Q9R0M0 · CELR2_MOUSE
- ProteinCadherin EGF LAG seven-pass G-type receptor 2
- GeneCelsr2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2919 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Receptor that may have an important role in cell/cell signaling during nervous system formation.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 2356-2357 | Cleavage; by autolysis | ||||
Sequence: MT |
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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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | plasma membrane | |
Molecular Function | calcium ion binding | |
Molecular Function | G protein-coupled receptor activity | |
Biological Process | cerebrospinal fluid secretion | |
Biological Process | cilium assembly | |
Biological Process | cilium movement | |
Biological Process | homophilic cell adhesion via plasma membrane adhesion molecules | |
Biological Process | motor neuron migration | |
Biological Process | neural plate anterior/posterior regionalization | |
Biological Process | regulation of DNA-templated transcription | |
Biological Process | regulation of protein localization | |
Biological Process | ventricular system development | |
Biological Process | Wnt signaling pathway |
Keywords
- Molecular function
- Ligand
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCadherin EGF LAG seven-pass G-type receptor 2
- 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 accessionQ9R0M0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 32-2380 | Extracellular | ||||
Sequence: DQVGPCRSLGSGGRSSSGACAPVGWLCPASASNLWLYTSRCRESGIELTGHLVPHHDGLRVWCPESGAHIPLPPSSEGCPWSCRLLGIGGHLSPQGTLTLPEEHPCLKAPRLRCQSCKLAQAPGLRAGEGSPEESLGGRRKRNVNTAPQFQPPSYQATVPENQPAGTSVASLRAIDPDEGEAGRLEYTMDALFDSRSNHFFSLDPITGVVTTAEELDRETKSTHVFRVTAQDHGMPRRSALATLTILVTDTNDHDPVFEQQEYKESLRENLEVGYEVLTVRATDGDAPPNANILYRLLEGAGGSPSDAFEIDPRSGVIRTRGPVDREEVESYKLTVEASDQGRDPGPRSSTAIVFLSVEDDNDNAPQFSEKRYVVQVREDVTPGAPVLRVTASDRDKGSNALVHYSIMSGNARGQFYLDAQTGALDVVSPLDYETTKEYTLRIRAQDGGRPPLSNVSGLVTVQVLDINDNAPIFVSTPFQATVLESVPLGYLVLHVQAIDADAGDNARLEYSLAGVGHDFPFTINNGTGWISVAAELDREEVDFYSFGVEARDHGTPALTASASVSVTILDVNDNNPTFTQPEYTVRLNEDAAVGTSVVTVSAVDRDAHSVITYQITSGNTRNRFSITSQSGGGLVSLALPLDYKLERQYVLAVTASDGTRQDTAQIVVNVTDANTHRPVFQSSHYTVNVNEDRPAGTTVVLISATDEDTGENARITYFMEDSIPQFRIDADTGAVTTQAELDYEDQVSYTLAITARDNGIPQKSDTTYLEILVNDVNDNAPQFLRDSYQGSVYEDVPPFTSVLQISATDRDSGLNGRVFYTFQGGDDGDGDFIVESTSGIVRTLRRLDRENVAQYVLRAYAVDKGMPPARTPMEVTVTVLDVNDNPPVFEQDEFDVFVEENSPIGLAVARVTATDPDEGTNAQIMYQIVEGNIPEVFQLDIFSGELTALVDLDYEDRPEYVLVIQATSAPLVSRATVHVRLLDRNDNPPVLGNFEILFNNYVTNRSSSFPGGAIGRVPAHDPDISDSLTYSFERGNELSLVLLNASTGELRLSRALDNNRPLEAIMSVLVSDGVHSVTAQCSLRVTIITDEMLTHSITLRLEDMSPERFLSPLLGLFIQAVAATLATPPDHVVVFNVQRDTDAPGGHILNVSLSVGQPPGPGGGPPFLPSEDLQERLYLNRSLLTAISAQRVLPFDDNICLREPCENYMRCVSVLRFDSSAPFIASSSVLFRPIHPVGGLRCRCPPGFTGDYCETEVDLCYSRPCGPHGRCRSREGGYTCLCLDGYTGEHCEASTHSGRCTPGVCKNGGTCVNLLVGGFKCDCPSGDFEKPFCQVTTRSFPARSFITFRGLRQRFHFTLALSFATKERNGLLLYNGRFNEKHDFVALEVIQEQVQLTFSAGESTTTVSPFVPGGVSDGQWHTVQLKYYNKPLLGQTGLPQGPSEQKVAVVSVDGCDTGVALRFGAMLGNYSCAAQGTQGGSKKSLDLTGPLLLGGVPDLPESFPVRMRHFVGCMKDLQVDSRHIDMADFIANNGTVPGCPTKKIVCDSSICHNGGTCVNQWNAFSCECPLGFGGKSCAQEMANPQRFLGSSLVAWHGLSLPISQPWHLSLMFRTRQADGVLLQAVTRGRSTITLQLRAGHVVLSVEGTGLQASSLRLEPGRANDGDWHHAQLALGASGGPGHAILSFDYGQQKAEGNLGPRLHGLHLSNITVGGVPGPASGVARGFRGCLQGVRVSETPEGISSLDPSRGESINVEPGCSWPDPCDSNPCPTNSYCSNDWDSYSCSCVLGYYGDNCTNVCDLNPCEHQSVCTRKPNTPHGYICECLPNYLGPYCETRIDQPCPRGWWGHPTCGPCNCDVSKGFDPDCNKTSGECHCKENHYRPPGSPTCLLCDCYPTGSLSRVCDPEDGQCPCKPGVIGRQCDRCDNPFAEVTTNGCEVNYDSCPRAIEAGIWWPRTRFGLPAAAPCPKGSFGTAVRHCDEHRGWLPPNLFNCTSVTFSELKGFAERLQRNESGLDSGRSQRLALLLRNATQHTSGYFGSDVKVAYQLATRLLAHESAQRGFGLSATQDVHFTENLLRVGSALLDAANKRHWELIQQTEGGTAWLLQHYEAYASALAQNMRHTYLSPFTIVTPNIVISVVRLDKGNFAGTKLPRYEALRGERPPDLETTVILPESVFREMPSMVRSAGPGEAQETEELARRQRRHPELSQGEAVASVIIYHTLAGLLPHNYDPDKRSLRVPKRPVINTPVVSISVHDDEELLPRALDKPVTVQFRLLETEERTKPICVFWNHSILVSGTGGWSARGCEVVFRNESHVSCQCNHMTSFAVLMDMSRRENGEILPLKTLT | ||||||
Transmembrane | 2381-2401 | Helical; Name=1 | ||||
Sequence: YVALGVTLAALMLTFLFLTLL | ||||||
Topological domain | 2402-2413 | Cytoplasmic | ||||
Sequence: RALRSNQHGIRR | ||||||
Transmembrane | 2414-2433 | Helical; Name=2 | ||||
Sequence: NLTAALGLAQLVFLLGINQA | ||||||
Topological domain | 2434-2438 | Extracellular | ||||
Sequence: DLPFA | ||||||
Transmembrane | 2439-2459 | Helical; Name=3 | ||||
Sequence: CTVIAILLHFLYLCTFSWALL | ||||||
Topological domain | 2460-2480 | Cytoplasmic | ||||
Sequence: EALHLYRALTEVRDVNASPMR | ||||||
Transmembrane | 2481-2501 | Helical; Name=4 | ||||
Sequence: FYYMLGWGVPAFITGLAVGLD | ||||||
Topological domain | 2502-2518 | Extracellular | ||||
Sequence: PEGYGNPDFCWLSVYDT | ||||||
Transmembrane | 2519-2539 | Helical; Name=5 | ||||
Sequence: LIWSFAGPVAFAVSMSVFLYI | ||||||
Topological domain | 2540-2563 | Cytoplasmic | ||||
Sequence: LSARASCAAQRQGFEKKGPVSGLR | ||||||
Transmembrane | 2564-2584 | Helical; Name=6 | ||||
Sequence: SSFTVLLLLSATWLLALLSVN | ||||||
Topological domain | 2585-2591 | Extracellular | ||||
Sequence: SDTLLFH | ||||||
