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Protein

Cadherin EGF LAG seven-pass G-type receptor 1

Gene

Celsr1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • G-protein coupled receptor activity Source: UniProtKB
  • protein dimerization activity Source: UniProtKB
  • transmembrane signaling receptor activity Source: UniProtKB

GO - Biological processi

  • anterior/posterior pattern specification Source: MGI
  • apical protein localization Source: MGI
  • cell-cell signaling Source: UniProtKB
  • central nervous system development Source: UniProtKB
  • establishment of body hair planar orientation Source: MGI
  • establishment of planar polarity Source: UniProtKB
  • establishment of planar polarity of embryonic epithelium Source: MGI
  • gastrulation with mouth forming second Source: UniProtKB
  • G-protein coupled receptor signaling pathway Source: UniProtKB
  • hair follicle development Source: MGI
  • homophilic cell adhesion via plasma membrane adhesion molecules Source: InterPro
  • inner ear morphogenesis Source: MGI
  • lateral sprouting involved in lung morphogenesis Source: MGI
  • locomotory behavior Source: MGI
  • neural tube closure Source: UniProtKB
  • neuron migration Source: MGI
  • orthogonal dichotomous subdivision of terminal units involved in lung branching morphogenesis Source: MGI
  • planar cell polarity pathway involved in neural tube closure Source: MGI
  • planar dichotomous subdivision of terminal units involved in lung branching morphogenesis Source: MGI
  • protein localization involved in establishment of planar polarity Source: MGI
  • regulation of actin cytoskeleton organization Source: MGI
  • regulation of neurotransmitter secretion Source: UniProtKB
  • Rho protein signal transduction Source: MGI
  • signal transduction Source: UniProtKB
  • wound healing Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, G-protein coupled receptor, Receptor, Transducer

Keywords - Ligandi

Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Cadherin EGF LAG seven-pass G-type receptor 1
Gene namesi
Name:Celsr1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1100883. Celsr1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini30 – 2484ExtracellularSequence analysisAdd BLAST2455
Transmembranei2485 – 2505Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini2506 – 2516CytoplasmicSequence analysisAdd BLAST11
Transmembranei2517 – 2537Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini2538 – 2542ExtracellularSequence analysis5
Transmembranei2543 – 2563Helical; Name=3Sequence analysisAdd BLAST21
Topological domaini2564 – 2587CytoplasmicSequence analysisAdd BLAST24
Transmembranei2588 – 2608Helical; Name=4Sequence analysisAdd BLAST21
Topological domaini2609 – 2625ExtracellularSequence analysisAdd BLAST17
Transmembranei2626 – 2646Helical; Name=5Sequence analysisAdd BLAST21
Topological domaini2647 – 2670CytoplasmicSequence analysisAdd BLAST24
Transmembranei2671 – 2691Helical; Name=6Sequence analysisAdd BLAST21
Topological domaini2692 – 2694ExtracellularSequence analysis3
Transmembranei2695 – 2715Helical; Name=7Sequence analysisAdd BLAST21
Topological domaini2716 – 3034CytoplasmicSequence analysisAdd BLAST319

GO - Cellular componenti

  • integral component of plasma membrane Source: UniProtKB
  • membrane Source: MGI
  • nucleoplasm Source: MGI
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 29Sequence analysisAdd BLAST29
ChainiPRO_000001291530 – 3034Cadherin EGF LAG seven-pass G-type receptor 1Add BLAST3005

