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O35161 (CELR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cadherin EGF LAG seven-pass G-type receptor 1
Gene names
Name:Celsr1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length3034 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subcellular location

Cell membrane; Multi-pass membrane protein.

Tissue specificity

Expressed in the brain, where it is localized principally in the ependymal cell layer, choroid plexus and the area postrema. Also found in spinal chord and in the eye. Ref.3

Developmental stage

First detected at E6. 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 in the vicinity of the primitive streak, and becomes predominant in that area at late gastrulation. At E10, detected in ventricular zones (VZ), but not in marginal zones (MZ), and weakly in other structures. Between E12 and E15, a high expression is present in the VZ in all brain areas. No expression in differentiated neuronal fields. In the newborn and postnatal stages, expression remains restricted to the VZ. Also found weakly in fetal lungs, kidney and epithelia. Ref.4

Post-translational modification

The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains By similarity.

Sequence similarities

Belongs to the G-protein coupled receptor 2 family. LN-TM7 subfamily.

Contains 9 cadherin domains.

Contains 8 EGF-like domains.

Contains 1 GPS domain.

Contains 1 laminin EGF-like domain.

Contains 2 laminin G-like domains.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainEGF-like domain
Laminin EGF-like domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
   Molecular functionDevelopmental protein
G-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
Hydroxylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Non-traceable author statement Ref.3. Source: UniProtKB

Rho protein signal transduction

Inferred from mutant phenotype PubMed 20223754. Source: MGI

anterior/posterior pattern specification

Inferred from mutant phenotype PubMed 18849982PubMed 19357712. Source: MGI

apical protein localization

Inferred from mutant phenotype PubMed 16687519. Source: MGI

cell-cell signaling

Non-traceable author statement Ref.3. Source: UniProtKB

central nervous system development

Non-traceable author statement Ref.3. Source: UniProtKB

establishment of body hair planar orientation

Inferred from mutant phenotype PubMed 18849982PubMed 19357712. Source: MGI

establishment of planar polarity

Inferred from mutant phenotype PubMed 12842012. Source: UniProtKB

establishment of planar polarity of embryonic epithelium

Inferred from mutant phenotype PubMed 12842012. Source: MGI

gastrulation with mouth forming second

Non-traceable author statement Ref.3. Source: UniProtKB

hair follicle development

Inferred from mutant phenotype PubMed 18849982. Source: MGI

homophilic cell adhesion

Inferred from electronic annotation. Source: InterPro

inner ear morphogenesis

Inferred from mutant phenotype PubMed 12842012. Source: MGI

lateral sprouting involved in lung morphogenesis

Inferred from mutant phenotype PubMed 20223754. Source: MGI

locomotory behavior

Inferred from mutant phenotype PubMed 10932191. Source: MGI

neural tube closure

Inferred from mutant phenotype PubMed 12842012. Source: UniProtKB

neuron migration

Inferred from mutant phenotype PubMed 20631168. Source: MGI

neuropeptide signaling pathway

Inferred from electronic annotation. Source: InterPro

orthogonal dichotomous subdivision of terminal units involved in lung branching morphogenesis

Inferred from mutant phenotype PubMed 20223754. Source: MGI

planar cell polarity pathway involved in neural tube closure

Inferred from genetic interaction PubMed 20704721. Source: MGI

planar dichotomous subdivision of terminal units involved in lung branching morphogenesis

Inferred from mutant phenotype PubMed 20223754. Source: MGI

protein localization involved in establishment of planar polarity

Inferred from direct assay PubMed 18849982. Source: MGI

regulation of actin cytoskeleton organization

Inferred from mutant phenotype PubMed 20223754. Source: MGI

regulation of neurotransmitter secretion

Non-traceable author statement Ref.3. Source: UniProtKB

signal transduction

Non-traceable author statement Ref.3. Source: UniProtKB

wound healing

Inferred from genetic interaction PubMed 20643356. Source: MGI

   Cellular_componentintegral component of plasma membrane

Traceable author statement Ref.3. Source: UniProtKB

membrane

Inferred from direct assay PubMed 20353824. Source: MGI

   Molecular_functionG-protein coupled receptor activity

Non-traceable author statement Ref.3. Source: UniProtKB

calcium ion binding

Traceable author statement PubMed 12842012. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 23292348. Source: IntAct

protein dimerization activity

Non-traceable author statement Ref.3. Source: UniProtKB

transmembrane signaling receptor activity

Non-traceable author statement Ref.3. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

atp6ap2Q7T0S32EBI-8294650,EBI-8294706From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Potential
Chain30 – 30343005Cadherin EGF LAG seven-pass G-type receptor 1
PRO_0000012915

Regions

Topological domain30 – 24842455Extracellular Potential
Transmembrane2485 – 250521Helical; Name=1; Potential
Topological domain2506 – 251611Cytoplasmic Potential
Transmembrane2517 – 253721Helical; Name=2; Potential
Topological domain2538 – 25425Extracellular Potential
Transmembrane2543 – 256321Helical; Name=3; Potential
Topological domain2564 – 258724Cytoplasmic Potential
Transmembrane2588 – 260821Helical; Name=4; Potential
Topological domain2609 – 262517Extracellular Potential
Transmembrane2626 – 264621Helical; Name=5; Potential
Topological domain2647 – 267024Cytoplasmic Potential
Transmembrane2671 – 269121Helical; Name=6; Potential
Topological domain2692 – 26943Extracellular Potential
Transmembrane2695 – 271521Helical; Name=7; Potential
Topological domain2716 – 3034319Cytoplasmic Potential
Domain261 – 368108Cadherin 1
Domain369 – 474106Cadherin 2
Domain475 – 580106Cadherin 3
Domain581 – 702122Cadherin 4
Domain703 – 804102Cadherin 5
Domain805 – 907103Cadherin 6
Domain908 – 1014107Cadherin 7
Domain1015 – 1116102Cadherin 8
Domain1121 – 1239119Cadherin 9
Domain1318 – 137659EGF-like 1; calcium-binding
Domain1378 – 141437EGF-like 2; calcium-binding
Domain1418 – 145639EGF-like 3; calcium-binding
Domain1457 – 1661205Laminin G-like 1
Domain1664 – 170037EGF-like 4; calcium-binding
Domain1704 – 1885182Laminin G-like 2
Domain1887 – 192236EGF-like 5; calcium-binding
Domain1923 – 196139EGF-like 6; calcium-binding
Domain1962 – 199433EGF-like 7; calcium-binding
Domain1996 – 203136EGF-like 8; calcium-binding
Domain2018 – 206548Laminin EGF-like
Domain2423 – 247553GPS
Compositional bias2674 – 26785Poly-Leu

Amino acid modifications

Modified residue16811(3R)-3-hydroxyasparagine Potential
Modified residue19041(3R)-3-hydroxyaspartate Potential
Modified residue27791Phosphoserine By similarity
Glycosylation2361N-linked (GlcNAc...) Potential
Glycosylation5611N-linked (GlcNAc...) Potential
Glycosylation6491N-linked (GlcNAc...) Potential
Glycosylation7931N-linked (GlcNAc...) Potential
Glycosylation11291N-linked (GlcNAc...) Potential
Glycosylation11541N-linked (GlcNAc...) Potential
Glycosylation12281N-linked (GlcNAc...) Potential
Glycosylation12641N-linked (GlcNAc...) Potential
Glycosylation12741N-linked (GlcNAc...) Potential
Glycosylation13021N-linked (GlcNAc...) Potential
Glycosylation15911N-linked (GlcNAc...) Potential
Glycosylation16381N-linked (GlcNAc...) Potential
Glycosylation16551N-linked (GlcNAc...) Potential
Glycosylation19941N-linked (GlcNAc...) Potential
Glycosylation21181N-linked (GlcNAc...) Potential
Glycosylation21371N-linked (GlcNAc...) Potential
Glycosylation21441N-linked (GlcNAc...) Potential
Glycosylation21551N-linked (GlcNAc...) Potential
Glycosylation21601N-linked (GlcNAc...) Potential
Glycosylation22721N-linked (GlcNAc...) Potential
Glycosylation24301N-linked (GlcNAc...) Potential
Glycosylation24521N-linked (GlcNAc...) Potential
Glycosylation25381N-linked (GlcNAc...) Potential
Disulfide bond1322 ↔ 1333 By similarity
Disulfide bond1327 ↔ 1364 By similarity
Disulfide bond1366 ↔ 1375 By similarity
Disulfide bond1382 ↔ 1393 By similarity
Disulfide bond1387 ↔ 1402 By similarity
Disulfide bond1404 ↔ 1413 By similarity
Disulfide bond1422 ↔ 1433 By similarity
Disulfide bond1427 ↔ 1443 By similarity
Disulfide bond1445 ↔ 1455 By similarity
Disulfide bond1635 ↔ 1661 By similarity
Disulfide bond1668 ↔ 1679 By similarity
Disulfide bond1673 ↔ 1688 By similarity
Disulfide bond1690 ↔ 1699 By similarity
Disulfide bond1855 ↔ 1885 By similarity
Disulfide bond1891 ↔ 1902 By similarity
Disulfide bond1896 ↔ 1911 By similarity
Disulfide bond1913 ↔ 1922 By similarity
Disulfide bond1926 ↔ 1937 By similarity
Disulfide bond1931 ↔ 1949 By similarity
Disulfide bond1951 ↔ 1960 By similarity
Disulfide bond1968 ↔ 1981 By similarity
Disulfide bond1983 ↔ 1993 By similarity
Disulfide bond2000 ↔ 2015 By similarity
Disulfide bond2002 ↔ 2018 By similarity
Disulfide bond2020 ↔ 2030 By similarity
Disulfide bond2039 ↔ 2048 By similarity
Disulfide bond2051 ↔ 2063 By similarity

Experimental info

Sequence conflict2181E → Q in AAC68836. Ref.1
Sequence conflict10501M → I in AAC68836. Ref.1
Sequence conflict1900 – 19012SH → RP in AAC68836. Ref.1
Sequence conflict25241T → A in AAC68836. Ref.1
Sequence conflict28051A → T in AAC68836. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O35161 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: FD9C4812AA1F0BCD

FASTA3,034330,471
        10         20         30         40         50         60 
MAPSSPRVLP ALVLLAAAAL PALELGAAAW ELRVPGGARA FALGPGWSYR LDTTRTPREL 

        70         80         90        100        110        120 
LDVSREGPAA GRRLGLGAGT LGCARLAGRL LPLQVRLVAR GAPTAPSLVL RARAYGARCG 

       130        140        150        160        170        180 
VRLLRRSARG AELRSPAVRS VPGLGDALCF PAAGGGAASL TSVLEAITNF PACSCPPVAG 

       190        200        210        220        230        240 
TGCRRGPICL RPGGSAELRL VCALGRAAGA VWVELVIEAT SGTPSESPSV SPSLLNLSQP 

       250        260        270        280        290        300 
RAGVVRRSRR GTGSSTSPQF PLPSYQVSVP ENEPAGTAVI ELRAHDPDEG DAGRLSYQME 

       310        320        330        340        350        360 
ALFDERSNGY FLIDAATGAV TTARSLDRET KDTHVLKVSA VDHGSPRRSA ATYLTVTVSD 

       370        380        390        400        410        420 
TNDHSPVFEQ SEYRERIREN LEVGYEVLTI RATDGDAPSN ANMRYRLLEG AGGVFEIDAR 

       430        440        450        460        470        480 
SGVVRTRAVV DREEAAEYQL LVEANDQGRN PGPLSASATV HIVVEDENDN YPQFSEKRYV 

       490        500        510        520        530        540 
VQVPEDVAVN TAVLRVQATD RDQGQNAAIH YSIVSGNLKG QFYLHSLSGS LDVINPLDFE 

       550        560        570        580        590        600 
AIREYTLRIK AQDGGRPPLI NSSGLVSVQV LDVNDNAPIF VSSPFQAAVL ENVPLGHSVL 

       610        620        630        640        650        660 
HIQAVDADAG ENARLQYRLV DTASTIVGGS SVDSENPASA PDFPFQIHNS SGWITVCAEL 

       670        680        690        700        710        720 
DREEVEHYSF GVEAVDHGSP AMSSSASVSI TVLDVNDNDP MFTQPVYELR LNEDAAVGSS 

       730        740        750        760        770        780 
VLTLRARDRD ANSVITYQLT GGNTRNRFAL SSQSGGGLIT LALPLDYKQE RQYVLAVTAS 

       790        800        810        820        830        840 
DGTRSHTAQV FINVTDANTH RPVFQSSHYT VSVSEDRPVG TSIATISATD EDTGENARIT 

       850        860        870        880        890        900 
YVLEDPVPQF RIDPDTGTIY TMTELDYEDQ AAYTLAITAQ DNGIPQKSDT TSLEILILDA 

       910        920        930        940        950        960 
NDNAPRFLRD FYQGSVFEDA PPSTSVLQVS ATDRDSGPNG RLLYTFQGGD DGDGDFYIEP 

       970        980        990       1000       1010       1020 
TSGVIRTQRR LDRENVAVYN LWALAVDRGS PNPLSASVGI QVSVLDINDN PPVFEKDELE 

      1030       1040       1050       1060       1070       1080 
LFVEENSPVG SVVARIRAND PDEGPNAQIM YQIVEGNVPE VFQLDLLSGD LRALVELDFE 

      1090       1100       1110       1120       1130       1140 
VRRDYMLVVQ ATSAPLVSRA TVHIRLLDQN DNPPELPDFQ ILFNNYVTNK SNSFPSGVIG 

      1150       1160       1170       1180       1190       1200 
RIPAHDPDLS DSLNYTFLQG NELSLLLLDP ATGELQLSRD LDNNRPLEAL MEVSVSDGIH 

      1210       1220       1230       1240       1250       1260 
SVTALCTLRV TIITDDMLTN SITVRLENMS QEKFLSPLLS LFVEGVATVL STTKDDIFVF 

      1270       1280       1290       1300       1310       1320 
NIQNDTDVSS NILNVTFSAL LPGGTRGRFF PSEDLQEQIY LNRTLLTTIS AQRVLPFDDN 

      1330       1340       1350       1360       1370       1380 
ICLREPCENY MKCVSVLRFD SSAPFISSTT VLFRPIHPIT GLRCRCPPGF TGDYCETEID 

      1390       1400       1410       1420       1430       1440 
LCYSNPCGAN GRCRSREGGY TCECFEDFTG EHCQVNVRSG RCASGVCKNG GTCVNLLIGG 

      1450       1460       1470       1480       1490       1500 
FHCVCPPGEY EHPYCEVSTR SFPPQSFVTF RGLRQRFHFT VSLAFATQDR NALLLYNGRF 

      1510       1520       1530       1540       1550       1560 
NEKHDFIALE IVEEQLQLTF SAGETTTTVT PQVPGGVSDG RWHSVLVQYY NKPNIGHLGL 

      1570       1580       1590       1600       1610       1620 
PHGPSGEKVA VVTVDDCDAA VAVHFGSYVG NYSCAAQGTQ SGSKKSLDLT GPLLLGGVPN 

      1630       1640       1650       1660       1670       1680 
LPEDFPVHSR QFVGCMRNLS IDGRIVDMAA FIANNGTRAG CASQRNFCDG TSCQNGGTCV 

      1690       1700       1710       1720       1730       1740 
NRWNTYLCEC PLRFGGKNCE QAMPHPQRFT GESVVLWSDL DITISVPWYL GLMFRTRKED 

      1750       1760       1770       1780       1790       1800 
GVLMEATAGT SSRLHLQILN SYIRFEVSYG PSDVASMQLS KSRITDGGWH HLLIELRSAK 

      1810       1820       1830       1840       1850       1860 
EGKDIKYLAV MTLDYGMDQS TVQIGNQLPG LKMRTIVIGG VTEDKVSVRH GFRGCMQGVR 

      1870       1880       1890       1900       1910       1920 
MGETSTNIAT LNMNDALKVR VKDGCDVEDP CASSPCPPHS HCRDTWDSYS CICDRGYFGK 

      1930       1940       1950       1960       1970       1980 
KCVDACLLNP CKHVAACVRS PNTPRGYSCE CGPGHYGQYC ENKVDLPCPK GWWGNPVCGP 

      1990       2000       2010       2020       2030       2040 
CHCAVSQGFD PDCNKTNGQC QCKENYYKPP AQDACLPCDC FPHGSHSRAC DMDTGQCACK 

      2050       2060       2070       2080       2090       2100 
PGVIGRQCNR CDNPFAEVTS LGCEVIYNGC PRAFEAGIWW PQTKFGQPAA VPCPKGSVGN 

      2110       2120       2130       2140       2150       2160 
AVRHCSGEKG WLPPELFNCT SGSFVDLKAL NEKLNRNETR MDGNRSLRLA KALRNATQGN 

      2170       2180       2190       2200       2210       2220 
STLFGNDVRT AYQLLARILQ HESRQQGFDL AATREANFHE DVVHTGSALL APATEASWEQ 

      2230       2240       2250       2260       2270       2280 
IQRSEAGAAQ LLRHFEAYFS NVARNVKRTY LRPFVIVTAN MILAVDIFDK LNFTGAQVPR 

      2290       2300       2310       2320       2330       2340 
FEDIQEELPR ELESSVSFPA DTFKPPEKKE GPVVRLTNRR TTPLTAQPEP RAERETSSSR 

      2350       2360       2370       2380       2390       2400 
RRRHPDEPGQ FAVALVVIYR TLGQLLPEHY DPDHRSLRLP NRPVINTPVV SAMVYSEGTP 

      2410       2420       2430       2440       2450       2460 
LPSSLQRPIL VEFSLLETEE RSKPVCVFWN HSLDTGGTGG WSAKGCELLS RNRTHVTCQC 

      2470       2480       2490       2500       2510       2520 
SHSASCAVLM DISRREHGEV LPLKIITYAA LSLSLVALLV AFVLLSLVRT LRSNLHSIHK 

      2530       2540       2550       2560       2570       2580 
NLITALFFSQ LIFMVGINQT ENPFLCTVVA ILLHYVSMGT FAWTLVENLH VYRMLTEVRN 

      2590       2600       2610       2620       2630       2640 
IDTGPMRFYH VVGWGIPAIV TGLAVGLDPQ GYGNPDFCWL SLQDTLIWSF AGPVGTVIII 

      2650       2660       2670       2680       2690       2700 
NTVIFVLSAK VSCQRKHHYY ERKGVVSMLR TAFLLLLLVT ATWLLGLLAV NSDTLSFHYL 

      2710       2720       2730       2740       2750       2760 
FAAFSCLQGI FVLLFHCVAH REVRKHLRAV LAGKKLQLDD SATTRATLLT RSLNCNNTYS 

      2770       2780       2790       2800       2810       2820 
EGPDMLRTAL GESTASLDST TRDEGVQKLS VSSGPARGNH GEPDASFIPR NSKKAHGPDS 

      2830       2840       2850       2860       2870       2880 
DSDSELSLDE HSSSYASSHT SDSEDDGGEA EDKWNPAGGP AHSTPKADAL ANHVPAGWPD 

      2890       2900       2910       2920       2930       2940 
ESLAGSDSEE LDTEPHLKVE TKVSVELHRQ AQGNHCGDRP SDPESGVLAK PVAVLSSQPQ 

      2950       2960       2970       2980       2990       3000 
EQRKGILKNK VTYPPPLPEQ PLKSRLREKL ADCEQSPTSS RTSSLGSGDG VHATDCVITI 

      3010       3020       3030 
KTPRREPGRE HLNGVAMNVR TGSAQANGSD SEKP 

« Hide

References

« Hide 'large scale' references
[1]"mCelsr1 is an evolutionarily conserved seven-pass transmembrane receptor and is expressed during mouse embryonic development."
Hadjantonakis A.-K., Formstone C.J., Little P.F.R.
Mech. Dev. 78:91-95(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"Celsr1, a neural-specific gene encoding an unusual seven-pass transmembrane receptor, maps to mouse chromosome 15 and human chromosome 22qter."
Hadjantonakis A.-K., Sheward W.J., Harmar A.J., de Galan L., Hoovers J.M.N., Little P.F.R.
Genomics 45:97-104(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
Strain: C57BL/6.
Tissue: Brain.
[4]"Developmental expression profiles of Celsr (Flamingo) genes in the mouse."
Tissir F., De-Backer O., Goffinet A.M., Lambert de Rouvroit C.A.
Mech. Dev. 112:157-160(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF031572 mRNA. Translation: AAC68836.1.
AC116764 Genomic DNA. No translation available.
AC139513 Genomic DNA. No translation available.
CCDSCCDS37172.1.
PIRT14119.
RefSeqNP_034016.2. NM_009886.2.
UniGeneMm.22680.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO35161. 1 interaction.
MINTMINT-5312768.
STRING10090.ENSMUSP00000016172.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteO35161.

Proteomic databases

PaxDbO35161.
PRIDEO35161.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000016172; ENSMUSP00000016172; ENSMUSG00000016028.
GeneID12614.
KEGGmmu:12614.
UCSCuc007xdt.1. mouse.

Organism-specific databases

CTD9620.
MGIMGI:1100883. Celsr1.

Phylogenomic databases

eggNOGNOG12793.
GeneTreeENSGT00750000117340.
HOGENOMHOG000231346.
HOVERGENHBG050887.
InParanoidO35161.
KOK04600.
OMAEYERPYC.
OrthoDBEOG7BP81K.
TreeFamTF323983.

Gene expression databases

BgeeO35161.
GenevestigatorO35161.

Family and domain databases

Gene3D2.60.120.200. 2 hits.
2.60.40.60. 9 hits.
InterProIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR022624. DUF3497.
IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR002049. EGF_laminin.
IPR017981. GPCR_2-like.
IPR001879. GPCR_2_extracellular_dom.
IPR000832. GPCR_2_secretin-like.
IPR000203. GPS.
IPR009030. Growth_fac_rcpt_N_dom.
IPR001791. Laminin_G.
[Graphical view]
PfamPF00002. 7tm_2. 1 hit.
PF00028. Cadherin. 8 hits.
PF12003. DUF3497. 1 hit.
PF00008. EGF. 3 hits.
PF01825. GPS. 1 hit.
PF02793. HRM. 1 hit.
PF00053. Laminin_EGF. 1 hit.
PF02210. Laminin_G_2. 2 hits.
[Graphical view]
PRINTSPR00205. CADHERIN.
PR00249. GPCRSECRETIN.
SMARTSM00112. CA. 9 hits.
SM00181. EGF. 6 hits.
SM00180. EGF_Lam. 1 hit.
SM00303. GPS. 1 hit.
SM00008. HormR. 1 hit.
SM00282. LamG. 2 hits.
[Graphical view]
SUPFAMSSF49313. SSF49313. 9 hits.
SSF49899. SSF49899. 2 hits.
SSF57184. SSF57184. 2 hits.
PROSITEPS00010. ASX_HYDROXYL. 2 hits.
PS00232. CADHERIN_1. 7 hits.
PS50268. CADHERIN_2. 9 hits.
PS00022. EGF_1. 6 hits.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 6 hits.
PS01248. EGF_LAM_1. 1 hit.
PS50027. EGF_LAM_2. 1 hit.
PS50227. G_PROTEIN_RECEP_F2_3. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
PS50221. GPS. 1 hit.
PS50025. LAM_G_DOMAIN. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio281774.
PROO35161.
SOURCESearch...

Entry information

Entry nameCELR1_MOUSE
AccessionPrimary (citable) accession number: O35161
Secondary accession number(s): E9QK27
Entry history
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 145 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries