Q07113 · MPRI_MOUSE
- ProteinCation-independent mannose-6-phosphate receptor
- GeneIgf2r
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2483 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Mediates the transport of phosphorylated lysosomal enzymes from the Golgi complex and the cell surface to lysosomes. Lysosomal enzymes bearing phosphomannosyl residues bind specifically to mannose-6-phosphate receptors in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelysosomal compartment where the low pH mediates the dissociation of the complex. The receptor is then recycled back to the Golgi for another round of trafficking through its binding to the retromer. This receptor also binds IGF2. Acts as a positive regulator of T-cell coactivation by binding DPP4.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCation-independent mannose-6-phosphate receptor
- Short namesCI Man-6-P receptor; CI-MPR; M6PR
- Alternative names
- CD Antigen Name
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ07113
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Golgi apparatus membrane ; Single-pass type I membrane protein
Endosome membrane ; Single-pass type I membrane protein
Note: Mainly localized in the Golgi at steady state and not detectable in lysosome. Colocalized with DPP4 in internalized cytoplasmic vesicles adjacent to the cell surface.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 36-2295 | Lumenal | ||||
Sequence: QAVDLDALCSYTWEAVDSKNNAVYKINVCGNVGISSCGPTSAICMCDLKTENCRSVGDSLLRSSARSLLEFNTTMGCQPSDSQHRIQTSITFLCGKTLGTPEFVTATDCVHYFEWRTTAACKKDIFKADKEVPCYAFDDKLQKHDLNPLIKLNGGYLVDDSDPDTSLFINVCRDIDSLRDPSTQLRVCPAGTAACLLKGNQAFDVGRPKEGLKLLSKDRLVLTYVKEEGEKPDFCNGHSPAVTVTFVCPSERREGTIPKLTAKSNCRYEVEWITEYACHRDYLQSESCSLSSEQHDITIDLSPLAQYGGSPYVSDGREYTFFINVCGDTKVSLCNNKEAAVCQEKKADSTQVKIAGRHQNQTLRYSDGDLTLIYSGGDECSSGFQRMSVINFECNKTAGKDGRGEPVFTGEVDCTYFFTWDTKYACIKEKEDLLCGAINGKKRYDLSVLARHSESEQNWEAVDGSQAESEKYFFINVCHRVLQEGKARNCPEDAAVCAVDKNGSKNLGKFVSSPTKEKGHIQLSYTDGDDCGSDKKISTNITLVCKPGDLESAPVLRAARSDGCFYEFEWHTAAACVLSKTEGENCTVLDAQAGFSFDLSLLTKKNGAYKVETEKYDFYINVCGPVSMDPCQSNSGACQVAKSGKSWNLGLSSTKLTYYDGMIQLSYRNGTPYNNEKHTPRATLITFLCDRDAGVGFPEYQEEDNSTYNFRWYTSYACPEEPLECMVTDPSMMEQYDLSSLVKSEGGSGGNWYAMENSREHVTRRKYYLNVCRPLNPVPGCDRYASACQMKYENHEGSLAETVSISNLGVAKIGPVVEESGSLLLEYVNGSACTTSDGQLTTYSTRIHLVCGRGFMNSHPIFTFNWECVVSFLWNTEAACPIQTITETDQACSIRDPSSGFVFNLSPLNDSAQGHVVLGIGKTFVFNICGAMPACGTVAGKPAYGCEAETQIEDIKDLRPQRPVGMERSLQLSAEGFLTLTYKGSSPSDRGTAFIIRFICNDDIYPGAPKFLHQDIDSTRGIRNTYFEFETALACTPSLVDCQVTDPAGNEYDLSALSMVRKPWTAVDTSAYGKRRHFYLSVCNPLPYIPGCHGIALGSCMVSEDNSFNLGVVQISPQATGNGSLSILYVNGDRCGDQRFSTRIVFECAQTSGSPMFQFVNNCEYVFVWRTVEACPVIREEGDNCQVKDPRHGNLYDLKPLGLNDTIVSVGEYTYYLRVCGKLSSDVCSAHDGSKAVSSCQEKKGPQGFQKVAGLLSQKLTFENGLLKMNYTGGDTCHKVYQRSTTIYFYCDRTTQKPVFLKETSDCSYMFEWRTQYACPPFNVTECSVQDAAGNSIDLSSLSRYSDNWEAVTRTGATEHYLINVCKSLSPHAGTEPCPPEAAVCLLNGSKPVNLGKVRDGPQWTDGVTVLQYVDGDLCPDKIRRRSTIIRFTCSDNQVNSRPLFISAVQDCEYTFSWPTPSACPVKSNTHDDCQVTNPSTGHLFDLSSLSGRAGINASYSEKGLVFMSICEENENCGPGVGACFGQTRISVGKASKRLSYKDQVLQLVYENGSPCPSLSDLRYKSVISFVCRPEAGPTNRPMLISLDKQTCTLFFSWHTPLACEQATECTVRNGSSIIDLSPLIHRTGGYEAYDESEDDTSDTTPDFYINICQPLNPMHGVPCPAGASVCKVPVDGPPIDIGRVTGPPIFNPVANEVYLNFESSTHCLADRYMNYTSLITFHCKRGVSMGTPKLIRTNDCDFVFEWETPIVCPDEVKTQGCAVTDEQLLYSFNLTSLSTSTFKVTRDARTYSIGVCTAAAGLGQEGCKDGGVCLLSGNKGASFGRLASMQLDYRHQDEAVILSYVNGDPCPPETDDGEPCVFPFIYKGKSYDECVLEGRAKLWCSKTANYDRDHEWGFCRQTNSYRMSAIIFTCDESEDIGRPQVFSEDRGCEVTFEWKTKVVCPPKKMECKFVQKHKTYDLRLLSSLTGSWDFVHEGNSYFINLCQRVYKGPLDCSERASICKKSATGQVQVLGLVHTQKLEVIDETVIVTYSKGYPCGGNKTASSVIELTCAKTVGRPAFKRFDSVSCTYYFYWYSRAACAVRPQEVTMVNGTLTNPVTGKSFSLGEIYFKLFSASGDMRTNGDNYLYEIQLSSITSSSYPACAGANICQVKPNDQHFSRKVGTSDMTKYYVQDGDLDVVFTSSSKCGKDKTKSVSSTIFFHCDPLVKDGIPEFSHETADCQYLFSWYTSAVCPLGVDFEDESAGPEYKGLSERSQA | ||||||
Transmembrane | 2296-2316 | Helical | ||||
Sequence: VGAVLSLLLVALTGCLLALLL | ||||||
Topological domain | 2317-2483 | Cytoplasmic | ||||
Sequence: HKKERRETVINKLTSCCRRSSGVSYKYSKVSKEEETDENETEWLMEEIQVPAPRLGKDGQENGHITTKAVKAEALSSLHGDDQDSEDEVLTVPEVKVHSGRGAEVESSQPLRNPQRKVLKEREGERLGLVRGEKARKGKFRPGQRKPTAPAKLVSFHDDSDEDLLHI |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-35 | |||||
Sequence: MRAVQLGPVPSGPRVALLPPLLLLLLLAAAGSAQA | ||||||
Chain | PRO_0000019230 | 36-2483 | Cation-independent mannose-6-phosphate receptor | |||
Sequence: QAVDLDALCSYTWEAVDSKNNAVYKINVCGNVGISSCGPTSAICMCDLKTENCRSVGDSLLRSSARSLLEFNTTMGCQPSDSQHRIQTSITFLCGKTLGTPEFVTATDCVHYFEWRTTAACKKDIFKADKEVPCYAFDDKLQKHDLNPLIKLNGGYLVDDSDPDTSLFINVCRDIDSLRDPSTQLRVCPAGTAACLLKGNQAFDVGRPKEGLKLLSKDRLVLTYVKEEGEKPDFCNGHSPAVTVTFVCPSERREGTIPKLTAKSNCRYEVEWITEYACHRDYLQSESCSLSSEQHDITIDLSPLAQYGGSPYVSDGREYTFFINVCGDTKVSLCNNKEAAVCQEKKADSTQVKIAGRHQNQTLRYSDGDLTLIYSGGDECSSGFQRMSVINFECNKTAGKDGRGEPVFTGEVDCTYFFTWDTKYACIKEKEDLLCGAINGKKRYDLSVLARHSESEQNWEAVDGSQAESEKYFFINVCHRVLQEGKARNCPEDAAVCAVDKNGSKNLGKFVSSPTKEKGHIQLSYTDGDDCGSDKKISTNITLVCKPGDLESAPVLRAARSDGCFYEFEWHTAAACVLSKTEGENCTVLDAQAGFSFDLSLLTKKNGAYKVETEKYDFYINVCGPVSMDPCQSNSGACQVAKSGKSWNLGLSSTKLTYYDGMIQLSYRNGTPYNNEKHTPRATLITFLCDRDAGVGFPEYQEEDNSTYNFRWYTSYACPEEPLECMVTDPSMMEQYDLSSLVKSEGGSGGNWYAMENSREHVTRRKYYLNVCRPLNPVPGCDRYASACQMKYENHEGSLAETVSISNLGVAKIGPVVEESGSLLLEYVNGSACTTSDGQLTTYSTRIHLVCGRGFMNSHPIFTFNWECVVSFLWNTEAACPIQTITETDQACSIRDPSSGFVFNLSPLNDSAQGHVVLGIGKTFVFNICGAMPACGTVAGKPAYGCEAETQIEDIKDLRPQRPVGMERSLQLSAEGFLTLTYKGSSPSDRGTAFIIRFICNDDIYPGAPKFLHQDIDSTRGIRNTYFEFETALACTPSLVDCQVTDPAGNEYDLSALSMVRKPWTAVDTSAYGKRRHFYLSVCNPLPYIPGCHGIALGSCMVSEDNSFNLGVVQISPQATGNGSLSILYVNGDRCGDQRFSTRIVFECAQTSGSPMFQFVNNCEYVFVWRTVEACPVIREEGDNCQVKDPRHGNLYDLKPLGLNDTIVSVGEYTYYLRVCGKLSSDVCSAHDGSKAVSSCQEKKGPQGFQKVAGLLSQKLTFENGLLKMNYTGGDTCHKVYQRSTTIYFYCDRTTQKPVFLKETSDCSYMFEWRTQYACPPFNVTECSVQDAAGNSIDLSSLSRYSDNWEAVTRTGATEHYLINVCKSLSPHAGTEPCPPEAAVCLLNGSKPVNLGKVRDGPQWTDGVTVLQYVDGDLCPDKIRRRSTIIRFTCSDNQVNSRPLFISAVQDCEYTFSWPTPSACPVKSNTHDDCQVTNPSTGHLFDLSSLSGRAGINASYSEKGLVFMSICEENENCGPGVGACFGQTRISVGKASKRLSYKDQVLQLVYENGSPCPSLSDLRYKSVISFVCRPEAGPTNRPMLISLDKQTCTLFFSWHTPLACEQATECTVRNGSSIIDLSPLIHRTGGYEAYDESEDDTSDTTPDFYINICQPLNPMHGVPCPAGASVCKVPVDGPPIDIGRVTGPPIFNPVANEVYLNFESSTHCLADRYMNYTSLITFHCKRGVSMGTPKLIRTNDCDFVFEWETPIVCPDEVKTQGCAVTDEQLLYSFNLTSLSTSTFKVTRDARTYSIGVCTAAAGLGQEGCKDGGVCLLSGNKGASFGRLASMQLDYRHQDEAVILSYVNGDPCPPETDDGEPCVFPFIYKGKSYDECVLEGRAKLWCSKTANYDRDHEWGFCRQTNSYRMSAIIFTCDESEDIGRPQVFSEDRGCEVTFEWKTKVVCPPKKMECKFVQKHKTYDLRLLSSLTGSWDFVHEGNSYFINLCQRVYKGPLDCSERASICKKSATGQVQVLGLVHTQKLEVIDETVIVTYSKGYPCGGNKTASSVIELTCAKTVGRPAFKRFDSVSCTYYFYWYSRAACAVRPQEVTMVNGTLTNPVTGKSFSLGEIYFKLFSASGDMRTNGDNYLYEIQLSSITSSSYPACAGANICQVKPNDQHFSRKVGTSDMTKYYVQDGDLDVVFTSSSKCGKDKTKSVSSTIFFHCDPLVKDGIPEFSHETADCQYLFSWYTSAVCPLGVDFEDESAGPEYKGLSERSQAVGAVLSLLLVALTGCLLALLLHKKERRETVINKLTSCCRRSSGVSYKYSKVSKEEETDENETEWLMEEIQVPAPRLGKDGQENGHITTKAVKAEALSSLHGDDQDSEDEVLTVPEVKVHSGRGAEVESSQPLRNPQRKVLKEREGERLGLVRGEKARKGKFRPGQRKPTAPAKLVSFHDDSDEDLLHI | ||||||
Disulfide bond | 44↔64 | |||||
Sequence: CSYTWEAVDSKNNAVYKINVC | ||||||
Disulfide bond | 72↔79 | |||||
Sequence: CGPTSAIC | ||||||
Glycosylation | 107 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 112↔144 | |||||
Sequence: CQPSDSQHRIQTSITFLCGKTLGTPEFVTATDC | ||||||
Disulfide bond | 129↔156 | |||||
Sequence: CGKTLGTPEFVTATDCVHYFEWRTTAAC | ||||||
Disulfide bond | 169↔207 | |||||
Sequence: CYAFDDKLQKHDLNPLIKLNGGYLVDDSDPDTSLFINVC | ||||||
Disulfide bond | 223↔230 | |||||
Sequence: CPAGTAAC | ||||||
Disulfide bond | 270↔301 | |||||
Sequence: CNGHSPAVTVTFVCPSERREGTIPKLTAKSNC | ||||||
Disulfide bond | 283↔313 | |||||
Sequence: CPSERREGTIPKLTAKSNCRYEVEWITEYAC | ||||||
Disulfide bond | 323↔361 | |||||
Sequence: CSLSSEQHDITIDLSPLAQYGGSPYVSDGREYTFFINVC | ||||||
Disulfide bond | 369↔377 | |||||
Sequence: CNNKEAAVC | ||||||
Glycosylation | 395 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 415↔449 | |||||
Sequence: CSSGFQRMSVINFECNKTAGKDGRGEPVFTGEVDC | ||||||
Disulfide bond | 429↔461 | |||||
Sequence: CNKTAGKDGRGEPVFTGEVDCTYFFTWDTKYAC | ||||||
Glycosylation | 430 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 470↔513 | |||||
Sequence: CGAINGKKRYDLSVLARHSESEQNWEAVDGSQAESEKYFFINVC | ||||||
Disulfide bond | 525↔532 | |||||
Sequence: CPEDAAVC | ||||||
Glycosylation | 537 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 566↔599 | |||||
Sequence: CGSDKKISTNITLVCKPGDLESAPVLRAARSDGC | ||||||
Glycosylation | 575 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 580↔611 | |||||
Sequence: CKPGDLESAPVLRAARSDGCFYEFEWHTAAAC | ||||||
Glycosylation | 620 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 621↔658 | |||||