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi236N-linked (GlcNAc...)Sequence analysis1
Glycosylationi561N-linked (GlcNAc...)Sequence analysis1
Glycosylationi649N-linked (GlcNAc...)Sequence analysis1
Glycosylationi793N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1129N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1154N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1228N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1264N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1274N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1302N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1322 ↔ 1333By similarity
Disulfide bondi1327 ↔ 1364By similarity
Disulfide bondi1366 ↔ 1375By similarity
Disulfide bondi1382 ↔ 1393By similarity
Disulfide bondi1387 ↔ 1402By similarity
Disulfide bondi1404 ↔ 1413By similarity
Disulfide bondi1422 ↔ 1433By similarity
Disulfide bondi1427 ↔ 1443By similarity
Disulfide bondi1445 ↔ 1455By similarity
Glycosylationi1591N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1635 ↔ 1661By similarity
Glycosylationi1638N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1655N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1668 ↔ 1679By similarity
Disulfide bondi1673 ↔ 1688By similarity
Modified residuei1681(3R)-3-hydroxyasparagineSequence analysis1
Disulfide bondi1690 ↔ 1699By similarity
Disulfide bondi1855 ↔ 1885By similarity
Disulfide bondi1891 ↔ 1902By similarity
Disulfide bondi1896 ↔ 1911By similarity
Modified residuei1904(3R)-3-hydroxyaspartateSequence analysis1
Disulfide bondi1913 ↔ 1922By similarity
Disulfide bondi1926 ↔ 1937By similarity
Disulfide bondi1931 ↔ 1949By similarity
Disulfide bondi1951 ↔ 1960By similarity
Disulfide bondi1968 ↔ 1981By similarity
Disulfide bondi1983 ↔ 1993By similarity
Glycosylationi1994N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2000 ↔ 2015By similarity
Disulfide bondi2002 ↔ 2018By similarity
Disulfide bondi2020 ↔ 2030By similarity
Disulfide bondi2039 ↔ 2048By similarity
Disulfide bondi2051 ↔ 2063By similarity
Glycosylationi2118N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2137N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2144N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2155N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2160N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2272N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2430N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2452N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2538N-linked (GlcNAc...)Sequence analysis1
Modified residuei2776PhosphoserineCombined sources1
Modified residuei2779PhosphoserineBy similarity1
Modified residuei2886PhosphoserineCombined sources1
Modified residuei2888PhosphoserineCombined sources1

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Phosphoprotein

Proteomic databases

MaxQBiO35161.
PaxDbiO35161.
PeptideAtlasiO35161.
PRIDEiO35161.

PTM databases

iPTMnetiO35161.
PhosphoSitePlusiO35161.

Expressioni

Tissue specificityi

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.1 Publication

Developmental stagei

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.1 Publication

Gene expression databases

BgeeiENSMUSG00000016028.
GenevisibleiO35161. MM.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
atp6ap2Q7T0S32EBI-8294650,EBI-8294706From a different organism.

GO - Molecular functioni

  • protein dimerization activity Source: UniProtKB

Protein-protein interaction databases

IntActiO35161. 1 interactor.
MINTiMINT-5312768.
STRINGi10090.ENSMUSP00000016172.

Structurei

3D structure databases

ProteinModelPortaliO35161.
SMRiO35161.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini261 – 368Cadherin 1PROSITE-ProRule annotationAdd BLAST108
Domaini369 – 474Cadherin 2PROSITE-ProRule annotationAdd BLAST106
Domaini475 – 580Cadherin 3PROSITE-ProRule annotationAdd BLAST106
Domaini581 – 702Cadherin 4PROSITE-ProRule annotationAdd BLAST122
Domaini703 – 804Cadherin 5PROSITE-ProRule annotationAdd BLAST102
Domaini805 – 907Cadherin 6PROSITE-ProRule annotationAdd BLAST103
Domaini908 – 1014Cadherin 7PROSITE-ProRule annotationAdd BLAST107
Domaini1015 – 1116Cadherin 8PROSITE-ProRule annotationAdd BLAST102
Domaini1121 – 1239Cadherin 9PROSITE-ProRule annotationAdd BLAST119
Domaini1318 – 1376EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd BLAST59
Domaini1378 – 1414EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1418 – 1456EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini1457 – 1661Laminin G-like 1PROSITE-ProRule annotationAdd BLAST205
Domaini1664 – 1700EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1704 – 1885Laminin G-like 2PROSITE-ProRule annotationAdd BLAST182
Domaini1887 – 1922EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini1923 – 1961EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini1962 – 1994EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd BLAST33
Domaini1996 – 2031EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini2018 – 2065Laminin EGF-likePROSITE-ProRule annotationAdd BLAST48
Domaini2423 – 2475GPSPROSITE-ProRule annotationAdd BLAST53

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi2674 – 2678Poly-Leu5

Sequence similaritiesi

Contains 9 cadherin domains.PROSITE-ProRule annotation
Contains 8 EGF-like domains.PROSITE-ProRule annotation
Contains 1 GPS domain.PROSITE-ProRule annotation
Contains 1 laminin EGF-like domain.PROSITE-ProRule annotation
Contains 2 laminin G-like domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Laminin EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4289. Eukaryota.
ENOG410XTGH. LUCA.
GeneTreeiENSGT00760000118805.
HOGENOMiHOG000231346.
HOVERGENiHBG050887.
InParanoidiO35161.
KOiK04600.
OMAiNAHKSAN.
OrthoDBiEOG091G0039.
TreeFamiTF323983.

Family and domain databases

Gene3Di2.60.120.200. 2 hits.
2.60.40.60. 9 hits.
InterProiIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR013320. ConA-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR032471. GAIN_dom_N.
IPR017981. GPCR_2-like.
IPR001879. GPCR_2_extracellular_dom.
IPR000832. GPCR_2_secretin-like.
IPR000203. GPS.
IPR009030. Growth_fac_rcpt_.
IPR002049. Laminin_EGF.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF00002. 7tm_2. 1 hit.
PF00028. Cadherin. 8 hits.
PF00008. EGF. 2 hits.
PF16489. GAIN. 1 hit.
PF01825. GPS. 1 hit.
PF02793. HRM. 1 hit.
PF00053. Laminin_EGF. 1 hit.
PF02210. Laminin_G_2. 2 hits.
[Graphical view]
PRINTSiPR00205. CADHERIN.
PR00249. GPCRSECRETIN.
SMARTiSM00112. CA. 9 hits.
SM00181. EGF. 6 hits.
SM00179. EGF_CA. 5 hits.
SM00180. EGF_Lam. 1 hit.
SM00303. GPS. 1 hit.
SM00008. HormR. 1 hit.
SM00282. LamG. 2 hits.
[Graphical view]
SUPFAMiSSF49313. SSF49313. 9 hits.
SSF49899. SSF49899. 2 hits.
SSF57184. SSF57184. 2 hits.
PROSITEiPS00010. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O35161-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPSSPRVLP ALVLLAAAAL PALELGAAAW ELRVPGGARA FALGPGWSYR
60 70 80 90 100
LDTTRTPREL LDVSREGPAA GRRLGLGAGT LGCARLAGRL LPLQVRLVAR
110 120 130 140 150
GAPTAPSLVL RARAYGARCG VRLLRRSARG AELRSPAVRS VPGLGDALCF
160 170 180 190 200
PAAGGGAASL TSVLEAITNF PACSCPPVAG TGCRRGPICL RPGGSAELRL
210 220 230 240 250
VCALGRAAGA VWVELVIEAT SGTPSESPSV SPSLLNLSQP RAGVVRRSRR
260 270 280 290 300
GTGSSTSPQF PLPSYQVSVP ENEPAGTAVI ELRAHDPDEG DAGRLSYQME
310 320 330 340 350
ALFDERSNGY FLIDAATGAV TTARSLDRET KDTHVLKVSA VDHGSPRRSA
360 370 380 390 400
ATYLTVTVSD TNDHSPVFEQ SEYRERIREN LEVGYEVLTI RATDGDAPSN
410 420 430 440 450
ANMRYRLLEG AGGVFEIDAR SGVVRTRAVV DREEAAEYQL LVEANDQGRN