Transmembrane | 2592-2612 | Helical; Name=7 | ||||
Sequence: YLFAACNCVQGPFIFLSYVVL | ||||||
Topological domain | 2613-2919 | Cytoplasmic | ||||
Sequence: SKEVRKALKFACSRKPSPDPALTTKSTLTSSYNCPSPYADGRLYQPYGDSAGSLHSASRSGKSQPSYIPFLLREESTLNPGQVPPGLGDPSGLFLEGQAQQHDPDTDSDSDLSLEDDQSGSYASTHSSDSEEEEEEAAFPGEQGWDSLLGPGAERLPLHSTPKDGGPGSGKVPWLGDFGTTTKENSGSGPLEERPRENGDALTREGSLGPLPGPSTQPHKGILKKKCLPTISEKSSLLRLPLEQGTGSSRGSSISEGSRHGPPPRPPPRQSLQEQLNGVMPVAMSIKAGTVDEDSSGSEFLFFNFLH |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-31 | |||||
Sequence: MRSRAASAPLPTPLLPLLLLLLLLPPSPLLG | ||||||
Chain | PRO_0000012917 | 32-2919 | Cadherin EGF LAG seven-pass G-type receptor 2 | |||
Sequence: DQVGPCRSLGSGGRSSSGACAPVGWLCPASASNLWLYTSRCRESGIELTGHLVPHHDGLRVWCPESGAHIPLPPSSEGCPWSCRLLGIGGHLSPQGTLTLPEEHPCLKAPRLRCQSCKLAQAPGLRAGEGSPEESLGGRRKRNVNTAPQFQPPSYQATVPENQPAGTSVASLRAIDPDEGEAGRLEYTMDALFDSRSNHFFSLDPITGVVTTAEELDRETKSTHVFRVTAQDHGMPRRSALATLTILVTDTNDHDPVFEQQEYKESLRENLEVGYEVLTVRATDGDAPPNANILYRLLEGAGGSPSDAFEIDPRSGVIRTRGPVDREEVESYKLTVEASDQGRDPGPRSSTAIVFLSVEDDNDNAPQFSEKRYVVQVREDVTPGAPVLRVTASDRDKGSNALVHYSIMSGNARGQFYLDAQTGALDVVSPLDYETTKEYTLRIRAQDGGRPPLSNVSGLVTVQVLDINDNAPIFVSTPFQATVLESVPLGYLVLHVQAIDADAGDNARLEYSLAGVGHDFPFTINNGTGWISVAAELDREEVDFYSFGVEARDHGTPALTASASVSVTILDVNDNNPTFTQPEYTVRLNEDAAVGTSVVTVSAVDRDAHSVITYQITSGNTRNRFSITSQSGGGLVSLALPLDYKLERQYVLAVTASDGTRQDTAQIVVNVTDANTHRPVFQSSHYTVNVNEDRPAGTTVVLISATDEDTGENARITYFMEDSIPQFRIDADTGAVTTQAELDYEDQVSYTLAITARDNGIPQKSDTTYLEILVNDVNDNAPQFLRDSYQGSVYEDVPPFTSVLQISATDRDSGLNGRVFYTFQGGDDGDGDFIVESTSGIVRTLRRLDRENVAQYVLRAYAVDKGMPPARTPMEVTVTVLDVNDNPPVFEQDEFDVFVEENSPIGLAVARVTATDPDEGTNAQIMYQIVEGNIPEVFQLDIFSGELTALVDLDYEDRPEYVLVIQATSAPLVSRATVHVRLLDRNDNPPVLGNFEILFNNYVTNRSSSFPGGAIGRVPAHDPDISDSLTYSFERGNELSLVLLNASTGELRLSRALDNNRPLEAIMSVLVSDGVHSVTAQCSLRVTIITDEMLTHSITLRLEDMSPERFLSPLLGLFIQAVAATLATPPDHVVVFNVQRDTDAPGGHILNVSLSVGQPPGPGGGPPFLPSEDLQERLYLNRSLLTAISAQRVLPFDDNICLREPCENYMRCVSVLRFDSSAPFIASSSVLFRPIHPVGGLRCRCPPGFTGDYCETEVDLCYSRPCGPHGRCRSREGGYTCLCLDGYTGEHCEASTHSGRCTPGVCKNGGTCVNLLVGGFKCDCPSGDFEKPFCQVTTRSFPARSFITFRGLRQRFHFTLALSFATKERNGLLLYNGRFNEKHDFVALEVIQEQVQLTFSAGESTTTVSPFVPGGVSDGQWHTVQLKYYNKPLLGQTGLPQGPSEQKVAVVSVDGCDTGVALRFGAMLGNYSCAAQGTQGGSKKSLDLTGPLLLGGVPDLPESFPVRMRHFVGCMKDLQVDSRHIDMADFIANNGTVPGCPTKKIVCDSSICHNGGTCVNQWNAFSCECPLGFGGKSCAQEMANPQRFLGSSLVAWHGLSLPISQPWHLSLMFRTRQADGVLLQAVTRGRSTITLQLRAGHVVLSVEGTGLQASSLRLEPGRANDGDWHHAQLALGASGGPGHAILSFDYGQQKAEGNLGPRLHGLHLSNITVGGVPGPASGVARGFRGCLQGVRVSETPEGISSLDPSRGESINVEPGCSWPDPCDSNPCPTNSYCSNDWDSYSCSCVLGYYGDNCTNVCDLNPCEHQSVCTRKPNTPHGYICECLPNYLGPYCETRIDQPCPRGWWGHPTCGPCNCDVSKGFDPDCNKTSGECHCKENHYRPPGSPTCLLCDCYPTGSLSRVCDPEDGQCPCKPGVIGRQCDRCDNPFAEVTTNGCEVNYDSCPRAIEAGIWWPRTRFGLPAAAPCPKGSFGTAVRHCDEHRGWLPPNLFNCTSVTFSELKGFAERLQRNESGLDSGRSQRLALLLRNATQHTSGYFGSDVKVAYQLATRLLAHESAQRGFGLSATQDVHFTENLLRVGSALLDAANKRHWELIQQTEGGTAWLLQHYEAYASALAQNMRHTYLSPFTIVTPNIVISVVRLDKGNFAGTKLPRYEALRGERPPDLETTVILPESVFREMPSMVRSAGPGEAQETEELARRQRRHPELSQGEAVASVIIYHTLAGLLPHNYDPDKRSLRVPKRPVINTPVVSISVHDDEELLPRALDKPVTVQFRLLETEERTKPICVFWNHSILVSGTGGWSARGCEVVFRNESHVSCQCNHMTSFAVLMDMSRRENGEILPLKTLTYVALGVTLAALMLTFLFLTLLRALRSNQHGIRRNLTAALGLAQLVFLLGINQADLPFACTVIAILLHFLYLCTFSWALLEALHLYRALTEVRDVNASPMRFYYMLGWGVPAFITGLAVGLDPEGYGNPDFCWLSVYDTLIWSFAGPVAFAVSMSVFLYILSARASCAAQRQGFEKKGPVSGLRSSFTVLLLLSATWLLALLSVNSDTLLFHYLFAACNCVQGPFIFLSYVVLSKEVRKALKFACSRKPSPDPALTTKSTLTSSYNCPSPYADGRLYQPYGDSAGSLHSASRSGKSQPSYIPFLLREESTLNPGQVPPGLGDPSGLFLEGQAQQHDPDTDSDSDLSLEDDQSGSYASTHSSDSEEEEEEAAFPGEQGWDSLLGPGAERLPLHSTPKDGGPGSGKVPWLGDFGTTTKENSGSGPLEERPRENGDALTREGSLGPLPGPSTQPHKGILKKKCLPTISEKSSLLRLPLEQGTGSSRGSSISEGSRHGPPPRPPPRQSLQEQLNGVMPVAMSIKAGTVDEDSSGSEFLFFNFLH | ||||||
Glycosylation | 486 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 557 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 701 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1036 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1076 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1182 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1212 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1292↔1303 | |||||
Sequence: CYSRPCGPHGRC | ||||||
Disulfide bond | 1297↔1312 | |||||
Sequence: CGPHGRCRSREGGYTC | ||||||
Disulfide bond | 1314↔1323 | |||||
Sequence: CLDGYTGEHC | ||||||
Disulfide bond | 1332↔1343 | |||||
Sequence: CTPGVCKNGGTC | ||||||
Disulfide bond | 1337↔1353 | |||||
Sequence: CKNGGTCVNLLVGGFKC | ||||||
Disulfide bond | 1355↔1365 | |||||
Sequence: CPSGDFEKPFC | ||||||
Glycosylation | 1501 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1545↔1571 | |||||
Sequence: CMKDLQVDSRHIDMADFIANNGTVPGC | ||||||
Glycosylation | 1565 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1578↔1589 | |||||
Sequence: CDSSICHNGGTC | ||||||
Disulfide bond | 1583↔1598 | |||||
Sequence: CHNGGTCVNQWNAFSC | ||||||
Modified residue | 1591 | (3R)-3-hydroxyasparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1600↔1609 | |||||
Sequence: CPLGFGGKSC | ||||||
Glycosylation | 1741 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1791↔1802 | |||||
Sequence: CSWPDPCDSNPC | ||||||
Disulfide bond | 1797↔1817 | |||||
Sequence: CDSNPCPTNSYCSNDWDSYSC | ||||||
Disulfide bond | 1819↔1828 | |||||
Sequence: CVLGYYGDNC | ||||||
Glycosylation | 1827 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1832↔1843 | |||||
Sequence: CDLNPCEHQSVC | ||||||
Disulfide bond | 1837↔1855 | |||||
Sequence: CEHQSVCTRKPNTPHGYIC | ||||||
Disulfide bond | 1857↔1866 | |||||
Sequence: CLPNYLGPYC | ||||||
Disulfide bond | 1887↔1899 | |||||
Sequence: CNCDVSKGFDPDC | ||||||
Disulfide bond | 1889↔1906 | |||||
Sequence: CDVSKGFDPDCNKTSGEC | ||||||
Glycosylation | 1900 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1908↔1921 | |||||
Sequence: CKENHYRPPGSPTC | ||||||
Disulfide bond | 1924↔1936 | |||||
Sequence: CDCYPTGSLSRVC | ||||||
Disulfide bond | 1926↔1943 | |||||
Sequence: CYPTGSLSRVCDPEDGQC | ||||||
Disulfide bond | 1945↔1954 | |||||
Sequence: CKPGVIGRQC | ||||||
Disulfide bond | 1957↔1969 | |||||
Sequence: CDNPFAEVTTNGC | ||||||
Glycosylation | 2024 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2043 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2061 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2319↔2351 | |||||
Sequence: CVFWNHSILVSGTGGWSARGCEVVFRNESHVSC | ||||||
Glycosylation | 2323 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2339↔2353 | |||||
Sequence: CEVVFRNESHVSCQC | ||||||
Glycosylation | 2345 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.
Autoproteolytically processed at the GPS region of the GAIN-B domain; this cleavage modulates receptor activity.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in the CNS and in the eye.
Developmental stage
Predominantly expressed in the developing CNS, the emerging dorsal root ganglia and cranial ganglia. In the CNS, expression is uniform along the rostrocaudal axis. During gastrulation, it is expressed within the anterior neural ectoderm. At 10 dpc, expression is strong in the ventricular zones (VZ) in all sectors of the brain, and lower in the marginal zones (MZ). Between 12 and 15 dpc, expression is prominent in the brain. It is strong in VZ, lower in MZ, except in telecephalic MZ where it is predominant. The intensity is higher in all VZ, and lower in differentiating fields than in VZ, except in the cerebral hemispheres, and to a lesser extent in the tectum and cerebellum. A weak expression is also observed in the fetal lungs, kidney and epithelia. In the newborn and postnatal stages, expression remains restricted to the VZ as well as in migrating and postmigratory cells throughout the brain.
Gene expression databases
Interaction
Subunit
Heterodimer of 2 chains generated by proteolytic processing; the large extracellular N-terminal fragment and the membrane-bound C-terminal fragment predominantly remain associated and non-covalently linked.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | Q9R0M0 | atp6ap2.S Q7T0S3 | 2 | EBI-8294754, EBI-8294706 |
Protein-protein interaction databases
Miscellaneous
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 156-194 | Disordered | ||||
Sequence: LRAGEGSPEESLGGRRKRNVNTAPQFQPPSYQATVPENQ | ||||||
Compositional bias | 173-194 | Polar residues | ||||
Sequence: RNVNTAPQFQPPSYQATVPENQ | ||||||
Domain | 182-289 | Cadherin 1 | ||||
Sequence: QPPSYQATVPENQPAGTSVASLRAIDPDEGEAGRLEYTMDALFDSRSNHFFSLDPITGVVTTAEELDRETKSTHVFRVTAQDHGMPRRSALATLTILVTDTNDHDPVF | ||||||
Domain | 290-399 | Cadherin 2 | ||||
Sequence: EQQEYKESLRENLEVGYEVLTVRATDGDAPPNANILYRLLEGAGGSPSDAFEIDPRSGVIRTRGPVDREEVESYKLTVEASDQGRDPGPRSSTAIVFLSVEDDNDNAPQF | ||||||
Domain | 400-505 | Cadherin 3 | ||||
Sequence: SEKRYVVQVREDVTPGAPVLRVTASDRDKGSNALVHYSIMSGNARGQFYLDAQTGALDVVSPLDYETTKEYTLRIRAQDGGRPPLSNVSGLVTVQVLDINDNAPIF | ||||||
Domain | 506-610 | Cadherin 4 | ||||
Sequence: VSTPFQATVLESVPLGYLVLHVQAIDADAGDNARLEYSLAGVGHDFPFTINNGTGWISVAAELDREEVDFYSFGVEARDHGTPALTASASVSVTILDVNDNNPTF | ||||||
Domain | 611-712 | Cadherin 5 | ||||
Sequence: TQPEYTVRLNEDAAVGTSVVTVSAVDRDAHSVITYQITSGNTRNRFSITSQSGGGLVSLALPLDYKLERQYVLAVTASDGTRQDTAQIVVNVTDANTHRPVF | ||||||
Domain | 713-815 | Cadherin 6 | ||||
Sequence: QSSHYTVNVNEDRPAGTTVVLISATDEDTGENARITYFMEDSIPQFRIDADTGAVTTQAELDYEDQVSYTLAITARDNGIPQKSDTTYLEILVNDVNDNAPQF | ||||||
Domain | 816-921 | Cadherin 7 | ||||
Sequence: LRDSYQGSVYEDVPPFTSVLQISATDRDSGLNGRVFYTFQGGDDGDGDFIVESTSGIVRTLRRLDRENVAQYVLRAYAVDKGMPPARTPMEVTVTVLDVNDNPPVF | ||||||
Domain | 922-1023 | Cadherin 8 | ||||
Sequence: EQDEFDVFVEENSPIGLAVARVTATDPDEGTNAQIMYQIVEGNIPEVFQLDIFSGELTALVDLDYEDRPEYVLVIQATSAPLVSRATVHVRLLDRNDNPPVL | ||||||
Domain | 1028-1146 | Cadherin 9 | ||||
Sequence: ILFNNYVTNRSSSFPGGAIGRVPAHDPDISDSLTYSFERGNELSLVLLNASTGELRLSRALDNNRPLEAIMSVLVSDGVHSVTAQCSLRVTIITDEMLTHSITLRLEDMSPERFLSPLL | ||||||
Domain | 1228-1286 | EGF-like 1; atypical | ||||
Sequence: DDNICLREPCENYMRCVSVLRFDSSAPFIASSSVLFRPIHPVGGLRCRCPPGFTGDYCE | ||||||
Domain | 1288-1318 | EGF-like 2; calcium-binding | ||||
Sequence: EVDLCYSRPCGPHGRCRSREGGYTCLCLDGY | ||||||
Domain | 1328-1366 | EGF-like 3; calcium-binding | ||||
Sequence: HSGRCTPGVCKNGGTCVNLLVGGFKCDCPSGDFEKPFCQ | ||||||
Domain | 1367-1571 | Laminin G-like 1 | ||||
Sequence: VTTRSFPARSFITFRGLRQRFHFTLALSFATKERNGLLLYNGRFNEKHDFVALEVIQEQVQLTFSAGESTTTVSPFVPGGVSDGQWHTVQLKYYNKPLLGQTGLPQGPSEQKVAVVSVDGCDTGVALRFGAMLGNYSCAAQGTQGGSKKSLDLTGPLLLGGVPDLPESFPVRMRHFVGCMKDLQVDSRHIDMADFIANNGTVPGC | ||||||
Domain | 1574-1610 | EGF-like 4; calcium-binding | ||||
Sequence: KKIVCDSSICHNGGTCVNQWNAFSCECPLGFGGKSCA | ||||||
Domain | 1614-1791 | Laminin G-like 2 | ||||
Sequence: ANPQRFLGSSLVAWHGLSLPISQPWHLSLMFRTRQADGVLLQAVTRGRSTITLQLRAGHVVLSVEGTGLQASSLRLEPGRANDGDWHHAQLALGASGGPGHAILSFDYGQQKAEGNLGPRLHGLHLSNITVGGVPGPASGVARGFRGCLQGVRVSETPEGISSLDPSRGESINVEPGC | ||||||
Domain | 1787-1829 | EGF-like 5; calcium-binding | ||||
Sequence: VEPGCSWPDPCDSNPCPTNSYCSNDWDSYSCSCVLGYYGDNCT | ||||||
Domain | 1830-1867 | EGF-like 6; calcium-binding | ||||
Sequence: NVCDLNPCEHQSVCTRKPNTPHGYICECLPNYLGPYCE | ||||||
Domain | 1883-1922 | EGF-like 7; calcium-binding | ||||
Sequence: TCGPCNCDVSKGFDPDCNKTSGECHCKENHYRPPGSPTCL | ||||||
Domain | 1924-1971 | Laminin EGF-like | ||||
Sequence: CDCYPTGSLSRVCDPEDGQCPCKPGVIGRQCDRCDNPFAEVTTNGCEV | ||||||
Domain | 2199-2369 | GAIN-B | ||||
Sequence: ETTVILPESVFREMPSMVRSAGPGEAQETEELARRQRRHPELSQGEAVASVIIYHTLAGLLPHNYDPDKRSLRVPKRPVINTPVVSISVHDDEELLPRALDKPVTVQFRLLETEERTKPICVFWNHSILVSGTGGWSARGCEVVFRNESHVSCQCNHMTSFAVLMDMSRRE | ||||||
Region | 2216-2241 | Disordered | ||||
Sequence: VRSAGPGEAQETEELARRQRRHPELS | ||||||
Compositional bias | 2226-2240 | Basic and acidic residues | ||||
Sequence: ETEELARRQRRHPEL | ||||||
Region | 2319-2369 | GPS | ||||
Sequence: CVFWNHSILVSGTGGWSARGCEVVFRNESHVSCQCNHMTSFAVLMDMSRRE | ||||||
Region | 2690-2884 | Disordered | ||||
Sequence: LNPGQVPPGLGDPSGLFLEGQAQQHDPDTDSDSDLSLEDDQSGSYASTHSSDSEEEEEEAAFPGEQGWDSLLGPGAERLPLHSTPKDGGPGSGKVPWLGDFGTTTKENSGSGPLEERPRENGDALTREGSLGPLPGPSTQPHKGILKKKCLPTISEKSSLLRLPLEQGTGSSRGSSISEGSRHGPPPRPPPRQSL | ||||||
Compositional bias | 2849-2868 | Polar residues | ||||
Sequence: LLRLPLEQGTGSSRGSSISE |
Sequence similarities
Belongs to the G-protein coupled receptor 2 family. LN-TM7 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Protein family/group databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
Q9R0M0-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length2,919
- Mass (Da)316,986
- Last updated2019-04-10 v3
- ChecksumA8F35C88C5808300
Q9R0M0-2
- Name2
- Differences from canonical
- 2912-2919: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F7BHW1 | F7BHW1_MOUSE | Celsr2 | 900 |
Features
Showing features for sequence conflict, compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 3 | in Ref. 1; BAA84070 | ||||
Sequence: S → T | ||||||
Compositional bias | 173-194 | Polar residues | ||||
Sequence: RNVNTAPQFQPPSYQATVPENQ | ||||||
Sequence conflict | 334 | in Ref. 1; BAA84070 | ||||
Sequence: G → D | ||||||
Sequence conflict | 638 | in Ref. 1; BAA84070 | ||||
Sequence: D → H | ||||||
Sequence conflict | 721 | in Ref. 1; BAA84070 | ||||
Sequence: V → G | ||||||
Sequence conflict | 762 | in Ref. 1; BAA84070 | ||||
Sequence: A → G | ||||||
Sequence conflict | 823 | in Ref. 1; BAA84070 | ||||
Sequence: S → T | ||||||
Sequence conflict | 838 | in Ref. 1; BAA84070 | ||||
Sequence: S → L | ||||||
Sequence conflict | 914 | in Ref. 1; BAA84070 | ||||
Sequence: V → G | ||||||
Sequence conflict | 1222 | in Ref. 1; BAA84070 | ||||
Sequence: Q → K | ||||||
Sequence conflict | 1268 | in Ref. 1; BAA84070 | ||||
Sequence: P → L | ||||||
Sequence conflict | 1280 | in Ref. 1; BAA84070 | ||||
Sequence: F → L | ||||||
Sequence conflict | 1296 | in Ref. 1; BAA84070 | ||||
Sequence: P → T | ||||||
Sequence conflict | 1315-1317 | in Ref. 1; BAA84070 | ||||
Sequence: LDG → RGC | ||||||
Sequence conflict | 1351 | in Ref. 1; BAA84070 | ||||
Sequence: F → I | ||||||
Sequence conflict | 1359 | in Ref. 1; BAA84070 | ||||
Sequence: D → H | ||||||
Sequence conflict | 1376 | in Ref. 1; BAA84070 | ||||
Sequence: S → P | ||||||
Sequence conflict | 1384 | in Ref. 1; BAA84070 | ||||
Sequence: R → H | ||||||
Sequence conflict | 1595 | in Ref. 1; BAA84070 | ||||
Sequence: A → T | ||||||
Sequence conflict | 1631 | in Ref. 1; BAA84070 | ||||
Sequence: S → Y | ||||||
Sequence conflict | 1641 | in Ref. 1; BAA84070 | ||||
Sequence: S → N | ||||||
Sequence conflict | 1674-1677 | in Ref. 1; BAA84070 | ||||
Sequence: VLSV → RLSM | ||||||
Sequence conflict | 1688 | in Ref. 1; BAA84070 | ||||
Sequence: R → H | ||||||
Sequence conflict | 1710 | in Ref. 1; BAA84070 | ||||
Sequence: G → R | ||||||
Sequence conflict | 1720 | in Ref. 1; BAA84070 | ||||
Sequence: D → N | ||||||
Sequence conflict | 1725 | in Ref. 1; BAA84070 | ||||
Sequence: K → T | ||||||
Sequence conflict | 1774-1775 | in Ref. 1; BAA84070 | ||||
Sequence: IS → VH | ||||||
Sequence conflict | 1793 | in Ref. 1; BAA84070 | ||||
Sequence: W → L | ||||||
Sequence conflict | 1808 | in Ref. 1; BAA84070 | ||||
Sequence: C → Y | ||||||
Sequence conflict | 1813 | in Ref. 1; BAA84070 | ||||
Sequence: D → N | ||||||
Sequence conflict | 1911 | in Ref. 1; BAA84070 | ||||
Sequence: N → K | ||||||
Sequence conflict | 2198 | in Ref. 5; AAC68837 and 1; BAA84070 | ||||
Sequence: L → V | ||||||
Compositional bias | 2226-2240 | Basic and acidic residues | ||||
Sequence: ETEELARRQRRHPEL | ||||||
Sequence conflict | 2282 | in Ref. 5; AAC68837 and 1; BAA84070 | ||||
Sequence: V → A | ||||||
Sequence conflict | 2534 | in Ref. 1; BAA84070 | ||||
Sequence: S → R | ||||||
Sequence conflict | 2570 | in Ref. 5; AAC68837 | ||||
Sequence: L → R | ||||||
Sequence conflict | 2638 | in Ref. 5; AAC68837 and 1; BAA84070 | ||||
Sequence: S → Y | ||||||
Sequence conflict | 2760 | in Ref. 1; BAA84070 | ||||
Sequence: L → C | ||||||
Sequence conflict | 2795 | in Ref. 5; AAC68837 | ||||
Sequence: K → R | ||||||
Sequence conflict | 2802 | in Ref. 1; BAA84070 | ||||
Sequence: P → A | ||||||
Compositional bias | 2849-2868 | Polar residues | ||||
Sequence: LLRLPLEQGTGSSRGSSISE | ||||||
Sequence conflict | 2899 | in Ref. 1; BAA84070 | ||||
Sequence: K → N | ||||||
Alternative sequence | VSP_025765 | 2912-2919 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB028499 EMBL· GenBank· DDBJ | BAA84070.1 EMBL· GenBank· DDBJ | mRNA | ||
AF031573 EMBL· GenBank· DDBJ | AAC68837.1 EMBL· GenBank· DDBJ | mRNA | ||
AL671899 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL672200 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH466607 EMBL· GenBank· DDBJ | EDL01967.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC005499 EMBL· GenBank· DDBJ | AAH05499.1 EMBL· GenBank· DDBJ | mRNA |