Q9R0M0 · CELR2_MOUSE

  • Protein
    Cadherin EGF LAG seven-pass G-type receptor 2
  • Gene
    Celsr2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Receptor that may have an important role in cell/cell signaling during nervous system formation.

Features

Showing features for site.

129192004006008001,0001,2001,4001,6001,8002,0002,2002,4002,6002,800
TypeIDPosition(s)Description
Site2356-2357Cleavage; by autolysis

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentplasma membrane
Molecular Functioncalcium ion binding
Molecular FunctionG protein-coupled receptor activity
Biological Processcerebrospinal fluid secretion
Biological Processcilium assembly
Biological Processcilium movement
Biological Processhomophilic cell adhesion via plasma membrane adhesion molecules
Biological Processmotor neuron migration
Biological Processneural plate anterior/posterior regionalization
Biological Processregulation of DNA-templated transcription
Biological Processregulation of protein localization
Biological Processventricular system development
Biological ProcessWnt signaling pathway

Keywords

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Cadherin EGF LAG seven-pass G-type receptor 2
  • Alternative names
    • Flamingo homolog

Gene names

    • Name
      Celsr2

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q9R0M0
  • Secondary accessions
    • A2AEE7
    • Q99K26
    • Q9Z2R4

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain32-2380Extracellular
Transmembrane2381-2401Helical; Name=1
Topological domain2402-2413Cytoplasmic
Transmembrane2414-2433Helical; Name=2
Topological domain2434-2438Extracellular
Transmembrane2439-2459Helical; Name=3
Topological domain2460-2480Cytoplasmic
Transmembrane2481-2501Helical; Name=4
Topological domain2502-2518Extracellular
Transmembrane2519-2539Helical; Name=5
Topological domain2540-2563Cytoplasmic
Transmembrane2564-2584Helical; Name=6
Topological domain2585-2591Extracellular
Transmembrane2592-2612Helical; Name=7
Topological domain2613-2919Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation, disulfide bond, modified residue.

TypeIDPosition(s)Description
Signal1-31
ChainPRO_000001291732-2919Cadherin EGF LAG seven-pass G-type receptor 2
Glycosylation486N-linked (GlcNAc...) asparagine
Glycosylation557N-linked (GlcNAc...) asparagine
Glycosylation701N-linked (GlcNAc...) asparagine
Glycosylation1036N-linked (GlcNAc...) asparagine
Glycosylation1076N-linked (GlcNAc...) asparagine
Glycosylation1182N-linked (GlcNAc...) asparagine
Glycosylation1212N-linked (GlcNAc...) asparagine
Disulfide bond1292↔1303
Disulfide bond1297↔1312
Disulfide bond1314↔1323
Disulfide bond1332↔1343
Disulfide bond1337↔1353
Disulfide bond1355↔1365
Glycosylation1501N-linked (GlcNAc...) asparagine
Disulfide bond1545↔1571
Glycosylation1565N-linked (GlcNAc...) asparagine
Disulfide bond1578↔1589
Disulfide bond1583↔1598
Modified residue1591(3R)-3-hydroxyasparagine
Disulfide bond1600↔1609
Glycosylation1741N-linked (GlcNAc...) asparagine
Disulfide bond1791↔1802
Disulfide bond1797↔1817
Disulfide bond1819↔1828
Glycosylation1827N-linked (GlcNAc...) asparagine
Disulfide bond1832↔1843
Disulfide bond1837↔1855
Disulfide bond1857↔1866
Disulfide bond1887↔1899
Disulfide bond1889↔1906
Glycosylation1900N-linked (GlcNAc...) asparagine
Disulfide bond1908↔1921
Disulfide bond1924↔1936
Disulfide bond1926↔1943
Disulfide bond1945↔1954
Disulfide bond1957↔1969
Glycosylation2024N-linked (GlcNAc...) asparagine
Glycosylation2043N-linked (GlcNAc...) asparagine
Glycosylation2061N-linked (GlcNAc...) asparagine
Disulfide bond2319↔2351
Glycosylation2323N-linked (GlcNAc...) asparagine
Disulfide bond2339↔2353
Glycosylation2345N-linked (GlcNAc...) asparagine

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

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

TypeEntry 1Entry 2Number of experimentsIntact
XENO Q9R0M0atp6ap2.S Q7T0S32EBI-8294754, EBI-8294706

Protein-protein interaction databases

Miscellaneous

Structure

3D structure databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region156-194Disordered
Compositional bias173-194Polar residues
Domain182-289Cadherin 1
Domain290-399Cadherin 2
Domain400-505Cadherin 3
Domain506-610Cadherin 4
Domain611-712Cadherin 5
Domain713-815Cadherin 6
Domain816-921Cadherin 7
Domain922-1023Cadherin 8
Domain1028-1146Cadherin 9
Domain1228-1286EGF-like 1; atypical
Domain1288-1318EGF-like 2; calcium-binding
Domain1328-1366EGF-like 3; calcium-binding
Domain1367-1571Laminin G-like 1
Domain1574-1610EGF-like 4; calcium-binding
Domain1614-1791Laminin G-like 2
Domain1787-1829EGF-like 5; calcium-binding
Domain1830-1867EGF-like 6; calcium-binding
Domain1883-1922EGF-like 7; calcium-binding
Domain1924-1971Laminin EGF-like
Domain2199-2369GAIN-B
Region2216-2241Disordered
Compositional bias2226-2240Basic and acidic residues
Region2319-2369GPS
Region2690-2884Disordered
Compositional bias2849-2868Polar residues

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Protein family/group databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete
  • Sequence processing
    The 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.