460 470 480 490 500
PGPLSASATV HIVVEDENDN YPQFSEKRYV VQVPEDVAVN TAVLRVQATD
510 520 530 540 550
RDQGQNAAIH YSIVSGNLKG QFYLHSLSGS LDVINPLDFE AIREYTLRIK
560 570 580 590 600
AQDGGRPPLI NSSGLVSVQV LDVNDNAPIF VSSPFQAAVL ENVPLGHSVL
610 620 630 640 650
HIQAVDADAG ENARLQYRLV DTASTIVGGS SVDSENPASA PDFPFQIHNS
660 670 680 690 700
SGWITVCAEL DREEVEHYSF GVEAVDHGSP AMSSSASVSI TVLDVNDNDP
710 720 730 740 750
MFTQPVYELR LNEDAAVGSS VLTLRARDRD ANSVITYQLT GGNTRNRFAL
760 770 780 790 800
SSQSGGGLIT LALPLDYKQE RQYVLAVTAS DGTRSHTAQV FINVTDANTH
810 820 830 840 850
RPVFQSSHYT VSVSEDRPVG TSIATISATD EDTGENARIT YVLEDPVPQF
860 870 880 890 900
RIDPDTGTIY TMTELDYEDQ AAYTLAITAQ DNGIPQKSDT TSLEILILDA
910 920 930 940 950
NDNAPRFLRD FYQGSVFEDA PPSTSVLQVS ATDRDSGPNG RLLYTFQGGD
960 970 980 990 1000
DGDGDFYIEP TSGVIRTQRR LDRENVAVYN LWALAVDRGS PNPLSASVGI
1010 1020 1030 1040 1050
QVSVLDINDN PPVFEKDELE LFVEENSPVG SVVARIRAND PDEGPNAQIM
1060 1070 1080 1090 1100
YQIVEGNVPE VFQLDLLSGD LRALVELDFE VRRDYMLVVQ ATSAPLVSRA
1110 1120 1130 1140 1150
TVHIRLLDQN DNPPELPDFQ ILFNNYVTNK SNSFPSGVIG RIPAHDPDLS
1160 1170 1180 1190 1200
DSLNYTFLQG NELSLLLLDP ATGELQLSRD LDNNRPLEAL MEVSVSDGIH
1210 1220 1230 1240 1250
SVTALCTLRV TIITDDMLTN SITVRLENMS QEKFLSPLLS LFVEGVATVL
1260 1270 1280 1290 1300
STTKDDIFVF NIQNDTDVSS NILNVTFSAL LPGGTRGRFF PSEDLQEQIY
1310 1320 1330 1340 1350
LNRTLLTTIS AQRVLPFDDN ICLREPCENY MKCVSVLRFD SSAPFISSTT
1360 1370 1380 1390 1400
VLFRPIHPIT GLRCRCPPGF TGDYCETEID LCYSNPCGAN GRCRSREGGY
1410 1420 1430 1440 1450
TCECFEDFTG EHCQVNVRSG RCASGVCKNG GTCVNLLIGG FHCVCPPGEY
1460 1470 1480 1490 1500
EHPYCEVSTR SFPPQSFVTF RGLRQRFHFT VSLAFATQDR NALLLYNGRF
1510 1520 1530 1540 1550
NEKHDFIALE IVEEQLQLTF SAGETTTTVT PQVPGGVSDG RWHSVLVQYY
1560 1570 1580 1590 1600
NKPNIGHLGL PHGPSGEKVA VVTVDDCDAA VAVHFGSYVG NYSCAAQGTQ
1610 1620 1630 1640 1650
SGSKKSLDLT GPLLLGGVPN LPEDFPVHSR QFVGCMRNLS IDGRIVDMAA
1660 1670 1680 1690 1700
FIANNGTRAG CASQRNFCDG TSCQNGGTCV NRWNTYLCEC PLRFGGKNCE
1710 1720 1730 1740 1750
QAMPHPQRFT GESVVLWSDL DITISVPWYL GLMFRTRKED GVLMEATAGT
1760 1770 1780 1790 1800
SSRLHLQILN SYIRFEVSYG PSDVASMQLS KSRITDGGWH HLLIELRSAK
1810 1820 1830 1840 1850
EGKDIKYLAV MTLDYGMDQS TVQIGNQLPG LKMRTIVIGG VTEDKVSVRH
1860 1870 1880 1890 1900
GFRGCMQGVR MGETSTNIAT LNMNDALKVR VKDGCDVEDP CASSPCPPHS
1910 1920 1930 1940 1950
HCRDTWDSYS CICDRGYFGK KCVDACLLNP CKHVAACVRS PNTPRGYSCE
1960 1970 1980 1990 2000
CGPGHYGQYC ENKVDLPCPK GWWGNPVCGP CHCAVSQGFD PDCNKTNGQC
2010 2020 2030 2040 2050
QCKENYYKPP AQDACLPCDC FPHGSHSRAC DMDTGQCACK PGVIGRQCNR
2060 2070 2080 2090 2100
CDNPFAEVTS LGCEVIYNGC PRAFEAGIWW PQTKFGQPAA VPCPKGSVGN
2110 2120 2130 2140 2150
AVRHCSGEKG WLPPELFNCT SGSFVDLKAL NEKLNRNETR MDGNRSLRLA
2160 2170 2180 2190 2200
KALRNATQGN STLFGNDVRT AYQLLARILQ HESRQQGFDL AATREANFHE
2210 2220 2230 2240 2250
DVVHTGSALL APATEASWEQ IQRSEAGAAQ LLRHFEAYFS NVARNVKRTY
2260 2270 2280 2290 2300
LRPFVIVTAN MILAVDIFDK LNFTGAQVPR FEDIQEELPR ELESSVSFPA
2310 2320 2330 2340 2350
DTFKPPEKKE GPVVRLTNRR TTPLTAQPEP RAERETSSSR RRRHPDEPGQ
2360 2370 2380 2390 2400
FAVALVVIYR TLGQLLPEHY DPDHRSLRLP NRPVINTPVV SAMVYSEGTP
2410 2420 2430 2440 2450
LPSSLQRPIL VEFSLLETEE RSKPVCVFWN HSLDTGGTGG WSAKGCELLS
2460 2470 2480 2490 2500
RNRTHVTCQC SHSASCAVLM DISRREHGEV LPLKIITYAA LSLSLVALLV
2510 2520 2530 2540 2550
AFVLLSLVRT LRSNLHSIHK NLITALFFSQ LIFMVGINQT ENPFLCTVVA
2560 2570 2580 2590 2600
ILLHYVSMGT FAWTLVENLH VYRMLTEVRN IDTGPMRFYH VVGWGIPAIV
2610 2620 2630 2640 2650
TGLAVGLDPQ GYGNPDFCWL SLQDTLIWSF AGPVGTVIII NTVIFVLSAK
2660 2670 2680 2690 2700
VSCQRKHHYY ERKGVVSMLR TAFLLLLLVT ATWLLGLLAV NSDTLSFHYL
2710 2720 2730 2740 2750
FAAFSCLQGI FVLLFHCVAH REVRKHLRAV LAGKKLQLDD SATTRATLLT
2760 2770 2780 2790 2800
RSLNCNNTYS EGPDMLRTAL GESTASLDST TRDEGVQKLS VSSGPARGNH
2810 2820 2830 2840 2850
GEPDASFIPR NSKKAHGPDS DSDSELSLDE HSSSYASSHT SDSEDDGGEA
2860 2870 2880 2890 2900
EDKWNPAGGP AHSTPKADAL ANHVPAGWPD ESLAGSDSEE LDTEPHLKVE
2910 2920 2930 2940 2950
TKVSVELHRQ AQGNHCGDRP SDPESGVLAK PVAVLSSQPQ EQRKGILKNK
2960 2970 2980 2990 3000
VTYPPPLPEQ PLKSRLREKL ADCEQSPTSS RTSSLGSGDG VHATDCVITI
3010 3020 3030
KTPRREPGRE HLNGVAMNVR TGSAQANGSD SEKP
Length:3,034
Mass (Da):330,471
Last modified:July 27, 2011 - v3
Checksum:iFD9C4812AA1F0BCD
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti218E → Q in AAC68836 (PubMed:9858697).Curated1
Sequence conflicti1050M → I in AAC68836 (PubMed:9858697).Curated1
Sequence conflicti1900 – 1901SH → RP in AAC68836 (PubMed:9858697).Curated2
Sequence conflicti2524T → A in AAC68836 (PubMed:9858697).Curated1
Sequence conflicti2805A → T in AAC68836 (PubMed:9858697).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF031572 mRNA. Translation: AAC68836.1.
AC116764 Genomic DNA. No translation available.
AC139513 Genomic DNA. No translation available.
CCDSiCCDS37172.1.
PIRiT14119.
RefSeqiNP_034016.2. NM_009886.2.
UniGeneiMm.22680.

Genome annotation databases

EnsembliENSMUST00000016172; ENSMUSP00000016172; ENSMUSG00000016028.
GeneIDi12614.
KEGGimmu:12614.
UCSCiuc007xdt.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF031572 mRNA. Translation: AAC68836.1.
AC116764 Genomic DNA. No translation available.
AC139513 Genomic DNA. No translation available.
CCDSiCCDS37172.1.
PIRiT14119.
RefSeqiNP_034016.2. NM_009886.2.
UniGeneiMm.22680.

3D structure databases

ProteinModelPortaliO35161.
SMRiO35161.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO35161. 1 interactor.
MINTiMINT-5312768.
STRINGi10090.ENSMUSP00000016172.

Protein family/group databases

GPCRDBiSearch...

PTM databases

iPTMnetiO35161.
PhosphoSitePlusiO35161.

Proteomic databases

MaxQBiO35161.
PaxDbiO35161.
PeptideAtlasiO35161.
PRIDEiO35161.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000016172; ENSMUSP00000016172; ENSMUSG00000016028.
GeneIDi12614.
KEGGimmu:12614.
UCSCiuc007xdt.1. mouse.

Organism-specific databases

CTDi9620.
MGIiMGI:1100883. Celsr1.

Phylogenomic databases

eggNOGiKOG4289. Eukaryota.
ENOG410XTGH. LUCA.
GeneTreeiENSGT00760000118805.
HOGENOMiHOG000231346.
HOVERGENiHBG050887.
InParanoidiO35161.
KOiK04600.
OMAiNAHKSAN.
OrthoDBiEOG091G0039.
TreeFamiTF323983.

Miscellaneous databases

ChiTaRSiCelsr1. mouse.
PROiO35161.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000016028.
GenevisibleiO35161. MM.

Family and domain databases

Gene3Di2.60.120.200. 2 hits.
2.60.40.60. 9 hits.
InterProiIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR013320. ConA-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR032471. GAIN_dom_N.
IPR017981. GPCR_2-like.
IPR001879. GPCR_2_extracellular_dom.
IPR000832. GPCR_2_secretin-like.
IPR000203. GPS.
IPR009030. Growth_fac_rcpt_.
IPR002049. Laminin_EGF.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF00002. 7tm_2. 1 hit.
PF00028. Cadherin. 8 hits.
PF00008. EGF. 2 hits.
PF16489. GAIN. 1 hit.
PF01825. GPS. 1 hit.
PF02793. HRM. 1 hit.
PF00053. Laminin_EGF. 1 hit.
PF02210. Laminin_G_2. 2 hits.
[Graphical view]
PRINTSiPR00205. CADHERIN.
PR00249. GPCRSECRETIN.
SMARTiSM00112. CA. 9 hits.
SM00181. EGF. 6 hits.
SM00179. EGF_CA. 5 hits.
SM00180. EGF_Lam. 1 hit.
SM00303. GPS. 1 hit.
SM00008. HormR. 1 hit.
SM00282. LamG. 2 hits.
[Graphical view]
SUPFAMiSSF49313. SSF49313. 9 hits.
SSF49899. SSF49899. 2 hits.
SSF57184. SSF57184. 2 hits.
PROSITEiPS00010. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiCELR1_MOUSE
AccessioniPrimary (citable) accession number: O35161
Secondary accession number(s): E9QK27
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: July 27, 2011
Last modified: November 2, 2016
This is version 162 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.