Sequence: CTVLDAQAGFSFDLSLLTKKNGAYKVETEKYDFYINVC | ||||||
Disulfide bond | 666↔673 | |||||
Sequence: CQSNSGAC | ||||||
Disulfide bond | 724↔753 | |||||
Sequence: CDRDAGVGFPEYQEEDNSTYNFRWYTSYAC | ||||||
Glycosylation | 740 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 760↔807 | |||||
Sequence: CMVTDPSMMEQYDLSSLVKSEGGSGGNWYAMENSREHVTRRKYYLNVC | ||||||
Disulfide bond | 816↔823 | |||||
Sequence: CDRYASAC | ||||||
Glycosylation | 864 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 868↔903 | |||||
Sequence: CTTSDGQLTTYSTRIHLVCGRGFMNSHPIFTFNWEC | ||||||
Disulfide bond | 886↔915 | |||||
Sequence: CGRGFMNSHPIFTFNWECVVSFLWNTEAAC | ||||||
Disulfide bond | 927↔964 | |||||
Sequence: CSIRDPSSGFVFNLSPLNDSAQGHVVLGIGKTFVFNIC | ||||||
Glycosylation | 944 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 970↔981 | |||||
Sequence: CGTVAGKPAYGC | ||||||
Disulfide bond | 1035↔1070 | |||||
Sequence: CNDDIYPGAPKFLHQDIDSTRGIRNTYFEFETALAC | ||||||
Disulfide bond | 1077↔1118 | |||||
Sequence: CQVTDPAGNEYDLSALSMVRKPWTAVDTSAYGKRRHFYLSVC | ||||||
Disulfide bond | 1127↔1135 | |||||
Sequence: CHGIALGSC | ||||||
Glycosylation | 1157 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1170↔1198 | |||||
Sequence: CGDQRFSTRIVFECAQTSGSPMFQFVNNC | ||||||
Disulfide bond | 1183↔1210 | |||||
Sequence: CAQTSGSPMFQFVNNCEYVFVWRTVEAC | ||||||
Disulfide bond | 1220↔1255 | |||||
Sequence: CQVKDPRHGNLYDLKPLGLNDTIVSVGEYTYYLRVC | ||||||
Glycosylation | 1239 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1263↔1275 | |||||
Sequence: CSAHDGSKAVSSC | ||||||
Glycosylation | 1305 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1312↔1342 | |||||
Sequence: CHKVYQRSTTIYFYCDRTTQKPVFLKETSDC | ||||||
Disulfide bond | 1326↔1354 | |||||
Sequence: CDRTTQKPVFLKETSDCSYMFEWRTQYAC | ||||||
Glycosylation | 1358 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1362↔1401 | |||||
Sequence: CSVQDAAGNSIDLSSLSRYSDNWEAVTRTGATEHYLINVC | ||||||
Disulfide bond | 1413↔1420 | |||||
Sequence: CPPEAAVC | ||||||
Glycosylation | 1423 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1454↔1487 | |||||
Sequence: CPDKIRRRSTIIRFTCSDNQVNSRPLFISAVQDC | ||||||
Disulfide bond | 1469↔1499 | |||||
Sequence: CSDNQVNSRPLFISAVQDCEYTFSWPTPSAC | ||||||
Disulfide bond | 1509↔1546 | |||||
Sequence: CQVTNPSTGHLFDLSSLSGRAGINASYSEKGLVFMSIC | ||||||
Glycosylation | 1532 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1552↔1559 | |||||
Sequence: CGPGVGAC | ||||||
Disulfide bond | 1591↔1627 | |||||
Sequence: CPSLSDLRYKSVISFVCRPEAGPTNRPMLISLDKQTC | ||||||
Disulfide bond | 1607↔1639 | |||||
Sequence: CRPEAGPTNRPMLISLDKQTCTLFFSWHTPLAC | ||||||
Disulfide bond | 1645↔1688 | |||||
Sequence: CTVRNGSSIIDLSPLIHRTGGYEAYDESEDDTSDTTPDFYINIC | ||||||
Glycosylation | 1649 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1699↔1706 | |||||
Sequence: CPAGASVC | ||||||
Disulfide bond | 1743↔1776 | |||||
Sequence: CLADRYMNYTSLITFHCKRGVSMGTPKLIRTNDC | ||||||
Glycosylation | 1750 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1759↔1788 | |||||
Sequence: CKRGVSMGTPKLIRTNDCDFVFEWETPIVC | ||||||
Disulfide bond | 1797↔1832 | |||||
Sequence: CAVTDEQLLYSFNLTSLSTSTFKVTRDARTYSIGVC | ||||||
Glycosylation | 1809 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1843↔1849 | |||||
Sequence: CKDGGVC | ||||||
Disulfide bond | 1886↔1968 | |||||
Sequence: CPPETDDGEPCVFPFIYKGKSYDECVLEGRAKLWCSKTANYDRDHEWGFCRQTNSYRMSAIIFTCDESEDIGRPQVFSEDRGC | ||||||
Disulfide bond | 1896↔1920 | |||||
Sequence: CVFPFIYKGKSYDECVLEGRAKLWC | ||||||
Disulfide bond | 1910↔1935 | |||||
Sequence: CVLEGRAKLWCSKTANYDRDHEWGFC | ||||||
Disulfide bond | 1950↔1980 | |||||
Sequence: CDESEDIGRPQVFSEDRGCEVTFEWKTKVVC | ||||||
Disulfide bond | 1987↔2022 | |||||
Sequence: CKFVQKHKTYDLRLLSSLTGSWDFVHEGNSYFINLC | ||||||
Disulfide bond | 2032↔2039 | |||||
Sequence: CSERASIC | ||||||
Disulfide bond | 2075↔2106 | |||||
Sequence: CGGNKTASSVIELTCAKTVGRPAFKRFDSVSC | ||||||
Glycosylation | 2078 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2089↔2118 | |||||
Sequence: CAKTVGRPAFKRFDSVSCTYYFYWYSRAAC | ||||||
Glycosylation | 2129 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2181↔2187 | |||||
Sequence: CAGANIC | ||||||
Disulfide bond | 2225↔2259 | |||||
Sequence: CGKDKTKSVSSTIFFHCDPLVKDGIPEFSHETADC | ||||||
Disulfide bond | 2241↔2271 | |||||
Sequence: CDPLVKDGIPEFSHETADCQYLFSWYTSAVC | ||||||
Modified residue | 2342 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 2401 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2417 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Modified residue | 2471 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2476 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Palmitoylated. Undergoes cysteine S-palmitoylation which promotes interaction with the retromer cargo-selective complex which mediates its retrograde trafficking to the Golgi apparatus.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Binds HA-I and HA-II plasma membrane adapters (By similarity).
Interacts with DPP4; the interaction is direct. Binds GGA1, GGA2 and GGA3 (By similarity).
Interacts with the heterotrimeric retromer cargo-selective complex (CSC), formed by VPS26 (VPS26A or VPS26B), VPS29 and VPS35; which is involved in retrograde trafficking of the receptor from endosomes to the Golgi apparatus (By similarity).
Interacts with DPP4; the interaction is direct. Binds GGA1, GGA2 and GGA3 (By similarity).
Interacts with the heterotrimeric retromer cargo-selective complex (CSC), formed by VPS26 (VPS26A or VPS26B), VPS29 and VPS35; which is involved in retrograde trafficking of the receptor from endosomes to the Golgi apparatus (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q07113 | Sting1 Q3TBT3 | 2 | EBI-2891155, EBI-3862093 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 42-158 | MRH 1 | ||||
Sequence: ALCSYTWEAVDSKNNAVYKINVCGNVGISSCGPTSAICMCDLKTENCRSVGDSLLRSSARSLLEFNTTMGCQPSDSQHRIQTSITFLCGKTLGTPEFVTATDCVHYFEWRTTAACKK | ||||||
Domain | 167-315 | MRH 2 | ||||
Sequence: VPCYAFDDKLQKHDLNPLIKLNGGYLVDDSDPDTSLFINVCRDIDSLRDPSTQLRVCPAGTAACLLKGNQAFDVGRPKEGLKLLSKDRLVLTYVKEEGEKPDFCNGHSPAVTVTFVCPSERREGTIPKLTAKSNCRYEVEWITEYACHR | ||||||
Domain | 321-463 | MRH 3 | ||||
Sequence: ESCSLSSEQHDITIDLSPLAQYGGSPYVSDGREYTFFINVCGDTKVSLCNNKEAAVCQEKKADSTQVKIAGRHQNQTLRYSDGDLTLIYSGGDECSSGFQRMSVINFECNKTAGKDGRGEPVFTGEVDCTYFFTWDTKYACIK | ||||||
Domain | 468-613 | MRH 4 | ||||
Sequence: LLCGAINGKKRYDLSVLARHSESEQNWEAVDGSQAESEKYFFINVCHRVLQEGKARNCPEDAAVCAVDKNGSKNLGKFVSSPTKEKGHIQLSYTDGDDCGSDKKISTNITLVCKPGDLESAPVLRAARSDGCFYEFEWHTAAACVL | ||||||
Domain | 619-755 | MRH 5 | ||||
Sequence: ENCTVLDAQAGFSFDLSLLTKKNGAYKVETEKYDFYINVCGPVSMDPCQSNSGACQVAKSGKSWNLGLSSTKLTYYDGMIQLSYRNGTPYNNEKHTPRATLITFLCDRDAGVGFPEYQEEDNSTYNFRWYTSYACPE | ||||||
Domain | 758-917 | MRH 6 | ||||
Sequence: LECMVTDPSMMEQYDLSSLVKSEGGSGGNWYAMENSREHVTRRKYYLNVCRPLNPVPGCDRYASACQMKYENHEGSLAETVSISNLGVAKIGPVVEESGSLLLEYVNGSACTTSDGQLTTYSTRIHLVCGRGFMNSHPIFTFNWECVVSFLWNTEAACPI | ||||||
Domain | 925-1072 | MRH 7 | ||||
Sequence: QACSIRDPSSGFVFNLSPLNDSAQGHVVLGIGKTFVFNICGAMPACGTVAGKPAYGCEAETQIEDIKDLRPQRPVGMERSLQLSAEGFLTLTYKGSSPSDRGTAFIIRFICNDDIYPGAPKFLHQDIDSTRGIRNTYFEFETALACTP | ||||||
Domain | 1075-1212 | MRH 8 | ||||
Sequence: VDCQVTDPAGNEYDLSALSMVRKPWTAVDTSAYGKRRHFYLSVCNPLPYIPGCHGIALGSCMVSEDNSFNLGVVQISPQATGNGSLSILYVNGDRCGDQRFSTRIVFECAQTSGSPMFQFVNNCEYVFVWRTVEACPV | ||||||
Domain | 1218-1356 | MRH 9 | ||||
Sequence: DNCQVKDPRHGNLYDLKPLGLNDTIVSVGEYTYYLRVCGKLSSDVCSAHDGSKAVSSCQEKKGPQGFQKVAGLLSQKLTFENGLLKMNYTGGDTCHKVYQRSTTIYFYCDRTTQKPVFLKETSDCSYMFEWRTQYACPP | ||||||
Domain | 1360-1501 | MRH 10 | ||||
Sequence: TECSVQDAAGNSIDLSSLSRYSDNWEAVTRTGATEHYLINVCKSLSPHAGTEPCPPEAAVCLLNGSKPVNLGKVRDGPQWTDGVTVLQYVDGDLCPDKIRRRSTIIRFTCSDNQVNSRPLFISAVQDCEYTFSWPTPSACPV | ||||||
Domain | 1507-1641 | MRH 11 | ||||
Sequence: DDCQVTNPSTGHLFDLSSLSGRAGINASYSEKGLVFMSICEENENCGPGVGACFGQTRISVGKASKRLSYKDQVLQLVYENGSPCPSLSDLRYKSVISFVCRPEAGPTNRPMLISLDKQTCTLFFSWHTPLACEQ | ||||||
Domain | 1643-1790 | MRH 12 | ||||
Sequence: TECTVRNGSSIIDLSPLIHRTGGYEAYDESEDDTSDTTPDFYINICQPLNPMHGVPCPAGASVCKVPVDGPPIDIGRVTGPPIFNPVANEVYLNFESSTHCLADRYMNYTSLITFHCKRGVSMGTPKLIRTNDCDFVFEWETPIVCPD | ||||||
Domain | 1795-1982 | MRH 13 | ||||
Sequence: QGCAVTDEQLLYSFNLTSLSTSTFKVTRDARTYSIGVCTAAAGLGQEGCKDGGVCLLSGNKGASFGRLASMQLDYRHQDEAVILSYVNGDPCPPETDDGEPCVFPFIYKGKSYDECVLEGRAKLWCSKTANYDRDHEWGFCRQTNSYRMSAIIFTCDESEDIGRPQVFSEDRGCEVTFEWKTKVVCPP | ||||||
Domain | 1891-1937 | Fibronectin type-II | ||||
Sequence: DDGEPCVFPFIYKGKSYDECVLEGRAKLWCSKTANYDRDHEWGFCRQ | ||||||
Domain | 1985-2120 | MRH 14 | ||||
Sequence: MECKFVQKHKTYDLRLLSSLTGSWDFVHEGNSYFINLCQRVYKGPLDCSERASICKKSATGQVQVLGLVHTQKLEVIDETVIVTYSKGYPCGGNKTASSVIELTCAKTVGRPAFKRFDSVSCTYYFYWYSRAACAV | ||||||
Domain | 2128-2273 | MRH 15 | ||||
Sequence: VNGTLTNPVTGKSFSLGEIYFKLFSASGDMRTNGDNYLYEIQLSSITSSSYPACAGANICQVKPNDQHFSRKVGTSDMTKYYVQDGDLDVVFTSSSKCGKDKTKSVSSTIFFHCDPLVKDGIPEFSHETADCQYLFSWYTSAVCPL | ||||||
Region | 2415-2483 | Disordered | ||||
Sequence: SGRGAEVESSQPLRNPQRKVLKEREGERLGLVRGEKARKGKFRPGQRKPTAPAKLVSFHDDSDEDLLHI | ||||||
Compositional bias | 2431-2453 | Basic and acidic residues | ||||
Sequence: QRKVLKEREGERLGLVRGEKARK |
Domain
Contains 15 repeating units of approximately 147 AA harboring four disulfide bonds each. The most highly conserved region within the repeat consists of a stretch of 13 AA that contains cysteines at both ends.
Sequence similarities
Belongs to the MRL1/IGF2R family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length2,483
- Mass (Da)273,815
- Last updated1996-10-01 v1
- Checksum8F64F6189FD05CD1
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 10-11 | in Ref. 2 | ||||
Sequence: PS → RP | ||||||
Sequence conflict | 13 | in Ref. 2 | ||||
Sequence: Missing | ||||||
Sequence conflict | 209 | in Ref. 2; AAA19568 | ||||
Sequence: D → V | ||||||
Sequence conflict | 456-457 | in Ref. 2 | ||||
Sequence: DT → VS | ||||||
Sequence conflict | 1626-1631 | in Ref. 6; CAA42940 | ||||
Sequence: TCTLFF → GSTFFS | ||||||
Sequence conflict | 1694-1695 | in Ref. 6; CAA42940 | ||||
Sequence: MH → TC | ||||||
Sequence conflict | 1699 | in Ref. 6; CAA42940 | ||||
Sequence: C → R | ||||||
Sequence conflict | 1759 | in Ref. 2; AAA19568 | ||||
Sequence: C → Y | ||||||
Sequence conflict | 2028 | in Ref. 6; CAA42940 | ||||
Sequence: G → V | ||||||
Sequence conflict | 2032 | in Ref. 6; CAA42940 | ||||
Sequence: C → S | ||||||
Compositional bias | 2431-2453 | Basic and acidic residues | ||||
Sequence: QRKVLKEREGERLGLVRGEKARK |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L22143 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22096 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22097 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22098 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22099 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22100 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22101 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22102 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22103 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22104 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22105 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22106 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22107 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22108 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22109 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22110 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22111 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22112 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22113 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22114 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22115 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22116 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22117 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22118 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22119 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22120 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22121 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22122 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22123 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22124 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22125 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22126 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22127 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22128 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22129 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22130 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22131 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22132 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22133 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22134 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22135 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22136 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22137 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22138 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22139 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22140 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22141 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22142 EMBL· GenBank· DDBJ | AAA39320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U04710 EMBL· GenBank· DDBJ | AAA19568.1 EMBL· GenBank· DDBJ | mRNA | ||
L06445 EMBL· GenBank· DDBJ | AAA37921.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L06446 EMBL· GenBank· DDBJ | AAA37922.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U26348 EMBL· GenBank· DDBJ | AAA98844.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M58586 EMBL· GenBank· DDBJ | AAA39483.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X60389 EMBL· GenBank· DDBJ | CAA42940.1 EMBL· GenBank· DDBJ | mRNA | ||
L19500 EMBL· GenBank· DDBJ | AAA16037.1 EMBL· GenBank· DDBJ | mRNA |