O35161 (CELR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cadherin EGF LAG seven-pass G-type receptor 1

Gene names

Name:

Celsr1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	3034 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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 component	Cell membrane Membrane
Domain	EGF-like domain Laminin EGF-like domain Repeat Signal Transmembrane Transmembrane helix
Ligand	Calcium
Molecular function	Developmental protein G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein Hydroxylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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 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 wound healing Inferred from genetic interaction PubMed 20643356. Source: MGI
Cellular_component	integral to plasma membrane Traceable author statement Ref.3. Source: UniProtKB
Molecular_function	G-protein coupled receptor activity Non-traceable author statement Ref.3. Source: UniProtKB calcium ion binding Traceable author statement PubMed 12842012. Source: UniProtKB protein dimerization activity Non-traceable author statement Ref.3. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 29	29	Potential
	Chain	30 – 3034	3005	Cadherin EGF LAG seven-pass G-type receptor 1		PRO_0000012915
Regions
	Topological domain	30 – 2484	2455	Extracellular Potential
	Transmembrane	2485 – 2505	21	Helical; Name=1; Potential
	Topological domain	2506 – 2516	11	Cytoplasmic Potential
	Transmembrane	2517 – 2537	21	Helical; Name=2; Potential
	Topological domain	2538 – 2542	5	Extracellular Potential
	Transmembrane	2543 – 2563	21	Helical; Name=3; Potential
	Topological domain	2564 – 2587	24	Cytoplasmic Potential
	Transmembrane	2588 – 2608	21	Helical; Name=4; Potential
	Topological domain	2609 – 2625	17	Extracellular Potential
	Transmembrane	2626 – 2646	21	Helical; Name=5; Potential
	Topological domain	2647 – 2670	24	Cytoplasmic Potential
	Transmembrane	2671 – 2691	21	Helical; Name=6; Potential
	Topological domain	2692 – 2694	3	Extracellular Potential
	Transmembrane	2695 – 2715	21	Helical; Name=7; Potential
	Topological domain	2716 – 3034	319	Cytoplasmic Potential
	Domain	261 – 368	108	Cadherin 1
	Domain	369 – 474	106	Cadherin 2
	Domain	475 – 580	106	Cadherin 3
	Domain	581 – 702	122	Cadherin 4
	Domain	703 – 804	102	Cadherin 5
	Domain	805 – 907	103	Cadherin 6
	Domain	908 – 1014	107	Cadherin 7
	Domain	1015 – 1116	102	Cadherin 8
	Domain	1121 – 1239	119	Cadherin 9
	Domain	1318 – 1376	59	EGF-like 1; calcium-binding
	Domain	1378 – 1414	37	EGF-like 2; calcium-binding
	Domain	1418 – 1456	39	EGF-like 3; calcium-binding
	Domain	1457 – 1661	205	Laminin G-like 1
	Domain	1664 – 1700	37	EGF-like 4; calcium-binding
	Domain	1704 – 1885	182	Laminin G-like 2
	Domain	1887 – 1922	36	EGF-like 5; calcium-binding
	Domain	1923 – 1961	39	EGF-like 6; calcium-binding
	Domain	1962 – 1994	33	EGF-like 7; calcium-binding
	Domain	1996 – 2031	36	EGF-like 8; calcium-binding
	Domain	2018 – 2065	48	Laminin EGF-like
	Domain	2423 – 2475	53	GPS
	Compositional bias	2674 – 2678	5	Poly-Leu
Amino acid modifications
	Modified residue	1681	1	(3R)-3-hydroxyasparagine Potential
	Modified residue	1904	1	(3R)-3-hydroxyaspartate Potential
	Modified residue	2779	1	Phosphoserine By similarity
	Glycosylation	236	1	N-linked (GlcNAc...) Potential
	Glycosylation	561	1	N-linked (GlcNAc...) Potential
	Glycosylation	649	1	N-linked (GlcNAc...) Potential
	Glycosylation	793	1	N-linked (GlcNAc...) Potential
	Glycosylation	1129	1	N-linked (GlcNAc...) Potential
	Glycosylation	1154	1	N-linked (GlcNAc...) Potential
	Glycosylation	1228	1	N-linked (GlcNAc...) Potential
	Glycosylation	1264	1	N-linked (GlcNAc...) Potential
	Glycosylation	1274	1	N-linked (GlcNAc...) Potential
	Glycosylation	1302	1	N-linked (GlcNAc...) Potential
	Glycosylation	1591	1	N-linked (GlcNAc...) Potential
	Glycosylation	1638	1	N-linked (GlcNAc...) Potential
	Glycosylation	1655	1	N-linked (GlcNAc...) Potential
	Glycosylation	1994	1	N-linked (GlcNAc...) Potential
	Glycosylation	2118	1	N-linked (GlcNAc...) Potential
	Glycosylation	2137	1	N-linked (GlcNAc...) Potential
	Glycosylation	2144	1	N-linked (GlcNAc...) Potential
	Glycosylation	2155	1	N-linked (GlcNAc...) Potential
	Glycosylation	2160	1	N-linked (GlcNAc...) Potential
	Glycosylation	2272	1	N-linked (GlcNAc...) Potential
	Glycosylation	2430	1	N-linked (GlcNAc...) Potential
	Glycosylation	2452	1	N-linked (GlcNAc...) Potential
	Glycosylation	2538	1	N-linked (GlcNAc...) Potential
	Disulfide bond	1322 ↔ 1333		By similarity
	Disulfide bond	1327 ↔ 1364		By similarity
	Disulfide bond	1366 ↔ 1375		By similarity
	Disulfide bond	1382 ↔ 1393		By similarity
	Disulfide bond	1387 ↔ 1402		By similarity
	Disulfide bond	1404 ↔ 1413		By similarity
	Disulfide bond	1422 ↔ 1433		By similarity
	Disulfide bond	1427 ↔ 1443		By similarity
	Disulfide bond	1445 ↔ 1455		By similarity
	Disulfide bond	1635 ↔ 1661		By similarity
	Disulfide bond	1668 ↔ 1679		By similarity
	Disulfide bond	1673 ↔ 1688		By similarity
	Disulfide bond	1690 ↔ 1699		By similarity
	Disulfide bond	1855 ↔ 1885		By similarity
	Disulfide bond	1891 ↔ 1902		By similarity
	Disulfide bond	1896 ↔ 1911		By similarity
	Disulfide bond	1913 ↔ 1922		By similarity
	Disulfide bond	1926 ↔ 1937		By similarity
	Disulfide bond	1931 ↔ 1949		By similarity
	Disulfide bond	1951 ↔ 1960		By similarity
	Disulfide bond	1968 ↔ 1981		By similarity
	Disulfide bond	1983 ↔ 1993		By similarity
	Disulfide bond	2000 ↔ 2015		By similarity
	Disulfide bond	2002 ↔ 2018		By similarity
	Disulfide bond	2020 ↔ 2030		By similarity
	Disulfide bond	2039 ↔ 2048		By similarity
	Disulfide bond	2051 ↔ 2063		By similarity
Experimental info
	Sequence conflict	218	1	E → Q in AAC68836. Ref.1
	Sequence conflict	1050	1	M → I in AAC68836. Ref.1
	Sequence conflict	1900 – 1901	2	SH → RP in AAC68836. Ref.1
	Sequence conflict	2524	1	T → A in AAC68836. Ref.1
	Sequence conflict	2805	1	A → T in AAC68836. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O35161 [UniParc]. Last modified July 27, 2011. Version 3. Checksum: FD9C4812AA1F0BCD	FASTA	3,034	330,471
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00127701.
PIR	T14119.
RefSeq	NP_034016.2. NM_009886.2.
UniGene	Mm.22680.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000016172.
Protein family/group databases
GPCRDB	Search...
PTM databases
PhosphoSite	O35161.
Proteomic databases
PaxDb	O35161.
PRIDE	O35161.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000016172; ENSMUSP00000016172; ENSMUSG00000016028.
GeneID	12614.
KEGG	mmu:12614.
UCSC	uc007xdt.1. mouse.
Organism-specific databases
CTD	9620.
MGI	MGI:1100883. Celsr1.
Phylogenomic databases
eggNOG	NOG12793.
GeneTree	ENSGT00700000104170.
HOGENOM	HOG000231346.
HOVERGEN	HBG050887.
InParanoid	O35161.
KO	K04600.
OMA	NKPNIGH.
OrthoDB	EOG4KKZ23.
Gene expression databases
Bgee	O35161.
Genevestigator	O35161.
GermOnline	ENSMUSG00000016028. Mus musculus.
Family and domain databases
Gene3D	2.60.120.200. 2 hits. 2.60.40.60. 9 hits.
InterPro	IPR002126. 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_dom. IPR001791. Laminin_G. [Graphical view]
Pfam	PF00002. 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]
PRINTS	PR00205. CADHERIN. PR00249. GPCRSECRETIN.
SMART	SM00112. 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]
SUPFAM	SSF49313. Cadherin. 9 hits. SSF49899. ConA_like_lec_gl. 2 hits.
PROSITE	PS00010. 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. PS00649. G_PROTEIN_RECEP_F2_1. False negative. PS00650. G_PROTEIN_RECEP_F2_2. False negative. 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]
ProtoNet	Search...
Other
NextBio	281774.
SOURCE	Search...

Entry information

Entry name

CELR1_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 136 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program