYRVTLITENLGHPRGIAVDPTVGYLFFSDWESLSGEPKLERAFMDGSNRKDLVKTKLGWPAGVTLDMISKRVYWVDSRFDYIETVTYDGIQRKTVVHGGSLIPHPFGVSLFEGQVFFTDWTKMAVLKANKFTETNPQVYYQASLRPYGVTVYHSLRQPYATNPCKDNNGGCEQVCVLSHRTDNDGLGFRCKCTFGFQLDTDERHCIAVQNFLIFSSQVAIRGIPFTLSTQEDVMVPVSGNPSFFVGIDFDAQDSTIFFSDMSKHMIFKQKIDGTGREILAANRVENVESLAFDWISKNLYWTDSHYKSISVMRLADKTRRTVVQYLNNPRSVVVHPFAGYLFFTDWFRPAKIMRAWSDGSHLLPVINTTLGWPNGLAIDWAASRLYWVDAYFDKIEHSTFDGLDRRRLGHIEQMTHPFGLAIFGEHLFFTDWRLGAIIRVRKADGGEMTVIRSGIAYILHLKSYDVNIQTGSNACNQPTHPNGDCSHFCFPVPNFQRVCGCPYGMRLASNHLTCEGDPTNEPPTEQCGLFSFPCKNGRCVPNYYLCDGVDDCHDNSDEQLCGTLNNTCSSSAFTCGHGECIPAHWRCDKRNDCVDGSDEHNCPTHAPASCLDTQYTCDNHQCISKNWVCDTDNDCGDGSDEKNCNSTETCQPSQFNCPNHRCIDLSFVCDGDKDCVDGSDEVGCVLNCTASQFKCASGDKCIGVTNRCDGVFDCSDNSDEAGCPTRPPGMCHSDEFQCQEDGICIPNFWECDGHPDCLYGSDEHNACVPKTCPSSYFHCDNGNCIHRAWLCDRDNDCGDMSDEKDCPTQPFRCPSWQWQCLGHNICVNLSVVCDGIFDCPNGTDESPLCNGNSCSDFNGGCTHECVQEPFGAKCLCPLGFLLANDSKTCEDIDECDILGSCSQHCYNMRGSFRCSCDTGYMLESDGRTCKVTASESLLLLVASQNKIIADSVTSQVHNIYSLVENGSYIVAVDFDSISGRIFWSDATQGKTWSAFQNGTDRRVVFDSSIILTETIAIDWVGRNLYWTDYALETIEVSKIDGSHRTVLISKNLTNPRGLALDPRMNEHLLFWSDWGHHPRIERASMDGSMRTVIVQDKIFWPCGLTIDYPNRLLYFMDSYLDYMDFCDYNGHHRRQVIASDLIIRHPYALTLFEDSVYWTDRATRRVMRANKWHGGNQSVVMYNIQWPLGIVAVHPSKQPNSVNPCAFSRCSHLCLLSSQGPHFYSCVCPSGWSLSPDLLNCLRDDQPFLITVRQHIIFGISLNPEVKSNDAMVPIAGIQNGLDVEFDDAEQYIYWVENPGEIHRVKTDGTNRTVFASISMVGPSMNLALDWISRNLYSTNPRTQSIEVLTLHGDIRYRKTLIANDGTALGVGFPIGITVDPARGKLYWSDQGTDSGVPAKIASANMDGTSVKTLFTGNLEHLECVTLDIEEQKLYWAVTGRGVIERGNVDGTDRMILVHQLSHPWGIAVHDSFLYYTDEQYEVIERVDKATGANKIVLRDNVPNLRGLQVYHRRNAAESSNGCSNNMNACQQICLPVPGGLFSCACATGFKLNPDNRSCSPYNSFIVVSMLSAIRGFSLELSDHSETMVPVAGQGRNALHVDVDVSSGFIYWCDFSSSVASDNAIRRIKPDGSSLMNIVTHGIGENGVRGIAVDWVAGNLYFTNAFVSETLIEVLRINTTYRRVLLKVTVDMPRHIVVDPKNRYLFWADYGQRPKIERSFLDCTNRTVLVSEGIVTPRGLAVDRSDGYVYWVDDSLDIIARIRINGENSEVIRYGSRYPTPYGITVFENSIIWVDRNLKKIFQASKEPENTEPPTVIRDNINWLRDVTIFDKQVQPRSPAEVNNNPCLENNGGCSHLCFALPGLHTPKCDCAFGTLQSDGKNCAISTENFLIFALSNSLRSLHLDPENHSPPFQTINVERTVMSLDYDSVSDRIYFTQNLASGVGQISYATLSSGIHTPTVIASGIGTADGIAFDWITRRIYYSDYLNQMINSMAEDGSNRTVIARVPKPRAIVLDPCQGYLYWADWDTHAKIERATLGGNFRVPIVNSSLVMPSGLTLDYEEDLLYWVDASLQRIERSTLTGVDREVIVNAAVHAFGLTLYGQYIYWTDLYTQRIYRANKYDGSGQIAMTTNLLSQPRGINTVVKNQKQQCNNPCEQFNGGCSHICAPGPNGAECQCPHEGNWYLANNRKHCIVDNGERCGASSFTCSNGRCISEEWKCDNDNDCGDGSDEMESVCALHTCSPTAFTCANGRCVQYSYRCDYYNDCGDGSDEAGCLFRDCNATTEFMCNNRRCIPREFICNGVDNCHDNNTSDEKNCPDRTCQSGYTKCHNSNICIPRVYLCDGDNDCGDNSDENPTYCTTHTCSSSEFQCASGRCIPQHWYCDQETDCFDASDEPASCGHSERTCLADEFKCDGGRCIPSEWICDGDNDCGDMSDEDKRHQCQNQNCSDSEFLCVNDRPPDRRCIPQSWVCDGDVDCTDGYDENQNCTRRTCSENEFTCGYGLCIPKIFRCDRHNDCGDYSDERGCLYQTCQQNQFTCQNGRCISKTFVCDEDNDCGDGSDELMHLCHTPEPTCPPHEFKCDNGRCIEMMKLCNHLDDCLDNSDEKGCGINECHDPSISGCDHNCTDTLTSFYCSCRPGYKLMSDKRTCVDIDECTEMPFVCSQKCENVIGSYICKCAPGYLREPDGKTCRQNSNIEPYLIFSNRYYLRNLTIDGYFYSLILEGLDNVVALDFDRVEKRLYWIDTQRQVIERMFLNKTNKETIINHRLPAAESLAVDWVSRKLYWLDARLDGLFVSDLNGGHRRMLAQHCVDANNTFCFDNPRGLALHPQYGYLYWADWGHRAYIGRVGMDGTNKSVIISTKLEWPNGITIDYTNDLLYWADAHLGYIEYSDLEGHHRHTVYDGALPHPFAITIFEDTIYWTDWNTRTVEKGNKYDGSNRQTLVNTTHRPFDIHVYHPYRQPIVSNPCGTNNGGCSHLCLIKPGGKGFTCECPDDFRTLQLSGSTYCMPMCSSTQFLCANNEKCIPIWWKCDGQKDCSDGSDELALCPQRFCRLGQFQCSDGNCTSPQTLCNAHQNCPDGSDEDRLLCENHHCDSNEWQCANKRCIPESWQCDTFNDCEDNSDEDSSHCASRTCRPGQFRCANGRCIPQAWKCDVDNDCGDHSDEPIEECMSSAHLCDNFTEFSCKTNYRCIPKWAVCNGVDDCRDNSDEQGCEERTCHPVGDFRCKNHHCIPLRWQCDGQNDCGDNSDEENCAPRECTESEFRCVNQQCIPSRWICDHYNDCGDNSDERDCEMRTCHPEYFQCTSGHCVHSELKCDGSADCLDASDEADCPTRFPDGAYCQATMFECKNHVCIPPYWKCDGDDDCGDGSDEELHLCLDVPCNSPNRFRCDNNRCIYSHEVCNGVDDCGDGTDETEEHCRKPTPKPCTEYEYKCGNGHCIPHDNVCDDADDCGDWSDELGCNKGKERTCAENICEQNCTQLNEGGFICSCTAGFETNVFDRTSCLDINECEQFGTCPQHCRNTKGSYECVCADGFTSMSDRPGKRCAAEGSSPLLLLPDNVRIRKYNLSSERFSEYLQDEEYIQAVDYDWDPKDIGLSVVYYTVRGEGSRFGAIKRAYIPNFESGRNNLVQEVDLKLKYVMQPDGIAVDWVGRHIYWSDVKNKRIEVAKLDGRYRKWLISTDLDQPAAIAVNPKLGLMFWTDWGKEPKIESAWMNGEDRNILVFEDLGWPTGLSIDYLNNDRIYWSDFKEDVIETIKYDGTDRRVIAKEAMNPYSLDIFEDQLYWISKEKGEVWKQNKFGQGKKEKTLVVNPWLTQVRIFHQLRYNKSVPNLCKQICSHLCLLRPGGYSCACPQGSSFIEGSTTECDAAIELPINLPPPCRCMHGGNCYFDETDLPKCKCPSGYTGKYCEMAFSKGISPGTT | ||||||
Transmembrane | 4424-4446 | Helical | ||||
Sequence: AVAVLLTILLIVVIGALAIAGFF | ||||||
Topological domain | 4447-4655 | Cytoplasmic | ||||
Sequence: HYRRTGSLLPALPKLPSLSSLVKPSENGNGVTFRSGADLNMDIGVSGFGPETAIDRSMAMSEDFVMEMGKQPIIFENPMYSARDSAVKVVQPIQVTVSENVDNKNYGSPINPSEIVPETNPTSPAADGTQVTKWNLFKRKSKQTTNFENPIYAQMENEQKESVAATPPPSPSLPAKPKPPSRRDPTPTYSATEDTFKDTANLVKEDSEV |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Donnai-Barrow syndrome (DBS)
- Note
- DescriptionAn autosomal recessive syndrome characterized by complete or partial agenesis of the corpus callosum, congenital diaphragmatic hernia, facial dysmorphology, ocular anomalies, sensorineural hearing loss, developmental delay, and proteinuria. There is variability in the expression of some features, such as diaphragmatic hernia, corpus callosum anomalies and proteinuria.
- See alsoMIM:222448
Natural variants in DBS
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_037013 | 2522 | Y>H | in DBS; dbSNP:rs80338747 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_037009 | 83 | in dbSNP:rs2229263 | |||
Sequence: N → S | ||||||
Natural variant | VAR_064727 | 103 | found in a renal cell carcinoma sample; somatic mutation | |||
Sequence: C → R | ||||||
Natural variant | VAR_061294 | 259 | in dbSNP:rs34693334 | |||
Sequence: G → R | ||||||
Natural variant | VAR_037010 | 669 | in dbSNP:rs34291900 | |||
Sequence: G → D | ||||||
Natural variant | VAR_037011 | 909 | in dbSNP:rs36082715 | |||
Sequence: H → R | ||||||
Natural variant | VAR_037012 | 1083 | in dbSNP:rs2302691 | |||
Sequence: H → Q | ||||||
Natural variant | VAR_029182 | 1279 | in dbSNP:rs17848149 | |||
Sequence: D → A | ||||||
Natural variant | VAR_005421 | 1287 | ||||
Sequence: A → P | ||||||
Natural variant | VAR_029183 | 2012 | in dbSNP:rs4667596 | |||
Sequence: R → K | ||||||
Natural variant | VAR_020218 | 2065 | in dbSNP:rs2228168 | |||
Sequence: I → T | ||||||
Natural variant | VAR_037013 | 2522 | in DBS; dbSNP:rs80338747 | |||
Sequence: Y → H | ||||||
Natural variant | VAR_029184 | 2632 | in dbSNP:rs17848169 | |||
Sequence: N → D | ||||||
Natural variant | VAR_005422 | 2872 | in dbSNP:rs2228171 | |||
Sequence: A → T | ||||||
Natural variant | VAR_037014 | 3011 | in dbSNP:rs11674973 | |||
Sequence: R → M | ||||||
Natural variant | VAR_020219 | 3305 | in dbSNP:rs3213760 | |||
Sequence: R → H | ||||||
Natural variant | VAR_075534 | 3779 | found in patients with mild intellectual disability; uncertain significance; dbSNP:rs199583537 | |||
Sequence: D → N | ||||||
Natural variant | VAR_075535 | 3828 | found in patients with a phenotype suggestive of Stickler syndrome; uncertain significance | |||
Sequence: D → G | ||||||
Natural variant | VAR_005423 | 4094 | in dbSNP:rs2075252 | |||
Sequence: K → E | ||||||
Natural variant | VAR_005424 | 4210 | in dbSNP:rs4667591 | |||
Sequence: I → L | ||||||
Natural variant | VAR_035996 | 4272 | in a colorectal cancer sample; somatic mutation | |||
Sequence: M → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 5,372 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-25 | UniProt | |||||
Sequence: MDRGPAAVACTLLLALVACLAPASG | |||||||
Chain | PRO_0000017321 | 26-4655 | UniProt | Low-density lipoprotein receptor-related protein 2 | |||
Sequence: QECDSAHFRCGSGHCIPADWRCDGTKDCSDDADEIGCAVVTCQQGYFKCQSEGQCIPNSWVCDQDQDCDDGSDERQDCSQSTCSSHQITCSNGQCIPSEYRCDHVRDCPDGADENDCQYPTCEQLTCDNGACYNTSQKCDWKVDCRDSSDEINCTEICLHNEFSCGNGECIPRAYVCDHDNDCQDGSDEHACNYPTCGGYQFTCPSGRCIYQNWVCDGEDDCKDNGDEDGCESGPHDVHKCSPREWSCPESGRCISIYKVCDGILDCPGREDENNTSTGKYCSMTLCSALNCQYQCHETPYGGACFCPPGYIINHNDSRTCVEFDDCQIWGICDQKCESRPGRHLCHCEEGYILERGQYCKANDSFGEASIIFSNGRDLLIGDIHGRSFRILVESQNRGVAVGVAFHYHLQRVFWTDTVQNKVFSVDINGLNIQEVLNVSVETPENLAVDWVNNKIYLVETKVNRIDMVNLDGSYRVTLITENLGHPRGIAVDPTVGYLFFSDWESLSGEPKLERAFMDGSNRKDLVKTKLGWPAGVTLDMISKRVYWVDSRFDYIETVTYDGIQRKTVVHGGSLIPHPFGVSLFEGQVFFTDWTKMAVLKANKFTETNPQVYYQASLRPYGVTVYHSLRQPYATNPCKDNNGGCEQVCVLSHRTDNDGLGFRCKCTFGFQLDTDERHCIAVQNFLIFSSQVAIRGIPFTLSTQEDVMVPVSGNPSFFVGIDFDAQDSTIFFSDMSKHMIFKQKIDGTGREILAANRVENVESLAFDWISKNLYWTDSHYKSISVMRLADKTRRTVVQYLNNPRSVVVHPFAGYLFFTDWFRPAKIMRAWSDGSHLLPVINTTLGWPNGLAIDWAASRLYWVDAYFDKIEHSTFDGLDRRRLGHIEQMTHPFGLAIFGEHLFFTDWRLGAIIRVRKADGGEMTVIRSGIAYILHLKSYDVNIQTGSNACNQPTHPNGDCSHFCFPVPNFQRVCGCPYGMRLASNHLTCEGDPTNEPPTEQCGLFSFPCKNGRCVPNYYLCDGVDDCHDNSDEQLCGTLNNTCSSSAFTCGHGECIPAHWRCDKRNDCVDGSDEHNCPTHAPASCLDTQYTCDNHQCISKNWVCDTDNDCGDGSDEKNCNSTETCQPSQFNCPNHRCIDLSFVCDGDKDCVDGSDEVGCVLNCTASQFKCASGDKCIGVTNRCDGVFDCSDNSDEAGCPTRPPGMCHSDEFQCQEDGICIPNFWECDGHPDCLYGSDEHNACVPKTCPSSYFHCDNGNCIHRAWLCDRDNDCGDMSDEKDCPTQPFRCPSWQWQCLGHNICVNLSVVCDGIFDCPNGTDESPLCNGNSCSDFNGGCTHECVQEPFGAKCLCPLGFLLANDSKTCEDIDECDILGSCSQHCYNMRGSFRCSCDTGYMLESDGRTCKVTASESLLLLVASQNKIIADSVTSQVHNIYSLVENGSYIVAVDFDSISGRIFWSDATQGKTWSAFQNGTDRRVVFDSSIILTETIAIDWVGRNLYWTDYALETIEVSKIDGSHRTVLISKNLTNPRGLALDPRMNEHLLFWSDWGHHPRIERASMDGSMRTVIVQDKIFWPCGLTIDYPNRLLYFMDSYLDYMDFCDYNGHHRRQVIASDLIIRHPYALTLFEDSVYWTDRATRRVMRANKWHGGNQSVVMYNIQWPLGIVAVHPSKQPNSVNPCAFSRCSHLCLLSSQGPHFYSCVCPSGWSLSPDLLNCLRDDQPFLITVRQHIIFGISLNPEVKSNDAMVPIAGIQNGLDVEFDDAEQYIYWVENPGEIHRVKTDGTNRTVFASISMVGPSMNLALDWISRNLYSTNPRTQSIEVLTLHGDIRYRKTLIANDGTALGVGFPIGITVDPARGKLYWSDQGTDSGVPAKIASANMDGTSVKTLFTGNLEHLECVTLDIEEQKLYWAVTGRGVIERGNVDGTDRMILVHQLSHPWGIAVHDSFLYYTDEQYEVIERVDKATGANKIVLRDNVPNLRGLQVYHRRNAAESSNGCSNNMNACQQICLPVPGGLFSCACATGFKLNPDNRSCSPYNSFIVVSMLSAIRGFSLELSDHSETMVPVAGQGRNALHVDVDVSSGFIYWCDFSSSVASDNAIRRIKPDGSSLMNIVTHGIGENGVRGIAVDWVAGNLYFTNAFVSETLIEVLRINTTYRRVLLKVTVDMPRHIVVDPKNRYLFWADYGQRPKIERSFLDCTNRTVLVSEGIVTPRGLAVDRSDGYVYWVDDSLDIIARIRINGENSEVIRYGSRYPTPYGITVFENSIIWVDRNLKKIFQASKEPENTEPPTVIRDNINWLRDVTIFDKQVQPRSPAEVNNNPCLENNGGCSHLCFALPGLHTPKCDCAFGTLQSDGKNCAISTENFLIFALSNSLRSLHLDPENHSPPFQTINVERTVMSLDYDSVSDRIYFTQNLASGVGQISYATLSSGIHTPTVIASGIGTADGIAFDWITRRIYYSDYLNQMINSMAEDGSNRTVIARVPKPRAIVLDPCQGYLYWADWDTHAKIERATLGGNFRVPIVNSSLVMPSGLTLDYEEDLLYWVDASLQRIERSTLTGVDREVIVNAAVHAFGLTLYGQYIYWTDLYTQRIYRANKYDGSGQIAMTTNLLSQPRGINTVVKNQKQQCNNPCEQFNGGCSHICAPGPNGAECQCPHEGNWYLANNRKHCIVDNGERCGASSFTCSNGRCISEEWKCDNDNDCGDGSDEMESVCALHTCSPTAFTCANGRCVQYSYRCDYYNDCGDGSDEAGCLFRDCNATTEFMCNNRRCIPREFICNGVDNCHDNNTSDEKNCPDRTCQSGYTKCHNSNICIPRVYLCDGDNDCGDNSDENPTYCTTHTCSSSEFQCASGRCIPQHWYCDQETDCFDASDEPASCGHSERTCLADEFKCDGGRCIPSEWICDGDNDCGDMSDEDKRHQCQNQNCSDSEFLCVNDRPPDRRCIPQSWVCDGDVDCTDGYDENQNCTRRTCSENEFTCGYGLCIPKIFRCDRHNDCGDYSDERGCLYQTCQQNQFTCQNGRCISKTFVCDEDNDCGDGSDELMHLCHTPEPTCPPHEFKCDNGRCIEMMKLCNHLDDCLDNSDEKGCGINECHDPSISGCDHNCTDTLTSFYCSCRPGYKLMSDKRTCVDIDECTEMPFVCSQKCENVIGSYICKCAPGYLREPDGKTCRQNSNIEPYLIFSNRYYLRNLTIDGYFYSLILEGLDNVVALDFDRVEKRLYWIDTQRQVIERMFLNKTNKETIINHRLPAAESLAVDWVSRKLYWLDARLDGLFVSDLNGGHRRMLAQHCVDANNTFCFDNPRGLALHPQYGYLYWADWGHRAYIGRVGMDGTNKSVIISTKLEWPNGITIDYTNDLLYWADAHLGYIEYSDLEGHHRHTVYDGALPHPFAITIFEDTIYWTDWNTRTVEKGNKYDGSNRQTLVNTTHRPFDIHVYHPYRQPIVSNPCGTNNGGCSHLCLIKPGGKGFTCECPDDFRTLQLSGSTYCMPMCSSTQFLCANNEKCIPIWWKCDGQKDCSDGSDELALCPQRFCRLGQFQCSDGNCTSPQTLCNAHQNCPDGSDEDRLLCENHHCDSNEWQCANKRCIPESWQCDTFNDCEDNSDEDSSHCASRTCRPGQFRCANGRCIPQAWKCDVDNDCGDHSDEPIEECMSSAHLCDNFTEFSCKTNYRCIPKWAVCNGVDDCRDNSDEQGCEERTCHPVGDFRCKNHHCIPLRWQCDGQNDCGDNSDEENCAPRECTESEFRCVNQQCIPSRWICDHYNDCGDNSDERDCEMRTCHPEYFQCTSGHCVHSELKCDGSADCLDASDEADCPTRFPDGAYCQATMFECKNHVCIPPYWKCDGDDDCGDGSDEELHLCLDVPCNSPNRFRCDNNRCIYSHEVCNGVDDCGDGTDETEEHCRKPTPKPCTEYEYKCGNGHCIPHDNVCDDADDCGDWSDELGCNKGKERTCAENICEQNCTQLNEGGFICSCTAGFETNVFDRTSCLDINECEQFGTCPQHCRNTKGSYECVCADGFTSMSDRPGKRCAAEGSSPLLLLPDNVRIRKYNLSSERFSEYLQDEEYIQAVDYDWDPKDIGLSVVYYTVRGEGSRFGAIKRAYIPNFESGRNNLVQEVDLKLKYVMQPDGIAVDWVGRHIYWSDVKNKRIEVAKLDGRYRKWLISTDLDQPAAIAVNPKLGLMFWTDWGKEPKIESAWMNGEDRNILVFEDLGWPTGLSIDYLNNDRIYWSDFKEDVIETIKYDGTDRRVIAKEAMNPYSLDIFEDQLYWISKEKGEVWKQNKFGQGKKEKTLVVNPWLTQVRIFHQLRYNKSVPNLCKQICSHLCLLRPGGYSCACPQGSSFIEGSTTECDAAIELPINLPPPCRCMHGGNCYFDETDLPKCKCPSGYTGKYCEMAFSKGISPGTTAVAVLLTILLIVVIGALAIAGFFHYRRTGSLLPALPKLPSLSSLVKPSENGNGVTFRSGADLNMDIGVSGFGPETAIDRSMAMSEDFVMEMGKQPIIFENPMYSARDSAVKVVQPIQVTVSENVDNKNYGSPINPSEIVPETNPTSPAADGTQVTKWNLFKRKSKQTTNFENPIYAQMENEQKESVAATPPPSPSLPAKPKPPSRRDPTPTYSATEDTFKDTANLVKEDSEV | |||||||
Disulfide bond | 28↔40 | UniProt | |||||
Sequence: CDSAHFRCGSGHC | |||||||
Disulfide bond | 35↔53 | UniProt | |||||
Sequence: CGSGHCIPADWRCDGTKDC | |||||||
Disulfide bond | 47↔62 | UniProt | |||||
Sequence: CDGTKDCSDDADEIGC | |||||||
Disulfide bond | 67↔80 | UniProt | |||||
Sequence: CQQGYFKCQSEGQC | |||||||
Disulfide bond | 74↔93 | UniProt | |||||
Sequence: CQSEGQCIPNSWVCDQDQDC | |||||||
Disulfide bond | 87↔103 | UniProt | |||||
Sequence: CDQDQDCDDGSDERQDC | |||||||
Disulfide bond | 108↔120 | UniProt | |||||
Sequence: CSSHQITCSNGQC | |||||||
Disulfide bond | 115↔133 | UniProt | |||||
Sequence: CSNGQCIPSEYRCDHVRDC | |||||||
Disulfide bond | 127↔142 | UniProt | |||||
Sequence: CDHVRDCPDGADENDC | |||||||
Disulfide bond | 147↔157 | UniProt | |||||
Sequence: CEQLTCDNGAC | |||||||
Disulfide bond | 152↔170 | UniProt | |||||
Sequence: CDNGACYNTSQKCDWKVDC | |||||||
Glycosylation | 159 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 164↔179 | UniProt | |||||
Sequence: CDWKVDCRDSSDEINC | |||||||
Glycosylation | 178 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 183↔195 | UniProt | |||||
Sequence: CLHNEFSCGNGEC | |||||||
Disulfide bond | 190↔208 | UniProt | |||||
Sequence: CGNGECIPRAYVCDHDNDC | |||||||
Disulfide bond | 202↔217 | UniProt | |||||
Sequence: CDHDNDCQDGSDEHAC | |||||||
Disulfide bond | 222↔234 | UniProt | |||||
Sequence: CGGYQFTCPSGRC | |||||||
Disulfide bond | 229↔247 | UniProt | |||||
Sequence: CPSGRCIYQNWVCDGEDDC | |||||||
Disulfide bond | 241↔256 | UniProt | |||||
Sequence: CDGEDDCKDNGDEDGC | |||||||
Disulfide bond | 266↔279 | UniProt | |||||
Sequence: CSPREWSCPESGRC | |||||||
Disulfide bond | 273↔292 | UniProt | |||||
Sequence: CPESGRCISIYKVCDGILDC | |||||||
Disulfide bond | 286↔307 | UniProt | |||||
Sequence: CDGILDCPGREDENNTSTGKYC | |||||||
Glycosylation | 299 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 300 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 341 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 388 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 463 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 866 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 1026↔1038 | UniProt | |||||
Sequence: CGLFSFPCKNGRC | |||||||
Disulfide bond | 1033↔1051 | UniProt | |||||
Sequence: CKNGRCVPNYYLCDGVDDC | |||||||
Disulfide bond | 1045↔1060 | UniProt | |||||
Sequence: CDGVDDCHDNSDEQLC | |||||||
Glycosylation | 1064 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 1067↔1079 | UniProt | |||||
Sequence: CSSSAFTCGHGEC | |||||||
Disulfide bond | 1074↔1092 | UniProt | |||||
Sequence: CGHGECIPAHWRCDKRNDC | |||||||
Disulfide bond | 1086↔1101 | UniProt | |||||
Sequence: CDKRNDCVDGSDEHNC | |||||||
Disulfide bond | 1109↔1121 | UniProt | |||||
Sequence: CLDTQYTCDNHQC | |||||||
Disulfide bond | 1116↔1134 | UniProt | |||||
Sequence: CDNHQCISKNWVCDTDNDC | |||||||
Disulfide bond | 1128↔1143 | UniProt | |||||
Sequence: CDTDNDCGDGSDEKNC | |||||||
Glycosylation | 1144 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 1149↔1161 | UniProt | |||||
Sequence: CQPSQFNCPNHRC | |||||||
Disulfide bond | 1156↔1174 | UniProt | |||||
Sequence: CPNHRCIDLSFVCDGDKDC | |||||||
Disulfide bond | 1168↔1183 | UniProt | |||||
Sequence: CDGDKDCVDGSDEVGC | |||||||
Glycosylation | 1186 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 1187↔1200 | UniProt | |||||
Sequence: CTASQFKCASGDKC | |||||||
Disulfide bond | 1194↔1213 | UniProt | |||||
Sequence: CASGDKCIGVTNRCDGVFDC | |||||||
Disulfide bond | 1207↔1222 | UniProt | |||||
Sequence: CDGVFDCSDNSDEAGC | |||||||
Disulfide bond | 1230↔1243 | UniProt | |||||
Sequence: CHSDEFQCQEDGIC | |||||||
Disulfide bond | 1237↔1256 | UniProt | |||||
Sequence: CQEDGICIPNFWECDGHPDC | |||||||
Disulfide bond | 1250↔1266 | UniProt | |||||
Sequence: CDGHPDCLYGSDEHNAC | |||||||
Disulfide bond | 1271↔1283 | UniProt | |||||
Sequence: CPSSYFHCDNGNC | |||||||
Disulfide bond | 1278↔1296 | UniProt | |||||
Sequence: CDNGNCIHRAWLCDRDNDC | |||||||
Disulfide bond | 1290↔1305 | UniProt | |||||
Sequence: CDRDNDCGDMSDEKDC | |||||||
Disulfide bond | 1305↔1325 | UniProt | |||||
Sequence: CPTQPFRCPSWQWQCLGHNIC | |||||||
Disulfide bond | 1312↔1338 | UniProt | |||||
Sequence: CPSWQWQCLGHNICVNLSVVCDGIFDC | |||||||
Glycosylation | 1327 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 1332↔1348 | UniProt | |||||
Sequence: CDGIFDCPNGTDESPLC | |||||||
Glycosylation | 1340 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 1383 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 1394↔1404 | UniProt | |||||
Sequence: CDILGSCSQHC | |||||||
Disulfide bond | 1400↔1413 | UniProt | |||||
Sequence: CSQHCYNMRGSFRC | |||||||
Disulfide bond | 1415↔1428 | UniProt | |||||
Sequence: CDTGYMLESDGRTC | |||||||
Glycosylation | 1464 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 1496 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 1550 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 1675 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 1704↔1713 | UniProt | |||||
Sequence: CAFSRCSHLC | |||||||
Disulfide bond | 1709↔1725 | UniProt | |||||
Sequence: CSHLCLLSSQGPHFYSC | |||||||
Disulfide bond | 1727↔1740 | UniProt | |||||
Sequence: CPSGWSLSPDLLNC | |||||||
Glycosylation | 1810 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 2055 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 2177 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 2224 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 2499 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 2547 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 2700↔2712 | UniProt | |||||
Sequence: CGASSFTCSNGRC | |||||||
Disulfide bond | 2707↔2725 | UniProt | |||||
Sequence: CSNGRCISEEWKCDNDNDC | |||||||
Disulfide bond | 2719↔2736 | UniProt | |||||
Sequence: CDNDNDCGDGSDEMESVC | |||||||
Disulfide bond | 2741↔2753 | UniProt | |||||
Sequence: CSPTAFTCANGRC | |||||||
Disulfide bond | 2748↔2766 | UniProt | |||||
Sequence: CANGRCVQYSYRCDYYNDC | |||||||
Disulfide bond | 2760↔2775 | UniProt | |||||
Sequence: CDYYNDCGDGSDEAGC | |||||||
Disulfide bond | 2780↔2793 | UniProt | |||||
Sequence: CNATTEFMCNNRRC | |||||||
Glycosylation | 2781 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 2788↔2806 | UniProt | |||||
Sequence: CNNRRCIPREFICNGVDNC | |||||||
Disulfide bond | 2800↔2817 | UniProt | |||||
Sequence: CNGVDNCHDNNTSDEKNC | |||||||
Glycosylation | 2809 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 2810 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 2822↔2835 | UniProt | |||||
Sequence: CQSGYTKCHNSNIC | |||||||
Disulfide bond | 2829↔2848 | UniProt | |||||
Sequence: CHNSNICIPRVYLCDGDNDC | |||||||
Disulfide bond | 2842↔2859 | UniProt | |||||
Sequence: CDGDNDCGDNSDENPTYC | |||||||
Disulfide bond | 2864↔2876 | UniProt | |||||
Sequence: CSSSEFQCASGRC | |||||||
Disulfide bond | 2871↔2889 | UniProt | |||||
Sequence: CASGRCIPQHWYCDQETDC | |||||||
Disulfide bond | 2883↔2899 | UniProt | |||||
Sequence: CDQETDCFDASDEPASC | |||||||
Disulfide bond | 2906↔2918 | UniProt | |||||
Sequence: CLADEFKCDGGRC | |||||||
Disulfide bond | 2913↔2931 | UniProt | |||||
Sequence: CDGGRCIPSEWICDGDNDC | |||||||
Disulfide bond | 2925↔2943 | UniProt | |||||
Sequence: CDGDNDCGDMSDEDKRHQC | |||||||
Glycosylation | 2947 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 2948↔2965 | UniProt | |||||
Sequence: CSDSEFLCVNDRPPDRRC | |||||||
Disulfide bond | 2955↔2978 | UniProt | |||||
Sequence: CVNDRPPDRRCIPQSWVCDGDVDC | |||||||
Disulfide bond | 2972↔2988 | UniProt | |||||
Sequence: CDGDVDCTDGYDENQNC | |||||||
Glycosylation | 2987 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 2993↔3005 | UniProt | |||||
Sequence: CSENEFTCGYGLC | |||||||
Disulfide bond | 3000↔3018 | UniProt | |||||
Sequence: CGYGLCIPKIFRCDRHNDC | |||||||
Disulfide bond | 3012↔3027 | UniProt | |||||
Sequence: CDRHNDCGDYSDERGC | |||||||
Disulfide bond | 3032↔3044 | UniProt | |||||
Sequence: CQQNQFTCQNGRC | |||||||
Disulfide bond | 3039↔3057 | UniProt | |||||
Sequence: CQNGRCISKTFVCDEDNDC | |||||||
Disulfide bond | 3051↔3068 | UniProt | |||||
Sequence: CDEDNDCGDGSDELMHLC | |||||||
Disulfide bond | 3075↔3087 | UniProt | |||||
Sequence: CPPHEFKCDNGRC | |||||||
Disulfide bond | 3082↔3100 | UniProt | |||||
Sequence: CDNGRCIEMMKLCNHLDDC | |||||||
Disulfide bond | 3094↔3109 | UniProt | |||||
Sequence: CNHLDDCLDNSDEKGC | |||||||
Disulfide bond | 3114↔3126 | UniProt | |||||
Sequence: CHDPSISGCDHNC | |||||||
Disulfide bond | 3122↔3135 | UniProt | |||||
Sequence: CDHNCTDTLTSFYC | |||||||
Glycosylation | 3125 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 3137↔3150 | UniProt | |||||
Sequence: CRPGYKLMSDKRTC | |||||||
Disulfide bond | 3156↔3167 | UniProt | |||||
Sequence: CTEMPFVCSQKC | |||||||
Disulfide bond | 3163↔3176 | UniProt | |||||
Sequence: CSQKCENVIGSYIC | |||||||
Disulfide bond | 3178↔3191 | UniProt | |||||
Sequence: CAPGYLREPDGKTC | |||||||
Glycosylation | 3211 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 3257 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 3315 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 3355 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 3446 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 3512↔3525 | UniProt | |||||
Sequence: CSSTQFLCANNEKC | |||||||
Disulfide bond | 3519↔3538 | UniProt | |||||
Sequence: CANNEKCIPIWWKCDGQKDC | |||||||
Disulfide bond | 3532↔3548 | UniProt | |||||
Sequence: CDGQKDCSDGSDELALC | |||||||
Disulfide bond | 3553↔3565 | UniProt | |||||
Sequence: CRLGQFQCSDGNC | |||||||
Disulfide bond | 3560↔3578 | UniProt | |||||
Sequence: CSDGNCTSPQTLCNAHQNC | |||||||
Glycosylation | 3564 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 3572↔3589 | UniProt | |||||
Sequence: CNAHQNCPDGSDEDRLLC | |||||||
Disulfide bond | 3594↔3606 | UniProt | |||||
Sequence: CDSNEWQCANKRC | |||||||
Disulfide bond | 3601↔3619 | UniProt | |||||
Sequence: CANKRCIPESWQCDTFNDC | |||||||
Disulfide bond | 3613↔3630 | UniProt | |||||
Sequence: CDTFNDCEDNSDEDSSHC | |||||||
Disulfide bond | 3635↔3647 | UniProt | |||||
Sequence: CRPGQFRCANGRC | |||||||
Disulfide bond | 3642↔3660 | UniProt | |||||
Sequence: CANGRCIPQAWKCDVDNDC | |||||||
Disulfide bond | 3654↔3671 | UniProt | |||||
Sequence: CDVDNDCGDHSDEPIEEC | |||||||
Disulfide bond | 3678↔3692 | UniProt | |||||
Sequence: CDNFTEFSCKTNYRC | |||||||
Glycosylation | 3680 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 3686↔3705 | UniProt | |||||
Sequence: CKTNYRCIPKWAVCNGVDDC | |||||||
Disulfide bond | 3699↔3714 | UniProt | |||||
Sequence: CNGVDDCRDNSDEQGC | |||||||
Disulfide bond | 3719↔3732 | UniProt | |||||
Sequence: CHPVGDFRCKNHHC | |||||||
Disulfide bond | 3727↔3745 | UniProt | |||||
Sequence: CKNHHCIPLRWQCDGQNDC | |||||||
Disulfide bond | 3739↔3754 | UniProt | |||||
Sequence: CDGQNDCGDNSDEENC | |||||||
Disulfide bond | 3759↔3771 | UniProt | |||||
Sequence: CTESEFRCVNQQC | |||||||
Disulfide bond | 3766↔3784 | UniProt | |||||
Sequence: CVNQQCIPSRWICDHYNDC | |||||||
Disulfide bond | 3778↔3793 | UniProt | |||||
Sequence: CDHYNDCGDNSDERDC | |||||||
Disulfide bond | 3798↔3810 | UniProt | |||||
Sequence: CHPEYFQCTSGHC | |||||||
Disulfide bond | 3805↔3823 | UniProt | |||||
Sequence: CTSGHCVHSELKCDGSADC | |||||||
Disulfide bond | 3817↔3832 | UniProt | |||||
Sequence: CDGSADCLDASDEADC | |||||||
Disulfide bond | 3842↔3854 | UniProt | |||||
Sequence: CQATMFECKNHVC | |||||||
Disulfide bond | 3849↔3867 | UniProt | |||||
Sequence: CKNHVCIPPYWKCDGDDDC | |||||||
Disulfide bond | 3861↔3878 | UniProt | |||||
Sequence: CDGDDDCGDGSDEELHLC | |||||||
Disulfide bond | 3883↔3896 | UniProt | |||||
Sequence: CNSPNRFRCDNNRC | |||||||
Disulfide bond | 3891↔3909 | UniProt | |||||
Sequence: CDNNRCIYSHEVCNGVDDC | |||||||
Disulfide bond | 3903↔3920 | UniProt | |||||
Sequence: CNGVDDCGDGTDETEEHC | |||||||
Disulfide bond | 3928↔3940 | UniProt | |||||
Sequence: CTEYEYKCGNGHC | |||||||
Disulfide bond | 3935↔3953 | UniProt | |||||
Sequence: CGNGHCIPHDNVCDDADDC | |||||||
Disulfide bond | 3947↔3962 | UniProt | |||||
Sequence: CDDADDCGDWSDELGC | |||||||
Glycosylation | 3978 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 4011↔4021 | UniProt | |||||
Sequence: CEQFGTCPQHC | |||||||
Disulfide bond | 4017↔4030 | UniProt | |||||
Sequence: CPQHCRNTKGSYEC | |||||||
Disulfide bond | 4032↔4047 | UniProt | |||||
Sequence: CADGFTSMSDRPGKRC | |||||||
Glycosylation | 4068 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 4327 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 4381↔4389 | UniProt | |||||
Sequence: CRCMHGGNC | |||||||
Disulfide bond | 4383↔4399 | UniProt | |||||
Sequence: CMHGGNCYFDETDLPKC | |||||||
Disulfide bond | 4401↔4410 | UniProt | |||||
Sequence: CPSGYTGKYC | |||||||
Modified residue | 4463 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 4466 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 4569 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 4569 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 4612 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 4616 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 4616 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 4632 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 4653 | UniProt | Phosphoserine | ||||
Sequence: S |
Post-translational modification
A fraction undergoes proteolytic cleavage of the extracellular domain at the cell membrane to generate a cytoplasmic tail fragment. This is internalized into the early endosome from where it trafficks in an LDLRAP1/ARH-dependent manner to the endocytic recycling compartment (ERC). In the ERC, it is further cleaved by gamma-secretase to release a fragment which translocates to the nucleus and mediates transcriptional repression.
N-glycosylation is required for ligand binding.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in first and third trimester cytotrophoblasts in the placenta (at protein level) (PubMed:27798286).
Absorptive epithelia, including renal proximal tubules
Absorptive epithelia, including renal proximal tubules
Developmental stage
Expression in the choroid plexus of the brain is markedly reduced in aging subjects when compared with younger adults.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Binds plasminogen, extracellular matrix components, plasminogen activator-plasminogen activator inhibitor type I complex, apolipoprotein E-enriched beta-VLDL, lipoprotein lipase, lactoferrin, CLU/clusterin and calcium (PubMed:7768901).
Forms a multimeric complex together with LRPAP1 (PubMed:1400426).
Interacts (via PxLPxI/L motif) with ANKRA2 (via ankyrin repeats) (By similarity).
Interacts with LRP2BP (PubMed:12508107).
Interacts (via NPXY motif) with DAB2; the interaction is not affected by tyrosine phosphorylation of the NPXY motif (PubMed:10769163, PubMed:15134832).
Interacts with MB (By similarity).
Interacts with BMP4 (By similarity).
Interacts with the Sonic hedgehog protein N-product which is the active product of SHH (By similarity).
Interacts with CST3 in a calcium-dependent manner (PubMed:17462596).
Interacts with the vitamin-D binding protein GC/DBP (By similarity).
Interacts with sex hormone-binding protein SHBG (PubMed:16143106).
Interacts with angiotensin-2 (By similarity).
Also interacts with angiotensin 1-7 (By similarity).
Interacts with APOM (By similarity).
Interacts with selenoprotein SEPP1 (By similarity).
Interacts with LEP (By similarity).
Interacts with ALB (By similarity).
Interacts with the antiapoptotic protein BIRC5/survivin (PubMed:23825075).
Interacts with matrix metalloproteinase MMP2 in complex with metalloproteinase inhibitor TIMP1 (By similarity).
In neurons, forms a trimeric complex with APP and APPB1/FE65 (By similarity).
Interacts with LDLRAP1/ARH; mediates trafficking of LRP2 to the endocytic recycling compartment (By similarity).
Does not interact with beta-amyloid protein 40 alone but interacts with the complex composed of beta-amyloid protein 40 and CLU/APOJ (By similarity).
Interacts with MDK (By similarity).
Forms a multimeric complex together with LRPAP1 (PubMed:1400426).
Interacts (via PxLPxI/L motif) with ANKRA2 (via ankyrin repeats) (By similarity).
Interacts with LRP2BP (PubMed:12508107).
Interacts (via NPXY motif) with DAB2; the interaction is not affected by tyrosine phosphorylation of the NPXY motif (PubMed:10769163, PubMed:15134832).
Interacts with MB (By similarity).
Interacts with BMP4 (By similarity).
Interacts with the Sonic hedgehog protein N-product which is the active product of SHH (By similarity).
Interacts with CST3 in a calcium-dependent manner (PubMed:17462596).
Interacts with the vitamin-D binding protein GC/DBP (By similarity).
Interacts with sex hormone-binding protein SHBG (PubMed:16143106).
Interacts with angiotensin-2 (By similarity).
Also interacts with angiotensin 1-7 (By similarity).
Interacts with APOM (By similarity).
Interacts with selenoprotein SEPP1 (By similarity).
Interacts with LEP (By similarity).
Interacts with ALB (By similarity).
Interacts with the antiapoptotic protein BIRC5/survivin (PubMed:23825075).
Interacts with matrix metalloproteinase MMP2 in complex with metalloproteinase inhibitor TIMP1 (By similarity).
In neurons, forms a trimeric complex with APP and APPB1/FE65 (By similarity).
Interacts with LDLRAP1/ARH; mediates trafficking of LRP2 to the endocytic recycling compartment (By similarity).
Does not interact with beta-amyloid protein 40 alone but interacts with the complex composed of beta-amyloid protein 40 and CLU/APOJ (By similarity).
Interacts with MDK (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P98164 | RIBC2 Q9H4K1 | 2 | EBI-947916, EBI-740128 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, repeat, motif, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 27-63 | LDL-receptor class A 1 | ||||
Sequence: ECDSAHFRCGSGHCIPADWRCDGTKDCSDDADEIGCA | ||||||
Domain | 66-104 | LDL-receptor class A 2 | ||||
Sequence: TCQQGYFKCQSEGQCIPNSWVCDQDQDCDDGSDERQDCS | ||||||
Domain | 107-143 | LDL-receptor class A 3 | ||||
Sequence: TCSSHQITCSNGQCIPSEYRCDHVRDCPDGADENDCQ | ||||||
Domain | 146-180 | LDL-receptor class A 4 | ||||
Sequence: TCEQLTCDNGACYNTSQKCDWKVDCRDSSDEINCT | ||||||
Domain | 182-218 | LDL-receptor class A 5 | ||||
Sequence: ICLHNEFSCGNGECIPRAYVCDHDNDCQDGSDEHACN | ||||||
Domain | 221-257 | LDL-receptor class A 6 | ||||
Sequence: TCGGYQFTCPSGRCIYQNWVCDGEDDCKDNGDEDGCE | ||||||
Domain | 265-308 | LDL-receptor class A 7 | ||||
Sequence: KCSPREWSCPESGRCISIYKVCDGILDCPGREDENNTSTGKYCS | ||||||
Repeat | 436-478 | LDL-receptor class B 1 | ||||
Sequence: QRVFWTDTVQNKVFSVDINGLNIQEVLNVSVETPENLAVDWVN | ||||||
Repeat | 479-521 | LDL-receptor class B 2 | ||||
Sequence: NKIYLVETKVNRIDMVNLDGSYRVTLITENLGHPRGIAVDPTV | ||||||
Repeat | 522-568 | LDL-receptor class B 3 | ||||
Sequence: GYLFFSDWESLSGEPKLERAFMDGSNRKDLVKTKLGWPAGVTLDMIS | ||||||
Repeat | 569-613 | LDL-receptor class B 4 | ||||
Sequence: KRVYWVDSRFDYIETVTYDGIQRKTVVHGGSLIPHPFGVSLFEGQ | ||||||
Repeat | 753-795 | LDL-receptor class B 5 | ||||
Sequence: STIFFSDMSKHMIFKQKIDGTGREILAANRVENVESLAFDWIS | ||||||
Repeat | 796-837 | LDL-receptor class B 6 | ||||
Sequence: KNLYWTDSHYKSISVMRLADKTRRTVVQYLNNPRSVVVHPFA | ||||||
Repeat | 838-881 | LDL-receptor class B 7 | ||||
Sequence: GYLFFTDWFRPAKIMRAWSDGSHLLPVINTTLGWPNGLAIDWAA | ||||||
Repeat | 882-925 | LDL-receptor class B 8 | ||||
Sequence: SRLYWVDAYFDKIEHSTFDGLDRRRLGHIEQMTHPFGLAIFGEH | ||||||
Domain | 1025-1061 | LDL-receptor class A 8 | ||||
Sequence: QCGLFSFPCKNGRCVPNYYLCDGVDDCHDNSDEQLCG | ||||||
Domain | 1066-1102 | LDL-receptor class A 9 | ||||
Sequence: TCSSSAFTCGHGECIPAHWRCDKRNDCVDGSDEHNCP | ||||||
Domain | 1108-1144 | LDL-receptor class A 10 | ||||
Sequence: SCLDTQYTCDNHQCISKNWVCDTDNDCGDGSDEKNCN | ||||||
Domain | 1148-1184 | LDL-receptor class A 11 | ||||
Sequence: TCQPSQFNCPNHRCIDLSFVCDGDKDCVDGSDEVGCV | ||||||
Domain | 1186-1223 | LDL-receptor class A 12 | ||||
Sequence: NCTASQFKCASGDKCIGVTNRCDGVFDCSDNSDEAGCP | ||||||
Domain | 1229-1267 | LDL-receptor class A 13 | ||||
Sequence: MCHSDEFQCQEDGICIPNFWECDGHPDCLYGSDEHNACV | ||||||
Domain | 1270-1306 | LDL-receptor class A 14 | ||||
Sequence: TCPSSYFHCDNGNCIHRAWLCDRDNDCGDMSDEKDCP | ||||||
Domain | 1304-1349 | LDL-receptor class A 15 | ||||
Sequence: DCPTQPFRCPSWQWQCLGHNICVNLSVVCDGIFDCPNGTDESPLCN | ||||||
Domain | 1390-1429 | EGF-like 1; calcium-binding | ||||
Sequence: DIDECDILGSCSQHCYNMRGSFRCSCDTGYMLESDGRTCK | ||||||
Repeat | 1478-1520 | LDL-receptor class B 9 | ||||
Sequence: GRIFWSDATQGKTWSAFQNGTDRRVVFDSSIILTETIAIDWVG | ||||||
Repeat | 1521-1563 | LDL-receptor class B 10 | ||||
Sequence: RNLYWTDYALETIEVSKIDGSHRTVLISKNLTNPRGLALDPRM | ||||||
Repeat | 1566-1609 | LDL-receptor class B 11 | ||||
Sequence: HLLFWSDWGHHPRIERASMDGSMRTVIVQDKIFWPCGLTIDYPN | ||||||
Repeat | 1610-1654 | LDL-receptor class B 12 | ||||
Sequence: RLLYFMDSYLDYMDFCDYNGHHRRQVIASDLIIRHPYALTLFEDS | ||||||
Repeat | 1655-1695 | LDL-receptor class B 13 | ||||
Sequence: VYWTDRATRRVMRANKWHGGNQSVVMYNIQWPLGIVAVHPS | ||||||
Domain | 1700-1741 | EGF-like 2 | ||||
Sequence: SVNPCAFSRCSHLCLLSSQGPHFYSCVCPSGWSLSPDLLNCL | ||||||
Repeat | 1790-1832 | LDL-receptor class B 14 | ||||
Sequence: QYIYWVENPGEIHRVKTDGTNRTVFASISMVGPSMNLALDWIS | ||||||
Repeat | 1833-1882 | LDL-receptor class B 15 | ||||
Sequence: RNLYSTNPRTQSIEVLTLHGDIRYRKTLIANDGTALGVGFPIGITVDPAR | ||||||
Repeat | 1883-1930 | LDL-receptor class B 16 | ||||
Sequence: GKLYWSDQGTDSGVPAKIASANMDGTSVKTLFTGNLEHLECVTLDIEE | ||||||
Repeat | 1931-1972 | LDL-receptor class B 17 | ||||
Sequence: QKLYWAVTGRGVIERGNVDGTDRMILVHQLSHPWGIAVHDSF | ||||||
Repeat | 1973-2013 | LDL-receptor class B 18 | ||||
Sequence: LYYTDEQYEVIERVDKATGANKIVLRDNVPNLRGLQVYHRR | ||||||
Repeat | 2107-2156 | LDL-receptor class B 19 | ||||
Sequence: GFIYWCDFSSSVASDNAIRRIKPDGSSLMNIVTHGIGENGVRGIAVDWVA | ||||||
Repeat | 2157-2201 | LDL-receptor class B 20 | ||||
Sequence: GNLYFTNAFVSETLIEVLRINTTYRRVLLKVTVDMPRHIVVDPKN | ||||||
Repeat | 2202-2245 | LDL-receptor class B 21 | ||||
Sequence: RYLFWADYGQRPKIERSFLDCTNRTVLVSEGIVTPRGLAVDRSD | ||||||
Repeat | 2246-2289 | LDL-receptor class B 22 | ||||
Sequence: GYVYWVDDSLDIIARIRINGENSEVIRYGSRYPTPYGITVFENS | ||||||
Repeat | 2431-2477 | LDL-receptor class B 23 | ||||
Sequence: DRIYFTQNLASGVGQISYATLSSGIHTPTVIASGIGTADGIAFDWIT | ||||||
Repeat | 2478-2518 | LDL-receptor class B 24 | ||||
Sequence: RRIYYSDYLNQMINSMAEDGSNRTVIARVPKPRAIVLDPCQ | ||||||
Repeat | 2519-2562 | LDL-receptor class B 25 | ||||
Sequence: GYLYWADWDTHAKIERATLGGNFRVPIVNSSLVMPSGLTLDYEE | ||||||
Repeat | 2563-2604 | LDL-receptor class B 26 | ||||
Sequence: DLLYWVDASLQRIERSTLTGVDREVIVNAAVHAFGLTLYGQY | ||||||
Repeat | 2605-2646 | LDL-receptor class B 27 | ||||
Sequence: IYWTDLYTQRIYRANKYDGSGQIAMTTNLLSQPRGINTVVKN | ||||||
Domain | 2699-2737 | LDL-receptor class A 16 | ||||
Sequence: RCGASSFTCSNGRCISEEWKCDNDNDCGDGSDEMESVCA | ||||||
Domain | 2740-2776 | LDL-receptor class A 17 | ||||
Sequence: TCSPTAFTCANGRCVQYSYRCDYYNDCGDGSDEAGCL | ||||||
Domain | 2779-2818 | LDL-receptor class A 18 | ||||
Sequence: DCNATTEFMCNNRRCIPREFICNGVDNCHDNNTSDEKNCP | ||||||
Domain | 2821-2860 | LDL-receptor class A 19 | ||||
Sequence: TCQSGYTKCHNSNICIPRVYLCDGDNDCGDNSDENPTYCT | ||||||
Domain | 2863-2900 | LDL-receptor class A 20 | ||||
Sequence: TCSSSEFQCASGRCIPQHWYCDQETDCFDASDEPASCG | ||||||
Domain | 2905-2944 | LDL-receptor class A 21 | ||||
Sequence: TCLADEFKCDGGRCIPSEWICDGDNDCGDMSDEDKRHQCQ | ||||||
Domain | 2947-2989 | LDL-receptor class A 22 | ||||
Sequence: NCSDSEFLCVNDRPPDRRCIPQSWVCDGDVDCTDGYDENQNCT | ||||||
Domain | 2992-3028 | LDL-receptor class A 23 | ||||
Sequence: TCSENEFTCGYGLCIPKIFRCDRHNDCGDYSDERGCL | ||||||
Domain | 3031-3069 | LDL-receptor class A 24 | ||||
Sequence: TCQQNQFTCQNGRCISKTFVCDEDNDCGDGSDELMHLCH | ||||||
Domain | 3074-3110 | LDL-receptor class A 25 | ||||
Sequence: TCPPHEFKCDNGRCIEMMKLCNHLDDCLDNSDEKGCG | ||||||
Domain | 3110-3151 | EGF-like 3 | ||||
Sequence: GINECHDPSISGCDHNCTDTLTSFYCSCRPGYKLMSDKRTCV | ||||||
Domain | 3152-3192 | EGF-like 4; calcium-binding | ||||
Sequence: DIDECTEMPFVCSQKCENVIGSYICKCAPGYLREPDGKTCR | ||||||
Repeat | 3239-3281 | LDL-receptor class B 28 | ||||
Sequence: KRLYWIDTQRQVIERMFLNKTNKETIINHRLPAAESLAVDWVS | ||||||
Repeat | 3282-3324 | LDL-receptor class B 29 | ||||
Sequence: RKLYWLDARLDGLFVSDLNGGHRRMLAQHCVDANNTFCFDNPR | ||||||
Repeat | 3333-3376 | LDL-receptor class B 30 | ||||
Sequence: GYLYWADWGHRAYIGRVGMDGTNKSVIISTKLEWPNGITIDYTN | ||||||
Repeat | 3377-3419 | LDL-receptor class B 31 | ||||
Sequence: DLLYWADAHLGYIEYSDLEGHHRHTVYDGALPHPFAITIFEDT | ||||||
Repeat | 3420-3460 | LDL-receptor class B 32 | ||||
Sequence: IYWTDWNTRTVEKGNKYDGSNRQTLVNTTHRPFDIHVYHPY | ||||||
Domain | 3511-3549 | LDL-receptor class A 26 | ||||
Sequence: MCSSTQFLCANNEKCIPIWWKCDGQKDCSDGSDELALCP | ||||||
Domain | 3552-3590 | LDL-receptor class A 27 | ||||
Sequence: FCRLGQFQCSDGNCTSPQTLCNAHQNCPDGSDEDRLLCE | ||||||
Domain | 3593-3631 | LDL-receptor class A 28 | ||||
Sequence: HCDSNEWQCANKRCIPESWQCDTFNDCEDNSDEDSSHCA | ||||||
Domain | 3634-3672 | LDL-receptor class A 29 | ||||
Sequence: TCRPGQFRCANGRCIPQAWKCDVDNDCGDHSDEPIEECM | ||||||
Domain | 3677-3715 | LDL-receptor class A 30 | ||||
Sequence: LCDNFTEFSCKTNYRCIPKWAVCNGVDDCRDNSDEQGCE | ||||||
Domain | 3718-3755 | LDL-receptor class A 31 | ||||
Sequence: TCHPVGDFRCKNHHCIPLRWQCDGQNDCGDNSDEENCA | ||||||
Domain | 3758-3794 | LDL-receptor class A 32 | ||||
Sequence: ECTESEFRCVNQQCIPSRWICDHYNDCGDNSDERDCE | ||||||
Domain | 3797-3833 | LDL-receptor class A 33 | ||||
Sequence: TCHPEYFQCTSGHCVHSELKCDGSADCLDASDEADCP | ||||||
Domain | 3841-3879 | LDL-receptor class A 34 | ||||
Sequence: YCQATMFECKNHVCIPPYWKCDGDDDCGDGSDEELHLCL | ||||||
Domain | 3882-3921 | LDL-receptor class A 35 | ||||
Sequence: PCNSPNRFRCDNNRCIYSHEVCNGVDDCGDGTDETEEHCR | ||||||
Domain | 3927-3963 | LDL-receptor class A 36 | ||||
Sequence: PCTEYEYKCGNGHCIPHDNVCDDADDCGDWSDELGCN | ||||||
Domain | 4007-4048 | EGF-like 5; calcium-binding | ||||
Sequence: DINECEQFGTCPQHCRNTKGSYECVCADGFTSMSDRPGKRCA | ||||||
Repeat | 4154-4196 | LDL-receptor class B 33 | ||||
Sequence: RHIYWSDVKNKRIEVAKLDGRYRKWLISTDLDQPAAIAVNPKL | ||||||
Repeat | 4197-4240 | LDL-receptor class B 34 | ||||
Sequence: GLMFWTDWGKEPKIESAWMNGEDRNILVFEDLGWPTGLSIDYLN | ||||||
Repeat | 4242-4283 | LDL-receptor class B 35 | ||||
Sequence: DRIYWSDFKEDVIETIKYDGTDRRVIAKEAMNPYSLDIFEDQ | ||||||
Domain | 4377-4411 | EGF-like 6 | ||||
Sequence: LPPPCRCMHGGNCYFDETDLPKCKCPSGYTGKYCE | ||||||
Motif | 4453-4462 | SH3-binding | ||||
Sequence: SLLPALPKLP | ||||||
Motif | 4456-4461 | PxLPxI/L motif 1; mediates interaction with ANKRA2 | ||||
Sequence: PALPKL | ||||||
Motif | 4459-4464 | PxLPxI/L motif 2; mediates interaction with ANKRA2 | ||||
Sequence: PKLPSL | ||||||
Motif | 4521-4526 | Endocytosis signal | ||||
Sequence: FENPMY | ||||||
Region | 4550-4574 | Disordered | ||||
Sequence: KNYGSPINPSEIVPETNPTSPAADG | ||||||
Region | 4589-4602 | Interaction with DAB2 | ||||
Sequence: QTTNFENPIYAQME | ||||||
Motif | 4595-4598 | NPXY motif | ||||
Sequence: NPIY | ||||||
Motif | 4598-4601 | SH2-binding | ||||
Sequence: YAQM | ||||||
Region | 4601-4655 | Disordered | ||||
Sequence: MENEQKESVAATPPPSPSLPAKPKPPSRRDPTPTYSATEDTFKDTANLVKEDSEV | ||||||
Motif | 4611-4622 | SH3-binding | ||||
Sequence: ATPPPSPSLPAK | ||||||
Compositional bias | 4613-4630 | Pro residues | ||||
Sequence: PPPSPSLPAKPKPPSRRD |
Domain
Two overlapping PxLPxI/L motifs mediate interaction with ankyrin repeats of ANKRA2.
The cytoplasmic domain is required for sorting to the apical cell membrane.
Sequence similarities
Belongs to the LDLR family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length4,655
- Mass (Da)521,958
- Last updated2007-11-13 v3
- ChecksumC73C4206B8B28CE0
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E9PC35 | E9PC35_HUMAN | LRP2 | 1225 | ||
A0A3B3IRR0 | A0A3B3IRR0_HUMAN | LRP2 | 438 | ||
A0A3B3IT64 | A0A3B3IT64_HUMAN | LRP2 | 1361 |
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 2724 | in Ref. 3; AAB02882 | ||||
Sequence: D → G | ||||||
Sequence conflict | 2773 | in Ref. 3; AAB02882 | ||||
Sequence: A → T | ||||||
Sequence conflict | 2827 | in Ref. 3; AAB02882 | ||||
Sequence: T → P | ||||||
Sequence conflict | 2880-2882 | in Ref. 3; AAB02882 | ||||
Sequence: HWY → TFGI | ||||||
Sequence conflict | 2897 | in Ref. 3; AAB02882 | ||||
Sequence: A → S | ||||||
Sequence conflict | 2908 | in Ref. 3; AAB02882 | ||||
Sequence: A → S | ||||||
Sequence conflict | 2921 | in Ref. 3; AAB02882 | ||||
Sequence: S → N | ||||||
Sequence conflict | 2954 | in Ref. 3; AAB02882 | ||||
Sequence: L → P | ||||||
Sequence conflict | 2971-2972 | in Ref. 3; AAB02882 | ||||
Sequence: VC → PP | ||||||
Sequence conflict | 2982 | in Ref. 3; AAB02882 | ||||
Sequence: Y → H | ||||||
Sequence conflict | 2985 | in Ref. 3; AAB02882 | ||||
Sequence: N → I | ||||||
Sequence conflict | 3615 | in Ref. 3; AAB02882 | ||||
Sequence: T → S | ||||||
Sequence conflict | 3738 | in Ref. 3; AAB02882 | ||||
Sequence: Q → K | ||||||
Sequence conflict | 3784 | in Ref. 3; AAB02882 | ||||
Sequence: C → LW | ||||||
Sequence conflict | 3810 | in Ref. 3; AAB02882 | ||||
Sequence: C → R | ||||||
Sequence conflict | 4220 | in Ref. 3; AAB02882 | ||||
Sequence: R → P | ||||||
Compositional bias | 4613-4630 | Pro residues | ||||
Sequence: PPPSPSLPAKPKPPSRRD |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U33837 EMBL· GenBank· DDBJ | AAB41649.1 EMBL· GenBank· DDBJ | mRNA | ||
AC007556 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC008178 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
U04441 EMBL· GenBank· DDBJ | AAB02882.1 EMBL· GenBank· DDBJ | mRNA | ||
S73145 EMBL· GenBank· DDBJ | AAB30825.1 EMBL· GenBank· DDBJ | mRNA |