O08852 · PKD1_MOUSE
- ProteinPolycystin-1
- GenePkd1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids4293 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Component of a heteromeric calcium-permeable ion channel formed by PKD1 and PKD2 that is activated by interaction between PKD1 and a Wnt family member, such as WNT3A and WNT9B. Both PKD1 and PKD2 are required for channel activity (By similarity).
Involved in renal tubulogenesis (PubMed:24939912).
Involved in fluid-flow mechanosensation by the primary cilium in renal epithelium (PubMed:12514735).
Acts as a regulator of cilium length, together with PKD2 (PubMed:20096584).
The dynamic control of cilium length is essential in the regulation of mechanotransductive signaling. The cilium length response creates a negative feedback loop whereby fluid shear-mediated deflection of the primary cilium, which decreases intracellular cAMP, leads to cilium shortening and thus decreases flow-induced signaling. May be an ion-channel regulator. Involved in adhesive protein-protein and protein-carbohydrate interactions. Likely to be involved with polycystin-1-interacting protein 1 in the detection, sequestration and exocytosis of senescent mitochondria (By similarity).
Involved in renal tubulogenesis (PubMed:24939912).
Involved in fluid-flow mechanosensation by the primary cilium in renal epithelium (PubMed:12514735).
Acts as a regulator of cilium length, together with PKD2 (PubMed:20096584).
The dynamic control of cilium length is essential in the regulation of mechanotransductive signaling. The cilium length response creates a negative feedback loop whereby fluid shear-mediated deflection of the primary cilium, which decreases intracellular cAMP, leads to cilium shortening and thus decreases flow-induced signaling. May be an ion-channel regulator. Involved in adhesive protein-protein and protein-carbohydrate interactions. Likely to be involved with polycystin-1-interacting protein 1 in the detection, sequestration and exocytosis of senescent mitochondria (By similarity).
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 3040-3041 | Cleavage; by autolysis | ||||
Sequence: LT |
GO annotations
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePolycystin-1
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionO08852
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Note: PKD1 localization to the plasma and ciliary membranes requires PKD2, is independent of PKD2 channel activity, and involves stimulation of PKD1 autocatalytic cleavage at the GPS region of the GAIN-B domain (PubMed:12514735, PubMed:25405894).
PKD1:PKD2 interaction is required to reach the Golgi apparatus from endoplasmic reticulum and then traffic to the cilia (PubMed:25405894).
Ciliary localization of PKD1 requires BBS1 and ARL6/BBS3 (PubMed:24939912).
Cell surface localization requires GANAB (By similarity).
Detected on migrasomes and on extracellular exosomes in urine (By similarity).
PKD1:PKD2 interaction is required to reach the Golgi apparatus from endoplasmic reticulum and then traffic to the cilia (PubMed:25405894).
Ciliary localization of PKD1 requires BBS1 and ARL6/BBS3 (PubMed:24939912).
Cell surface localization requires GANAB (By similarity).
Detected on migrasomes and on extracellular exosomes in urine (By similarity).
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 24-3066 | Extracellular | ||||
Sequence: GDPGRGCGPCPLPCFCGPAPDAACRVNCSGRWLQTLGPSLRIPADATALDLSHNLLQTLDIGLLVNLSALVELDLSNNRISTLEEGVFANLFNLSEINLSGNPFECNCGLAWLPRWAKEHQVHVVQSEATTCRGPIPLAGQPLLSIPLLDNACGEEYVACLPDNSSGAVAAVPFYFAHEGPLETEACSAFCFSAGEGLAALSEQNQCLCGAGQASNSSAACSSWCSSISLSLNSACGGPTLLQHTFPASPGATLVGPHGPLASGQPADFHITSSLPISSTRWNFGDGSPEVDMASPAATHFYVLPGSYHMTVVLALGAGSALLETEVQVEATPTVLELVCPSFVHSNESLELGIRHRGGSALEVTYSILALDKEPAQVVHPLCPLDTEIFPGNGHCYRLVAEKAPWLQAQEQCRTWAGAALAMVDSPAIQHFLVSKVTRSLDVWIGFSSVEGTEGLDPRGEAFSLESCQNWLPGEPHPATAEHCVRLGPAGQCNTDLCSAPHSYVCELRPGGPVWDTENFVMGMSGGGLSGPLHPLAQQETVQGPLRPVEVMVFPGLSPSREAFLTAAEFSTQKLEEPAQMRLQVYRPSGGAAAVPEGSSEPDNRTEPAPKCVPEELWCPGANVCIPFDASCNSHVCINGSVSRLGLSRASYTLWKEFFFSVPAGPPTQYLVTLHSQDVPMLPGDLIGLQHDAGPGTLLQCPLASSCPGQALYLSTNASDWMTNLPVHLEEAWAGPVCSLQLLLVTERLTPLLGLGPNPGLQHPGHYEVRATVGNSVSRQNLSCSFSVVSPIAGLRVIHPIPLDGHIYVPTNGSVLVLQVDSGANATATAQWFGGNISAPFEDACPPEVDFLKQDCTEEANGTLFSVLMLPRLKEGDHTVEIVAQNGASQANLSLRVTAEEPICGLRAVPSPEARVLQGILVRYSPMVEAGSDVAFRWTIDDKQSLTFHNTVFNVIYQSAAIFKLSLTASNHVSNITVNYNVTVERMNKMHGLWVSAVPTVLPPNATLALTGGVLVDSAVEVAFLWNFGDGEQVLRQFKPPYDESFQVPDPTVAQVLVEHNTTHIYTTPGEYNLTVLVSNTYENLTQQVTVSVRTVLPNVAIGMSSNVLVAGQPITFSPYPLPSTDGVLYTWDFGDGSPVLIQSQPVLNHTYSMTGAYRITLEVNNTVSSVTAHADIRVFQELHGLTVYLSPSVEQGAPMVVSASVESGDNITWTFDMGDGTVFTGPEATVQHVYLRAQNFTVTVEAANPAGHLSQSLHVQVFVLEVLHIEPSTCIPTQPSAQLMAHVTGDPVHYLFDWTFGDGSSNVTVHGHPSVTHNFTRSGIFPLALVLSSHVNKAHYFTSICVEPEIRNITLQPERQFVKLGDEARLVAYSWPPFPYRYTWDFGTEDTTHTQTGGSEVKFIYREPGSYLVIVTVSNNISSTNDSAFVEVQEPVLVTGIRINGSHVLELQQPYLLSAMGSGSPATYLWELGDGSQSEGPEVTHIYSSTGDFTVRVSGWNEVSRSEAQLNITVKQRVRGLTINASRTVVPLNGSVSFSTLLEVGSDVHYSWVLCDRCTPIPGGPTISYTFRSVGTFNIIVTAENEVGSAQDSIFIYVLQFIEGLQVAGGDNGCCFPTNYTLQLQAAVRDGTNISYSWTAQQEGSLITLFGSGKCFSLTSLKASTYYVHLRATNMLGSAAANRTIDFVEPVESLILSASPNPAAVNMSLTLCAELAGGSGVVYTWYLEEGLSWKTSMPSTTHTFAAPGLHLVRVTAENQLGSVNATVEVAIQVPVGGLSIRTSEPDSIFVAAGSTLPFWGQLAEGTNVTWCWTLPGGSKDSQYIAVRFSTAGSFSLQLNASNAVSWVSAMYNLTVEEPIVNLMLWASSKVVAPGQPVHFEILLAAGSALTFRLQVGGSVPEVLPSPHFSHSFFRVGDHLVNVQAENHVSHAQAQVRILVLEAVVGLQVPNCCEPGMATGTEKNFTARVQRGSRVAYAWYFSLQKVQGDSLVILSGRDVTYTPVAAGLLEIHVRAFNELGGVNLTLMVEVQDIIQYVTLQSGRCFTNRSARFEAATSPSPRRVTYHWDFGDGTPVQKTEEFWADHYYLRPGDYHVEVNATNLVSFFVAQATVTVQVLACREPEVEVALPLQVLMRRSQRNYLEAHVDLRNCVSYQTEYRWEIYRTASCQRPGRMAQMVLPGVDVSRPQLVVPRLALPVGHYCFVFVVSFGDTPLARSIQANVTVAAERLVPIIEGGSYRVWSDTQDLVLDGSKSYDPNLEDGDQTPLNFHWACVASTQSETGGCVLNFGPRGSSVVTIPLERLEAGVEYTFNLIVWKAGRKEEATNQTVLIRSGRVPIVSLECVSCKAQAVYEVSRSSYVYLEGHCHNCSRGYKQGCWAARTFSNKTLVLNETTTSTGSTGMNLVVRPGALRDGEGYIFTLTVLGHSGEEEGCASIRLSPNRPPLGGSCRLFPLDSVRGLTTKVHFECTGWRDAEDGGAPLVYALLLKRCRQSYCENFCIYKGSLSTYGAVLPPGFQPLFVVSLAVVVQDQLGAAVVALNRSLTIVLPEPSGNPADLVPWLHSLTASVLPGLLKQADPQHVIEYSLALITVLNEYEQAPDVSEPNVEQQLRAQMRKNITETLISLRVNTVDDIQQITAALAQCMVSSRELMCRSCLKKMLQKLEGMMRILQAETTEGTLTPTTIADSILNITGDLIHLASLDMQGPQPLELGVEPPSLMVASKAYNLSSALMRILMRSRVLNEEPLTLAGEEIVALGKRSDPLSLLCYGKALGPSCHFSIPEAFSGALSNLSDVVQLIFLVDSNPFPFGYISNYTVSTKVASMAFQTQTGTQIPIEQLAAERAITVKVPNNSDQAAQSSHNPVGSTIVQPQTSVSAVVTADNSNPQAGLHLRITYTVLNERYLSAEPEPYLAVYLHSVSQPNEYNCSASRRISLEVLEGADHRLYTFFIAPGTGTLDRSYYLNLTSHFHWSALEVSVGLYTSLCQYFSEEMMMWRTEGIVPLEETSPSQAVCLTRHLTAFGASLFVPPSHVQFIFPEPSASIN | ||||||
Transmembrane | 3067-3087 | Helical | ||||
Sequence: YIVLLTCVICLVTYVVMAMIL | ||||||
Topological domain | 3088-3269 | Cytoplasmic | ||||
Sequence: RKLDQLDVSRVRVIPFCGKGGRFKYEILVKTGWSRGSGTTAHVGIMLYGEDNRSGHRHLDGDRAFHRNSLDIFQIATPHSLGSVWKIRVWHDNKGLSPAWFLQHIIVRDLQSARSTFFLVNDWLSVETEANGGLVEKEVLAANEAALWQFQRLLVAELQRGFFDKHIWLSIWDRPPRSRFTR | ||||||
Transmembrane | 3270-3290 | Helical | ||||
Sequence: VQRVTCCVLLLCLFLAANAVW | ||||||
Topological domain | 3291-3315 | Extracellular | ||||
Sequence: YGVVRDTTYSMGPVSSLISPGVDTV | ||||||
Transmembrane | 3316-3336 | Helical | ||||
Sequence: AIGLVSSVVVYPVYLAVLFLF | ||||||
Topological domain | 3337-3549 | Cytoplasmic | ||||
Sequence: RMSRSKVSGDQNPTPTGQQALDVDSYLDPSVLDSSLLTLSGLTEAFAGQVKNDLFLEDAKSLVCWPSSEGTLSWPDLLSDPSVVSSTLQRLTQGRPGCMLGSEEDGASLVSPSLPAKYLSASDEDLIHQVLADGANNLVPTQDTLLETDLLTSLSSVPGEKTETLILQTVGEERPASMGLSWEQSPVTRLSRTGLVEGFQKRLLPAWCAPLAH | ||||||
Transmembrane | 3550-3570 | Helical | ||||
Sequence: GLSLLLVAVAVAVSGWIGASF | ||||||
Topological domain | 3571-3572 | Extracellular | ||||
Sequence: PP | ||||||
Transmembrane | 3573-3593 | Helical | ||||
Sequence: SVSVMWLLSSSSSFLASFLGW | ||||||
Topological domain | 3594-3655 | Cytoplasmic | ||||
Sequence: EPLKVLLEALYFSLVAKRLHPDEDDTLVESPAVTPVSERVPRVRPPHGFALFLAKEEARKVK | ||||||
Transmembrane | 3656-3676 | Helical | ||||
Sequence: RLHDMLKRLLVYMLFLLVTLL | ||||||
Topological domain | 3677-3891 | Extracellular | ||||
Sequence: ANYGDASCHGHAYRLQSAIKQELDSQAFLAITRSDEFWPWMSHVFLPYVHGNQSSPELGPPRLRQVRLQEAFCPDPSSSEHMCSAAGSLSTSDYGIGWQSVVQNGSETWAYSAPDLLGAWYWGYCAVYDSGGYIQELGLSLEESRARLGFLQLHNWLDSRSRAVFVELTRYSPAVGLHAAVTLRLEFPVAGHALAAFSVRPFALRRLSTGLSLPL | ||||||
Transmembrane | 3892-3912 | Helical | ||||
Sequence: LTSVCLLLFALYFSMAEVQTW | ||||||
Topological domain | 3913-3925 | Cytoplasmic | ||||
Sequence: RKDGCACTARPDT | ||||||
Transmembrane | 3926-3946 | Helical | ||||
Sequence: WARCLLVILTAATGLVRLAQL | ||||||
Topological domain | 3947-3974 | Extracellular | ||||
Sequence: GIADRQWTHFVQDHPRHFTSFDQVAQLG | ||||||
Transmembrane | 3975-3995 | Helical | ||||
Sequence: SVARGLAASLLFLLLVKAAQQ | ||||||
Topological domain | 3996-4017 | Cytoplasmic | ||||
Sequence: LRFVRQWSVFGKTLCRALPELM | ||||||
Transmembrane | 4018-4038 | Helical | ||||
Sequence: GATLGLVLLGVAYAQMAILLI | ||||||
Topological domain | 4039-4080 | Extracellular | ||||
Sequence: SSGADTLYNMARAFLVLCPGARVPTLCPSESWYLSPLLCVGL | ||||||
Transmembrane | 4081-4100 | Helical | ||||
Sequence: WALRVWGALRLGAILLRWRY | ||||||
Topological domain | 4101-4293 | Cytoplasmic | ||||
Sequence: HALRGELYRPAWEPQDYEMVELFLRRLRLWMGFSKVKEFRHKVRFEGMDPLPSRSSRGSKSSPVVLPPSSGSEASHPSTSSSQPDGPSASLSRSTLKLEPEPSRLHAVFESLLVQFDRLNQATEDVYQLEQQLQSLQGHGHNGPPSSPSPGCFPGSQPALPSRLSRASQGLDQTVGPNRVSLWPNNKVHPSST |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Knockin mice expressing non-cleavable PKD1 show a hypomorphic phenotype. They are viable, show rapid cystic dilation in renal collecting duct and distal convoluted tubule, but not in the proximal portion of the nephron, during the postnatal period, and die with severe uremia, mostly at 3 weeks of age. Additionally, they show dilation of the common bile duct and intrahepatic biliary ducts, but develop a normal pancreas within their life span.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 269 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-23 | |||||
Sequence: MPLGAPALLALALGLGLWLGALA | ||||||
Chain | PRO_0000354054 | 24-4293 | Polycystin-1 | |||
Sequence: GDPGRGCGPCPLPCFCGPAPDAACRVNCSGRWLQTLGPSLRIPADATALDLSHNLLQTLDIGLLVNLSALVELDLSNNRISTLEEGVFANLFNLSEINLSGNPFECNCGLAWLPRWAKEHQVHVVQSEATTCRGPIPLAGQPLLSIPLLDNACGEEYVACLPDNSSGAVAAVPFYFAHEGPLETEACSAFCFSAGEGLAALSEQNQCLCGAGQASNSSAACSSWCSSISLSLNSACGGPTLLQHTFPASPGATLVGPHGPLASGQPADFHITSSLPISSTRWNFGDGSPEVDMASPAATHFYVLPGSYHMTVVLALGAGSALLETEVQVEATPTVLELVCPSFVHSNESLELGIRHRGGSALEVTYSILALDKEPAQVVHPLCPLDTEIFPGNGHCYRLVAEKAPWLQAQEQCRTWAGAALAMVDSPAIQHFLVSKVTRSLDVWIGFSSVEGTEGLDPRGEAFSLESCQNWLPGEPHPATAEHCVRLGPAGQCNTDLCSAPHSYVCELRPGGPVWDTENFVMGMSGGGLSGPLHPLAQQETVQGPLRPVEVMVFPGLSPSREAFLTAAEFSTQKLEEPAQMRLQVYRPSGGAAAVPEGSSEPDNRTEPAPKCVPEELWCPGANVCIPFDASCNSHVCINGSVSRLGLSRASYTLWKEFFFSVPAGPPTQYLVTLHSQDVPMLPGDLIGLQHDAGPGTLLQCPLASSCPGQALYLSTNASDWMTNLPVHLEEAWAGPVCSLQLLLVTERLTPLLGLGPNPGLQHPGHYEVRATVGNSVSRQNLSCSFSVVSPIAGLRVIHPIPLDGHIYVPTNGSVLVLQVDSGANATATAQWFGGNISAPFEDACPPEVDFLKQDCTEEANGTLFSVLMLPRLKEGDHTVEIVAQNGASQANLSLRVTAEEPICGLRAVPSPEARVLQGILVRYSPMVEAGSDVAFRWTIDDKQSLTFHNTVFNVIYQSAAIFKLSLTASNHVSNITVNYNVTVERMNKMHGLWVSAVPTVLPPNATLALTGGVLVDSAVEVAFLWNFGDGEQVLRQFKPPYDESFQVPDPTVAQVLVEHNTTHIYTTPGEYNLTVLVSNTYENLTQQVTVSVRTVLPNVAIGMSSNVLVAGQPITFSPYPLPSTDGVLYTWDFGDGSPVLIQSQPVLNHTYSMTGAYRITLEVNNTVSSVTAHADIRVFQELHGLTVYLSPSVEQGAPMVVSASVESGDNITWTFDMGDGTVFTGPEATVQHVYLRAQNFTVTVEAANPAGHLSQSLHVQVFVLEVLHIEPSTCIPTQPSAQLMAHVTGDPVHYLFDWTFGDGSSNVTVHGHPSVTHNFTRSGIFPLALVLSSHVNKAHYFTSICVEPEIRNITLQPERQFVKLGDEARLVAYSWPPFPYRYTWDFGTEDTTHTQTGGSEVKFIYREPGSYLVIVTVSNNISSTNDSAFVEVQEPVLVTGIRINGSHVLELQQPYLLSAMGSGSPATYLWELGDGSQSEGPEVTHIYSSTGDFTVRVSGWNEVSRSEAQLNITVKQRVRGLTINASRTVVPLNGSVSFSTLLEVGSDVHYSWVLCDRCTPIPGGPTISYTFRSVGTFNIIVTAENEVGSAQDSIFIYVLQFIEGLQVAGGDNGCCFPTNYTLQLQAAVRDGTNISYSWTAQQEGSLITLFGSGKCFSLTSLKASTYYVHLRATNMLGSAAANRTIDFVEPVESLILSASPNPAAVNMSLTLCAELAGGSGVVYTWYLEEGLSWKTSMPSTTHTFAAPGLHLVRVTAENQLGSVNATVEVAIQVPVGGLSIRTSEPDSIFVAAGSTLPFWGQLAEGTNVTWCWTLPGGSKDSQYIAVRFSTAGSFSLQLNASNAVSWVSAMYNLTVEEPIVNLMLWASSKVVAPGQPVHFEILLAAGSALTFRLQVGGSVPEVLPSPHFSHSFFRVGDHLVNVQAENHVSHAQAQVRILVLEAVVGLQVPNCCEPGMATGTEKNFTARVQRGSRVAYAWYFSLQKVQGDSLVILSGRDVTYTPVAAGLLEIHVRAFNELGGVNLTLMVEVQDIIQYVTLQSGRCFTNRSARFEAATSPSPRRVTYHWDFGDGTPVQKTEEFWADHYYLRPGDYHVEVNATNLVSFFVAQATVTVQVLACREPEVEVALPLQVLMRRSQRNYLEAHVDLRNCVSYQTEYRWEIYRTASCQRPGRMAQMVLPGVDVSRPQLVVPRLALPVGHYCFVFVVSFGDTPLARSIQANVTVAAERLVPIIEGGSYRVWSDTQDLVLDGSKSYDPNLEDGDQTPLNFHWACVASTQSETGGCVLNFGPRGSSVVTIPLERLEAGVEYTFNLIVWKAGRKEEATNQTVLIRSGRVPIVSLECVSCKAQAVYEVSRSSYVYLEGHCHNCSRGYKQGCWAARTFSNKTLVLNETTTSTGSTGMNLVVRPGALRDGEGYIFTLTVLGHSGEEEGCASIRLSPNRPPLGGSCRLFPLDSVRGLTTKVHFECTGWRDAEDGGAPLVYALLLKRCRQSYCENFCIYKGSLSTYGAVLPPGFQPLFVVSLAVVVQDQLGAAVVALNRSLTIVLPEPSGNPADLVPWLHSLTASVLPGLLKQADPQHVIEYSLALITVLNEYEQAPDVSEPNVEQQLRAQMRKNITETLISLRVNTVDDIQQITAALAQCMVSSRELMCRSCLKKMLQKLEGMMRILQAETTEGTLTPTTIADSILNITGDLIHLASLDMQGPQPLELGVEPPSLMVASKAYNLSSALMRILMRSRVLNEEPLTLAGEEIVALGKRSDPLSLLCYGKALGPSCHFSIPEAFSGALSNLSDVVQLIFLVDSNPFPFGYISNYTVSTKVASMAFQTQTGTQIPIEQLAAERAITVKVPNNSDQAAQSSHNPVGSTIVQPQTSVSAVVTADNSNPQAGLHLRITYTVLNERYLSAEPEPYLAVYLHSVSQPNEYNCSASRRISLEVLEGADHRLYTFFIAPGTGTLDRSYYLNLTSHFHWSALEVSVGLYTSLCQYFSEEMMMWRTEGIVPLEETSPSQAVCLTRHLTAFGASLFVPPSHVQFIFPEPSASINYIVLLTCVICLVTYVVMAMILRKLDQLDVSRVRVIPFCGKGGRFKYEILVKTGWSRGSGTTAHVGIMLYGEDNRSGHRHLDGDRAFHRNSLDIFQIATPHSLGSVWKIRVWHDNKGLSPAWFLQHIIVRDLQSARSTFFLVNDWLSVETEANGGLVEKEVLAANEAALWQFQRLLVAELQRGFFDKHIWLSIWDRPPRSRFTRVQRVTCCVLLLCLFLAANAVWYGVVRDTTYSMGPVSSLISPGVDTVAIGLVSSVVVYPVYLAVLFLFRMSRSKVSGDQNPTPTGQQALDVDSYLDPSVLDSSLLTLSGLTEAFAGQVKNDLFLEDAKSLVCWPSSEGTLSWPDLLSDPSVVSSTLQRLTQGRPGCMLGSEEDGASLVSPSLPAKYLSASDEDLIHQVLADGANNLVPTQDTLLETDLLTSLSSVPGEKTETLILQTVGEERPASMGLSWEQSPVTRLSRTGLVEGFQKRLLPAWCAPLAHGLSLLLVAVAVAVSGWIGASFPPSVSVMWLLSSSSSFLASFLGWEPLKVLLEALYFSLVAKRLHPDEDDTLVESPAVTPVSERVPRVRPPHGFALFLAKEEARKVKRLHDMLKRLLVYMLFLLVTLLANYGDASCHGHAYRLQSAIKQELDSQAFLAITRSDEFWPWMSHVFLPYVHGNQSSPELGPPRLRQVRLQEAFCPDPSSSEHMCSAAGSLSTSDYGIGWQSVVQNGSETWAYSAPDLLGAWYWGYCAVYDSGGYIQELGLSLEESRARLGFLQLHNWLDSRSRAVFVELTRYSPAVGLHAAVTLRLEFPVAGHALAAFSVRPFALRRLSTGLSLPLLTSVCLLLFALYFSMAEVQTWRKDGCACTARPDTWARCLLVILTAATGLVRLAQLGIADRQWTHFVQDHPRHFTSFDQVAQLGSVARGLAASLLFLLLVKAAQQLRFVRQWSVFGKTLCRALPELMGATLGLVLLGVAYAQMAILLISSGADTLYNMARAFLVLCPGARVPTLCPSESWYLSPLLCVGLWALRVWGALRLGAILLRWRYHALRGELYRPAWEPQDYEMVELFLRRLRLWMGFSKVKEFRHKVRFEGMDPLPSRSSRGSKSSPVVLPPSSGSEASHPSTSSSQPDGPSASLSRSTLKLEPEPSRLHAVFESLLVQFDRLNQATEDVYQLEQQLQSLQGHGHNGPPSSPSPGCFPGSQPALPSRLSRASQGLDQTVGPNRVSLWPNNKVHPSST | ||||||
Glycosylation | 50 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 89 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 116 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 121 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 187 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 239 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 370 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 436↔529 | |||||
Sequence: CRTWAGAALAMVDSPAIQHFLVSKVTRSLDVWIGFSSVEGTEGLDPRGEAFSLESCQNWLPGEPHPATAEHCVRLGPAGQCNTDLCSAPHSYVC | ||||||
Disulfide bond | 507↔521 | |||||
Sequence: CVRLGPAGQCNTDLC | ||||||
Glycosylation | 627 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 635↔648 | |||||
Sequence: CVPEELWCPGANVC | ||||||
Disulfide bond | 642↔660 | |||||
Sequence: CPGANVCIPFDASCNSHVC | ||||||
Glycosylation | 662 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 740 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 804 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 835 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 848 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 859 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 884 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 915 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 998 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1004 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1028 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1084 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1096 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1107 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1172 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1188 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1234 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1263 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1330 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1342 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1376 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1444 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1449 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1468 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1535 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1548 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1557 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1643 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1657 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1706 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1730 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1788 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1831 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1863 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1876 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1987 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2046 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2070 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2121 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2244 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2349 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2391 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2408 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2414 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2563 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2640 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2713 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2749 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2813 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2836 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2873 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2948 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2986 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 3007↔3035 | |||||
Sequence: CQYFSEEMMMWRTEGIVPLEETSPSQAVC | ||||||
Glycosylation | 3728 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 3780 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 4156 | Phosphoserine; by PRKX; in vitro | ||||
Sequence: S |
Post-translational modification
N-glycosylated.
After synthesis, undergoes autoproteolytic cleavage between Leu-3040 and Thr-3041 in the GPS region of the GAIN-B domain (PubMed:25405894).
Cleavage at the GPS region occurs through a cis-autoproteolytic mechanism involving an ester-intermediate via N-O acyl rearrangement (By similarity).
This process takes place in the early secretory pathway, depends on initial N-glycosylation, and requires the REJ domain (By similarity).
PKD1 is ubiquitously and incompletely cleaved in wild-type mice, so that uncleaved and cleaved PKD1 molecules coexist. The differential patterns of cleavage during embryonic development, as well as in adult mice, suggest different functions of uncleaved and cleaved molecules (PubMed:18003909).
Cleavage at the GPS region occurs through a cis-autoproteolytic mechanism involving an ester-intermediate via N-O acyl rearrangement (By similarity).
This process takes place in the early secretory pathway, depends on initial N-glycosylation, and requires the REJ domain (By similarity).
PKD1 is ubiquitously and incompletely cleaved in wild-type mice, so that uncleaved and cleaved PKD1 molecules coexist. The differential patterns of cleavage during embryonic development, as well as in adult mice, suggest different functions of uncleaved and cleaved molecules (PubMed:18003909).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Component of the heterotetrameric polycystin channel complex with PKD2; the tetramer contains one PKD1 chain and three PKD2 chains (By similarity).
Interacts with PKD2; the interaction is required for ciliary localization (PubMed:25405894).
Interacts with PKD2L1 (PubMed:15548533).
Interacts with PRKX; involved in differentiation and controlled morphogenesis of the kidney. Interacts (via extracellular domain) with WNT3A, WNT4 and WNT9B (By similarity).
Interacts with WNT5A, DVL1 and DVL2 (PubMed:27214281).
Interacts with NPHP1 (via SH3 domain) (PubMed:20856870).
Interacts with BBS1, BBS4, BBS5 and TTC8. Interacts with RGS7 (By similarity).
Interacts (via C-terminal domain) with RABEP1; the interaction connects PKD1:PKD2 to GGA1 and ARL3 that mediate the ciliary targeting (PubMed:25405894).
Interacts (via the PKD repeats in the N-terminal extracellular region) with EPCIP; the interaction is not dependent on N-glycosylation of either protein (By similarity).
Interacts with PKD2; the interaction is required for ciliary localization (PubMed:25405894).
Interacts with PKD2L1 (PubMed:15548533).
Interacts with PRKX; involved in differentiation and controlled morphogenesis of the kidney. Interacts (via extracellular domain) with WNT3A, WNT4 and WNT9B (By similarity).
Interacts with WNT5A, DVL1 and DVL2 (PubMed:27214281).
Interacts with NPHP1 (via SH3 domain) (PubMed:20856870).
Interacts with BBS1, BBS4, BBS5 and TTC8. Interacts with RGS7 (By similarity).
Interacts (via C-terminal domain) with RABEP1; the interaction connects PKD1:PKD2 to GGA1 and ARL3 that mediate the ciliary targeting (PubMed:25405894).
Interacts (via the PKD repeats in the N-terminal extracellular region) with EPCIP; the interaction is not dependent on N-glycosylation of either protein (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | O08852 | PKD2 Q13563-1 | 2 | EBI-6666305, EBI-9837017 |
Protein-protein interaction databases
Miscellaneous
Family & Domains
Features
Showing features for domain, repeat, region, compositional bias, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 24-67 | LRRNT | ||||
Sequence: GDPGRGCGPCPLPCFCGPAPDAACRVNCSGRWLQTLGPSLRIPA | ||||||