  • Length
    2,919
  • Mass (Da)
    316,986
  • Last updated
    2019-04-10 v3
  • Checksum
    A8F35C88C5808300
MRSRAASAPLPTPLLPLLLLLLLLPPSPLLGDQVGPCRSLGSGGRSSSGACAPVGWLCPASASNLWLYTSRCRESGIELTGHLVPHHDGLRVWCPESGAHIPLPPSSEGCPWSCRLLGIGGHLSPQGTLTLPEEHPCLKAPRLRCQSCKLAQAPGLRAGEGSPEESLGGRRKRNVNTAPQFQPPSYQATVPENQPAGTSVASLRAIDPDEGEAGRLEYTMDALFDSRSNHFFSLDPITGVVTTAEELDRETKSTHVFRVTAQDHGMPRRSALATLTILVTDTNDHDPVFEQQEYKESLRENLEVGYEVLTVRATDGDAPPNANILYRLLEGAGGSPSDAFEIDPRSGVIRTRGPVDREEVESYKLTVEASDQGRDPGPRSSTAIVFLSVEDDNDNAPQFSEKRYVVQVREDVTPGAPVLRVTASDRDKGSNALVHYSIMSGNARGQFYLDAQTGALDVVSPLDYETTKEYTLRIRAQDGGRPPLSNVSGLVTVQVLDINDNAPIFVSTPFQATVLESVPLGYLVLHVQAIDADAGDNARLEYSLAGVGHDFPFTINNGTGWISVAAELDREEVDFYSFGVEARDHGTPALTASASVSVTILDVNDNNPTFTQPEYTVRLNEDAAVGTSVVTVSAVDRDAHSVITYQITSGNTRNRFSITSQSGGGLVSLALPLDYKLERQYVLAVTASDGTRQDTAQIVVNVTDANTHRPVFQSSHYTVNVNEDRPAGTTVVLISATDEDTGENARITYFMEDSIPQFRIDADTGAVTTQAELDYEDQVSYTLAITARDNGIPQKSDTTYLEILVNDVNDNAPQFLRDSYQGSVYEDVPPFTSVLQISATDRDSGLNGRVFYTFQGGDDGDGDFIVESTSGIVRTLRRLDRENVAQYVLRAYAVDKGMPPARTPMEVTVTVLDVNDNPPVFEQDEFDVFVEENSPIGLAVARVTATDPDEGTNAQIMYQIVEGNIPEVFQLDIFSGELTALVDLDYEDRPEYVLVIQATSAPLVSRATVHVRLLDRNDNPPVLGNFEILFNNYVTNRSSSFPGGAIGRVPAHDPDISDSLTYSFERGNELSLVLLNASTGELRLSRALDNNRPLEAIMSVLVSDGVHSVTAQCSLRVTIITDEMLTHSITLRLEDMSPERFLSPLLGLFIQAVAATLATPPDHVVVFNVQRDTDAPGGHILNVSLSVGQPPGPGGGPPFLPSEDLQERLYLNRSLLTAISAQRVLPFDDNICLREPCENYMRCVSVLRFDSSAPFIASSSVLFRPIHPVGGLRCRCPPGFTGDYCETEVDLCYSRPCGPHGRCRSREGGYTCLCLDGYTGEHCEASTHSGRCTPGVCKNGGTCVNLLVGGFKCDCPSGDFEKPFCQVTTRSFPARSFITFRGLRQRFHFTLALSFATKERNGLLLYNGRFNEKHDFVALEVIQEQVQLTFSAGESTTTVSPFVPGGVSDGQWHTVQLKYYNKPLLGQTGLPQGPSEQKVAVVSVDGCDTGVALRFGAMLGNYSCAAQGTQGGSKKSLDLTGPLLLGGVPDLPESFPVRMRHFVGCMKDLQVDSRHIDMADFIANNGTVPGCPTKKIVCDSSICHNGGTCVNQWNAFSCECPLGFGGKSCAQEMANPQRFLGSSLVAWHGLSLPISQPWHLSLMFRTRQADGVLLQAVTRGRSTITLQLRAGHVVLSVEGTGLQASSLRLEPGRANDGDWHHAQLALGASGGPGHAILSFDYGQQKAEGNLGPRLHGLHLSNITVGGVPGPASGVARGFRGCLQGVRVSETPEGISSLDPSRGESINVEPGCSWPDPCDSNPCPTNSYCSNDWDSYSCSCVLGYYGDNCTNVCDLNPCEHQSVCTRKPNTPHGYICECLPNYLGPYCETRIDQPCPRGWWGHPTCGPCNCDVSKGFDPDCNKTSGECHCKENHYRPPGSPTCLLCDCYPTGSLSRVCDPEDGQCPCKPGVIGRQCDRCDNPFAEVTTNGCEVNYDSCPRAIEAGIWWPRTRFGLPAAAPCPKGSFGTAVRHCDEHRGWLPPNLFNCTSVTFSELKGFAERLQRNESGLDSGRSQRLALLLRNATQHTSGYFGSDVKVAYQLATRLLAHESAQRGFGLSATQDVHFTENLLRVGSALLDAANKRHWELIQQTEGGTAWLLQHYEAYASALAQNMRHTYLSPFTIVTPNIVISVVRLDKGNFAGTKLPRYEALRGERPPDLETTVILPESVFREMPSMVRSAGPGEAQETEELARRQRRHPELSQGEAVASVIIYHTLAGLLPHNYDPDKRSLRVPKRPVINTPVVSISVHDDEELLPRALDKPVTVQFRLLETEERTKPICVFWNHSILVSGTGGWSARGCEVVFRNESHVSCQCNHMTSFAVLMDMSRRENGEILPLKTLTYVALGVTLAALMLTFLFLTLLRALRSNQHGIRRNLTAALGLAQLVFLLGINQADLPFACTVIAILLHFLYLCTFSWALLEALHLYRALTEVRDVNASPMRFYYMLGWGVPAFITGLAVGLDPEGYGNPDFCWLSVYDTLIWSFAGPVAFAVSMSVFLYILSARASCAAQRQGFEKKGPVSGLRSSFTVLLLLSATWLLALLSVNSDTLLFHYLFAACNCVQGPFIFLSYVVLSKEVRKALKFACSRKPSPDPALTTKSTLTSSYNCPSPYADGRLYQPYGDSAGSLHSASRSGKSQPSYIPFLLREESTLNPGQVPPGLGDPSGLFLEGQAQQHDPDTDSDSDLSLEDDQSGSYASTHSSDSEEEEEEAAFPGEQGWDSLLGPGAERLPLHSTPKDGGPGSGKVPWLGDFGTTTKENSGSGPLEERPRENGDALTREGSLGPLPGPSTQPHKGILKKKCLPTISEKSSLLRLPLEQGTGSSRGSSISEGSRHGPPPRPPPRQSLQEQLNGVMPVAMSIKAGTVDEDSSGSEFLFFNFLH

Q9R0M0-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
F7BHW1F7BHW1_MOUSECelsr2900

Features

Showing features for sequence conflict, compositional bias, alternative sequence.

TypeIDPosition(s)Description
Sequence conflict3in Ref. 1; BAA84070
Compositional bias173-194Polar residues
Sequence conflict334in Ref. 1; BAA84070
Sequence conflict638in Ref. 1; BAA84070
Sequence conflict721in Ref. 1; BAA84070
Sequence conflict762in Ref. 1; BAA84070
Sequence conflict823in Ref. 1; BAA84070
Sequence conflict838in Ref. 1; BAA84070
Sequence conflict914in Ref. 1; BAA84070
Sequence conflict1222in Ref. 1; BAA84070
Sequence conflict1268in Ref. 1; BAA84070
Sequence conflict1280in Ref. 1; BAA84070
Sequence conflict1296in Ref. 1; BAA84070
Sequence conflict1315-1317in Ref. 1; BAA84070
Sequence conflict1351in Ref. 1; BAA84070
Sequence conflict1359in Ref. 1; BAA84070
Sequence conflict1376in Ref. 1; BAA84070
Sequence conflict1384in Ref. 1; BAA84070
Sequence conflict1595in Ref. 1; BAA84070
Sequence conflict1631in Ref. 1; BAA84070
Sequence conflict1641in Ref. 1; BAA84070
Sequence conflict1674-1677in Ref. 1; BAA84070
Sequence conflict1688in Ref. 1; BAA84070
Sequence conflict1710in Ref. 1; BAA84070
Sequence conflict1720in Ref. 1; BAA84070
Sequence conflict1725in Ref. 1; BAA84070
Sequence conflict1774-1775in Ref. 1; BAA84070
Sequence conflict1793in Ref. 1; BAA84070
Sequence conflict1808in Ref. 1; BAA84070
Sequence conflict1813in Ref. 1; BAA84070
Sequence conflict1911in Ref. 1; BAA84070
Sequence conflict2198in Ref. 5; AAC68837 and 1; BAA84070
Compositional bias2226-2240Basic and acidic residues
Sequence conflict2282in Ref. 5; AAC68837 and 1; BAA84070
Sequence conflict2534in Ref. 1; BAA84070
Sequence conflict2570in Ref. 5; AAC68837
Sequence conflict2638in Ref. 5; AAC68837 and 1; BAA84070
Sequence conflict2760in Ref. 1; BAA84070
Sequence conflict2795in Ref. 5; AAC68837
Sequence conflict2802in Ref. 1; BAA84070
Compositional bias2849-2868Polar residues
Sequence conflict2899in Ref. 1; BAA84070
Alternative sequenceVSP_0257652912-2919in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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