Repeat | 68-91 | LRR 1 | ||||
Sequence: DATALDLSHNLLQTLDIGLLVNLS | ||||||
Repeat | 92-113 | LRR 2 | ||||
Sequence: ALVELDLSNNRISTLEEGVFAN | ||||||
Domain | 125-178 | LRRCT | ||||
Sequence: NPFECNCGLAWLPRWAKEHQVHVVQSEATTCRGPIPLAGQPLLSIPLLDNACGE | ||||||
Domain | 177-271 | WSC | ||||
Sequence: GEEYVACLPDNSSGAVAAVPFYFAHEGPLETEACSAFCFSAGEGLAALSEQNQCLCGAGQASNSSAACSSWCSSISLSLNSACGGPTLLQHTFPA | ||||||
Domain | 272-359 | PKD 1 | ||||
Sequence: SPGATLVGPHGPLASGQPADFHITSSLPISSTRWNFGDGSPEVDMASPAATHFYVLPGSYHMTVVLALGAGSALLETEVQVEATPTVL | ||||||
Domain | 415-530 | C-type lectin | ||||
Sequence: GNGHCYRLVAEKAPWLQAQEQCRTWAGAALAMVDSPAIQHFLVSKVTRSLDVWIGFSSVEGTEGLDPRGEAFSLESCQNWLPGEPHPATAEHCVRLGPAGQCNTDLCSAPHSYVCE | ||||||
Region | 613-632 | Disordered | ||||
Sequence: GGAAAVPEGSSEPDNRTEPA | ||||||
Domain | 633-666 | LDL-receptor class A; atypical | ||||
Sequence: PKCVPEELWCPGANVCIPFDASCNSHVCINGSVS | ||||||
Domain | 849-922 | PKD 2 | ||||
Sequence: ATATAQWFGGNISAPFEDACPPEVDFLKQDCTEEANGTLFSVLMLPRLKEGDHTVEIVAQNGASQANLSLRVTA | ||||||
Domain | 929-1014 | PKD 3 | ||||
Sequence: LRAVPSPEARVLQGILVRYSPMVEAGSDVAFRWTIDDKQSLTFHNTVFNVIYQSAAIFKLSLTASNHVSNITVNYNVTVERMNKMH | ||||||
Domain | 1017-1123 | PKD 4 | ||||
Sequence: WVSAVPTVLPPNATLALTGGVLVDSAVEVAFLWNFGDGEQVLRQFKPPYDESFQVPDPTVAQVLVEHNTTHIYTTPGEYNLTVLVSNTYENLTQQVTVSVRTVLPNV | ||||||
Domain | 1121-1209 | PKD 5 | ||||
Sequence: PNVAIGMSSNVLVAGQPITFSPYPLPSTDGVLYTWDFGDGSPVLIQSQPVLNHTYSMTGAYRITLEVNNTVSSVTAHADIRVFQELHGL | ||||||
Domain | 1207-1292 | PKD 6 | ||||
Sequence: HGLTVYLSPSVEQGAPMVVSASVESGDNITWTFDMGDGTVFTGPEATVQHVYLRAQNFTVTVEAANPAGHLSQSLHVQVFVLEVLH | ||||||
Domain | 1288-1377 | PKD 7 | ||||
Sequence: LEVLHIEPSTCIPTQPSAQLMAHVTGDPVHYLFDWTFGDGSSNVTVHGHPSVTHNFTRSGIFPLALVLSSHVNKAHYFTSICVEPEIRNI | ||||||
Domain | 1376-1463 | PKD 8 | ||||
Sequence: NITLQPERQFVKLGDEARLVAYSWPPFPYRYTWDFGTEDTTHTQTGGSEVKFIYREPGSYLVIVTVSNNISSTNDSAFVEVQEPVLVT | ||||||
Domain | 1462-1545 | PKD 9 | ||||
Sequence: VTGIRINGSHVLELQQPYLLSAMGSGSPATYLWELGDGSQSEGPEVTHIYSSTGDFTVRVSGWNEVSRSEAQLNITVKQRVRGL | ||||||
Domain | 1544-1629 | PKD 10 | ||||
Sequence: GLTINASRTVVPLNGSVSFSTLLEVGSDVHYSWVLCDRCTPIPGGPTISYTFRSVGTFNIIVTAENEVGSAQDSIFIYVLQFIEGL | ||||||
Domain | 1630-1718 | PKD 11 | ||||
Sequence: QVAGGDNGCCFPTNYTLQLQAAVRDGTNISYSWTAQQEGSLITLFGSGKCFSLTSLKASTYYVHLRATNMLGSAAANRTIDFVEPVESL | ||||||
Domain | 1716-1802 | PKD 12 | ||||
Sequence: ESLILSASPNPAAVNMSLTLCAELAGGSGVVYTWYLEEGLSWKTSMPSTTHTFAAPGLHLVRVTAENQLGSVNATVEVAIQVPVGGL | ||||||
Domain | 1804-1886 | PKD 13 | ||||
Sequence: IRTSEPDSIFVAAGSTLPFWGQLAEGTNVTWCWTLPGGSKDSQYIAVRFSTAGSFSLQLNASNAVSWVSAMYNLTVEEPIVNL | ||||||
Domain | 1885-1970 | PKD 14 | ||||
Sequence: NLMLWASSKVVAPGQPVHFEILLAAGSALTFRLQVGGSVPEVLPSPHFSHSFFRVGDHLVNVQAENHVSHAQAQVRILVLEAVVGL | ||||||
Domain | 1972-2053 | PKD 15 | ||||
Sequence: VPNCCEPGMATGTEKNFTARVQRGSRVAYAWYFSLQKVQGDSLVILSGRDVTYTPVAAGLLEIHVRAFNELGGVNLTLMVEV | ||||||
Domain | 2056-2144 | PKD 16 | ||||
Sequence: IIQYVTLQSGRCFTNRSARFEAATSPSPRRVTYHWDFGDGTPVQKTEEFWADHYYLRPGDYHVEVNATNLVSFFVAQATVTVQVLACRE | ||||||
Domain | 2142-2828 | REJ | ||||
Sequence: CREPEVEVALPLQVLMRRSQRNYLEAHVDLRNCVSYQTEYRWEIYRTASCQRPGRMAQMVLPGVDVSRPQLVVPRLALPVGHYCFVFVVSFGDTPLARSIQANVTVAAERLVPIIEGGSYRVWSDTQDLVLDGSKSYDPNLEDGDQTPLNFHWACVASTQSETGGCVLNFGPRGSSVVTIPLERLEAGVEYTFNLIVWKAGRKEEATNQTVLIRSGRVPIVSLECVSCKAQAVYEVSRSSYVYLEGHCHNCSRGYKQGCWAARTFSNKTLVLNETTTSTGSTGMNLVVRPGALRDGEGYIFTLTVLGHSGEEEGCASIRLSPNRPPLGGSCRLFPLDSVRGLTTKVHFECTGWRDAEDGGAPLVYALLLKRCRQSYCENFCIYKGSLSTYGAVLPPGFQPLFVVSLAVVVQDQLGAAVVALNRSLTIVLPEPSGNPADLVPWLHSLTASVLPGLLKQADPQHVIEYSLALITVLNEYEQAPDVSEPNVEQQLRAQMRKNITETLISLRVNTVDDIQQITAALAQCMVSSRELMCRSCLKKMLQKLEGMMRILQAETTEGTLTPTTIADSILNITGDLIHLASLDMQGPQPLELGVEPPSLMVASKAYNLSSALMRILMRSRVLNEEPLTLAGEEIVALGKRSDPLSLLCYGKALGPSCHFSIPEAFSGALSNLSDVVQLIFLVDSNP | ||||||
Domain | 2857-3055 | GAIN-B | ||||
Sequence: PIEQLAAERAITVKVPNNSDQAAQSSHNPVGSTIVQPQTSVSAVVTADNSNPQAGLHLRITYTVLNERYLSAEPEPYLAVYLHSVSQPNEYNCSASRRISLEVLEGADHRLYTFFIAPGTGTLDRSYYLNLTSHFHWSALEVSVGLYTSLCQYFSEEMMMWRTEGIVPLEETSPSQAVCLTRHLTAFGASLFVPPSHVQ | ||||||
Region | 3007-3055 | GPS | ||||
Sequence: CQYFSEEMMMWRTEGIVPLEETSPSQAVCLTRHLTAFGASLFVPPSHVQ | ||||||
Domain | 3110-3225 | PLAT | ||||
Sequence: FKYEILVKTGWSRGSGTTAHVGIMLYGEDNRSGHRHLDGDRAFHRNSLDIFQIATPHSLGSVWKIRVWHDNKGLSPAWFLQHIIVRDLQSARSTFFLVNDWLSVETEANGGLVEKE | ||||||
Region | 4150-4197 | Disordered | ||||
Sequence: PLPSRSSRGSKSSPVVLPPSSGSEASHPSTSSSQPDGPSASLSRSTLK | ||||||
Compositional bias | 4154-4197 | Polar residues | ||||
Sequence: RSSRGSKSSPVVLPPSSGSEASHPSTSSSQPDGPSASLSRSTLK | ||||||
Coiled coil | 4210-4241 | |||||
Sequence: ESLLVQFDRLNQATEDVYQLEQQLQSLQGHGH | ||||||
Region | 4235-4293 | Disordered | ||||
Sequence: SLQGHGHNGPPSSPSPGCFPGSQPALPSRLSRASQGLDQTVGPNRVSLWPNNKVHPSST | ||||||
Compositional bias | 4261-4293 | Polar residues | ||||
Sequence: PSRLSRASQGLDQTVGPNRVSLWPNNKVHPSST |
Domain
The LDL-receptor class A domain is atypical; the potential calcium-binding site is missing.
Sequence similarities
Belongs to the polycystin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length4,293
- Mass (Da)466,577
- Last updated2011-07-27 v2
- ChecksumFA12403171DBBCE0
Computationally mapped potential isoform sequences
There are 7 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A2I3BPP4 | A0A2I3BPP4_MOUSE | Pkd1 | 237 | ||
A0A2I3BQ02 | A0A2I3BQ02_MOUSE | Pkd1 | 80 | ||
A0A2I3BQE7 | A0A2I3BQE7_MOUSE | Pkd1 | 27 | ||
A0A2I3BQG6 | A0A2I3BQG6_MOUSE | Pkd1 | 72 | ||
A0A2I3BRL4 | A0A2I3BRL4_MOUSE | Pkd1 | 234 | ||
A0A2I3BRP8 | A0A2I3BRP8_MOUSE | Pkd1 | 27 | ||
A0A2I3BRZ6 | A0A2I3BRZ6_MOUSE | Pkd1 | 1231 |
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 3 | in Ref. 1; AAC53207 | ||||
Sequence: L → P | ||||||
Sequence conflict | 771 | in Ref. 1; AAC53207 | ||||
Sequence: R → Q | ||||||
Sequence conflict | 871 | in Ref. 1; AAC53207 | ||||
Sequence: E → D | ||||||
Sequence conflict | 1180 | in Ref. 1; AAC53207 | ||||
Sequence: A → T | ||||||
Sequence conflict | 1292 | in Ref. 1; AAC53207 | ||||
Sequence: H → R | ||||||
Sequence conflict | 1632 | in Ref. 1; AAC53207 | ||||
Sequence: A → V | ||||||
Sequence conflict | 1684 | in Ref. 1; AAC53207 | ||||
Sequence: S → A | ||||||
Sequence conflict | 1770 | in Ref. 1; AAC53207 | ||||
Sequence: A → T | ||||||
Sequence conflict | 2085 | in Ref. 1; AAC53207 | ||||
Sequence: R → C | ||||||
Sequence conflict | 2507 | in Ref. 1; AAC53207 | ||||
Sequence: A → V | ||||||
Sequence conflict | 3956 | in Ref. 1; AAC53207 | ||||
Sequence: F → C | ||||||
Sequence conflict | 3962 | in Ref. 1; AAC53207 | ||||
Sequence: R → H | ||||||
Compositional bias | 4154-4197 | Polar residues | ||||
Sequence: RSSRGSKSSPVVLPPSSGSEASHPSTSSSQPDGPSASLSRSTLK | ||||||
Sequence conflict | 4237 | in Ref. 1; AAC53207 | ||||
Sequence: Q → R | ||||||
Compositional bias | 4261-4293 | Polar residues | ||||
Sequence: PSRLSRASQGLDQTVGPNRVSLWPNNKVHPSST |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U70209 EMBL· GenBank· DDBJ | AAC53207.1 EMBL· GenBank· DDBJ | mRNA | ||
AC132367 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |