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Protein

Cadherin EGF LAG seven-pass G-type receptor 2

Gene

Celsr2

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

GO - Biological processi

  • cerebrospinal fluid secretion Source: MGI
  • cilium assembly Source: MGI
  • cilium movement Source: MGI
  • homophilic cell adhesion via plasma membrane adhesion molecules Source: BHF-UCL
  • neural plate anterior/posterior regionalization Source: BHF-UCL
  • neuron migration Source: MGI
  • regulation of protein localization Source: MGI
  • regulation of transcription, DNA-templated Source: BHF-UCL
  • ventricular system development Source: MGI
  • Wnt signaling pathway Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Ligandi

Calcium

Protein family/group databases

MEROPSiP02.006.

Names & Taxonomyi

Protein namesi
Recommended name:
Cadherin EGF LAG seven-pass G-type receptor 2
Alternative name(s):
Flamingo homolog
Gene namesi
Name:Celsr2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1858235. Celsr2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini32 – 2381ExtracellularSequence analysisAdd BLAST2350
Transmembranei2382 – 2402Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini2403 – 2414CytoplasmicSequence analysisAdd BLAST12
Transmembranei2415 – 2434Helical; Name=2Sequence analysisAdd BLAST20
Topological domaini2435 – 2439ExtracellularSequence analysis5
Transmembranei2440 – 2460Helical; Name=3Sequence analysisAdd BLAST21
Topological domaini2461 – 2481CytoplasmicSequence analysisAdd BLAST21
Transmembranei2482 – 2502Helical; Name=4Sequence analysisAdd BLAST21
Topological domaini2503 – 2519ExtracellularSequence analysisAdd BLAST17
Transmembranei2520 – 2540Helical; Name=5Sequence analysisAdd BLAST21
Topological domaini2541 – 2564CytoplasmicSequence analysisAdd BLAST24
Transmembranei2565 – 2585Helical; Name=6Sequence analysisAdd BLAST21
Topological domaini2586 – 2592ExtracellularSequence analysis7
Transmembranei2593 – 2613Helical; Name=7Sequence analysisAdd BLAST21
Topological domaini2614 – 2920CytoplasmicSequence analysisAdd BLAST307

GO - Cellular componenti

  • cytoplasm Source: BHF-UCL
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 31Sequence analysisAdd BLAST31
ChainiPRO_000001291732 – 2920Cadherin EGF LAG seven-pass G-type receptor 2Add BLAST2889

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi486N-linked (GlcNAc...)Sequence analysis1
Glycosylationi558N-linked (GlcNAc...)Sequence analysis1
Glycosylationi702N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1037N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1077N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1183N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1213N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1293 ↔ 1304By similarity
Disulfide bondi1298 ↔ 1313By similarity
Disulfide bondi1315 ↔ 1318By similarity
Disulfide bondi1333 ↔ 1344By similarity
Disulfide bondi1338 ↔ 1354By similarity
Disulfide bondi1356 ↔ 1366By similarity
Glycosylationi1502N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1546 ↔ 1572By similarity
Glycosylationi1566N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1579 ↔ 1590By similarity
Disulfide bondi1584 ↔ 1599By similarity
Modified residuei1592(3R)-3-hydroxyasparagineSequence analysis1
Disulfide bondi1601 ↔ 1610By similarity
Glycosylationi1742N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1792 ↔ 1803By similarity
Disulfide bondi1798 ↔ 1818By similarity
Disulfide bondi1820 ↔ 1829By similarity
Glycosylationi1828N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1833 ↔ 1844By similarity
Disulfide bondi1838 ↔ 1856By similarity
Disulfide bondi1858 ↔ 1867By similarity
Disulfide bondi1888 ↔ 1900By similarity
Disulfide bondi1890 ↔ 1907By similarity
Glycosylationi1901N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1909 ↔ 1922By similarity
Disulfide bondi1925 ↔ 1937By similarity
Disulfide bondi1927 ↔ 1944By similarity
Disulfide bondi1946 ↔ 1955By similarity
Disulfide bondi1958 ↔ 1970By similarity
Glycosylationi2025N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2044N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2062N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2324N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2346N-linked (GlcNAc...)Sequence analysis1

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

Proteomic databases

PaxDbiQ9R0M0.
PRIDEiQ9R0M0.

PTM databases

iPTMnetiQ9R0M0.
PhosphoSitePlusiQ9R0M0.

Expressioni

Tissue specificityi

Expressed in the CNS and in the eye.1 Publication

Developmental stagei

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 E10, expression is strong in the ventricular zones (VZ) in all sectors of the brain, and lower in the marginal zones (MZ). Between E12 and E15, expression is prominant 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.1 Publication

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
atp6ap2Q7T0S32EBI-8294754,EBI-8294706From a different organism.

Protein-protein interaction databases

IntActiQ9R0M0. 1 interactor.
MINTiMINT-5202369.
STRINGi10090.ENSMUSP00000088046.

Structurei

3D structure databases

ProteinModelPortaliQ9R0M0.
SMRiQ9R0M0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini182 – 289Cadherin 1PROSITE-ProRule annotationAdd BLAST108
Domaini290 – 399Cadherin 2PROSITE-ProRule annotationAdd BLAST110
Domaini400 – 506Cadherin 3PROSITE-ProRule annotationAdd BLAST107
Domaini507 – 611Cadherin 4PROSITE-ProRule annotationAdd BLAST105
Domaini612 – 713Cadherin 5PROSITE-ProRule annotationAdd BLAST102
Domaini714 – 816Cadherin 6PROSITE-ProRule annotationAdd BLAST103
Domaini817 – 922Cadherin 7PROSITE-ProRule annotationAdd BLAST106
Domaini923 – 1024Cadherin 8PROSITE-ProRule annotationAdd BLAST102
Domaini1029 – 1147Cadherin 9PROSITE-ProRule annotationAdd BLAST119
Domaini1229 – 1287EGF-like 1; atypicalPROSITE-ProRule annotationAdd BLAST59
Domaini1289 – 1319EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd BLAST31
Domaini1329 – 1367EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini1368 – 1572Laminin G-like 1PROSITE-ProRule annotationAdd BLAST205
Domaini1575 – 1611EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1615 – 1792Laminin G-like 2PROSITE-ProRule annotationAdd BLAST178
Domaini1788 – 1830EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd BLAST43
Domaini1831 – 1868EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd BLAST38
Domaini1884 – 1923EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Domaini1925 – 1972Laminin EGF-likePROSITE-ProRule annotationAdd BLAST48
Domaini2317 – 2369GPSPROSITE-ProRule annotationAdd BLAST53

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi2744 – 2749Poly-Glu6

Sequence similaritiesi

Contains 9 cadherin domains.PROSITE-ProRule annotation
Contains 7 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.
HOGENOMiHOG000231346.
HOVERGENiHBG050887.
InParanoidiQ9R0M0.
PhylomeDBiQ9R0M0.

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. 1 hit.
PF16489. GAIN. 1 hit.
PF01825. GPS. 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. 1 hit.
PS00232. CADHERIN_1. 6 hits.
PS50268. CADHERIN_2. 9 hits.
PS00022. EGF_1. 6 hits.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 5 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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9R0M0-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MRTRAASAPL PTPLLPLLLL LLLLPPSPLL GDQVGPCRSL GSGGRSSSGA
60 70 80 90 100
CAPVGWLCPA SASNLWLYTS RCRESGIELT GHLVPHHDGL RVWCPESGAH
110 120 130 140 150
IPLPPSSEGC PWSCRLLGIG GHLSPQGTLT LPEEHPCLKA PRLRCQSCKL
160 170 180 190 200
AQAPGLRAGE GSPEESLGGR RKRNVNTAPQ FQPPSYQATV PENQPAGTSV
210 220 230 240 250
ASLRAIDPDE GEAGRLEYTM DALFDSRSNH FFSLDPITGV VTTAEELDRE
260 270 280 290 300
TKSTHVFRVT AQDHGMPRRS ALATLTILVT DTNDHDPVFE QQEYKESLRE
310 320 330 340 350
NLEVGYEVLT VRATDGDAPP NANILYRLLE GAGDSPSDAF EIDPRSGVIR
360 370 380 390 400
TRGPVDREEV ESYKLTVEAS DQGRDPGPRS STAIVFLSVE DDNDNAPQFS
410 420 430 440 450
EKRYVVQVRE DVTPGAPVLR VTASDRDKGS NALVHYSIMS GNARGQFYLD
460 470 480 490 500
AQTGALDVVS PLDYETTKEY TLRIRAQDGG RPPLSNVSGL VTVQVLDIND
510 520 530 540 550
IRPPIFVSTP FQATVLESVP LGYLVLHVQA IDADAGDNAR LEYSLAGVGH
560 570 580 590 600
DFPFTINNGT GWISVAAELD REEVDFYSFG VEARDHGTPA LTASASVSVT
610 620 630 640 650
ILDVNDNNPT FTQPEYTVRL NEDAAVGTSV VTVSAVDRHA HSVITYQITS
660 670 680 690 700
GNTRNRFSIT SQSGGGLVSL ALPLDYKLER QYVLAVTASD GTRQDTAQIV
710 720 730 740 750
VNVTDANTHR PVFQSSHYTV NGNEDRPAGT TVVLISATDE DTGENARITY
760 770 780 790 800
FMEDSIPQFR IDGDTGAVTT QAELDYEDQV SYTLAITARD NGIPQKSDTT
810 820 830 840 850
YLEILVNDVN DNAPQFLRDS YQGTVYEDVP PFTSVLQILA TDRDSGLNGR
860 870 880 890 900
VFYTFQGGDD GDGDFIVEST SGIVRTLRRL DRENVAQYVL RAYAVDKGMP
910 920 930 940 950
PARTPMEVTV TVLDGNDNPP VFEQDEFDVF VEENSPIGLA VARVTATDPD
960 970 980 990 1000
EGTNAQIMYQ IVEGNIPEVF QLDIFSGELT ALVDLDYEDR PEYVLVIQAT
1010 1020 1030 1040 1050
SAPLVSRATV HVRLLDRNDN PPVLGNFEIL FNNYVTNRSS SFPGGAIGRV
1060 1070 1080 1090 1100
PAHDPDISDS LTYSFERGNE LSLVLLNAST GELRLSRALD NNRPLEAIMS
1110 1120 1130 1140 1150
VLVSDGVHSV TAQCSLRVTI ITDEMLTHSI TLRLEDMSPE RFLSPLLGLF
1160 1170 1180 1190 1200
IQAVAATLAT PPDHVVVFNV QRDTDAPGGH ILNVSLSVGQ PPGPGGGPPF
1210 1220 1230 1240 1250
LPSEDLQERL YLNRSLLTAI SAKRVLPFDR QHLLREPCEN YMRCVSVLRF
1260 1270 1280 1290 1300
DSSAPFIASS SVLFRPIHLV GGLRCRCPPG LTGDYCETEV DLCYSRTCGP
1310 1320 1330 1340 1350
HGRCRSREGG YTCLCRGCYT GEHCEASTHS GRCTPGVCKN GGTCVNLLVG
1360 1370 1380 1390 1400
GIKCDCPSGH FEKPFCQVTT RSFPARPFIT FRGLHQRFHF TLALSFATKE
1410 1420 1430 1440 1450
RNGLLLYNGR FNEKHDFVAL EVIQEQVQLT FSAGESTTTV SPFVPGGVSD
1460 1470 1480 1490 1500
GQWHTVQLKY YNKPLLGQTG LPQGPSEQKV AVVSVDGCDT GVALRFGAML
1510 1520 1530 1540 1550
GNYSCAAQGT QGGSKKSLDL TGPLLLGGVP DLPESFPVRM RHFVGCMKDL
1560 1570 1580 1590 1600
QVDSRHIDMA DFIANNGTVP GCPTKKIVCD SSICHNGGTC VNQWNTFSCE
1610 1620 1630 1640 1650
CPLGFGGKSC AQEMANPQRF LGSSLVAWHG LYLPISQPWH LNLMFRTRQA
1660 1670 1680 1690 1700
DGVLLQAVTR GRSTITLQLR AGHVRLSMEG TGLQASSLHL EPGRANDGDW
1710 1720 1730 1740 1750
HHAQLALGAS RGPGHAILSF NYGQQTAEGN LGPRLHGLHL SNITVGGVPG
1760 1770 1780 1790 1800
PASGVARGFR GCLQGVRVSE TPEGVHSLDP SRGESINVEP GCSLPDPCDS
1810 1820 1830 1840 1850
NPCPTNSYYS NDWNSYSCSC VLGYYGDNCT NVCDLNPCEH QSVCTRKPNT
1860 1870 1880 1890 1900
PHGYICECLP NYLGPYCETR IDQPCPRGWW GHPTCGPCNC DVSKGFDPDC
1910 1920 1930 1940 1950
NKTSGECHCK EKHYRPPGSP TCLLCDCYPT GSLSRVCDPE DGQCPCKPGV
1960 1970 1980 1990 2000
IGRQCDRCDN PFAEVTTNGC EVNYDSCPRA IEAGIWWPRT RFGLPAAAPC
2010 2020 2030 2040 2050
PKGSFGTAVR HCDEHRGWLP PNLFNCTSVT FSELKGFAER LQRNESGLDS
2060 2070 2080 2090 2100
GRSQRLALLL RNATQHTSGY FGSDVKVAYQ LATRLLAHES AQRGFGLSAT
2110 2120 2130 2140 2150
QDVHFTENLL RVGSALLDAA NKRHWELIQQ TEGGTAWLLQ HYEAYASALA
2160 2170 2180 2190 2200
QNMRHTYLSP FTIVTPNIVI SVVRLDKGNF AGTKLPRYEA LRGERPPDVE
2210 2220 2230 2240 2250
TTVILPESVF REMPSMVRSA GPGEAQETEE LARRQRRHPE LSQGEAVASV
2260 2270 2280 2290 2300
IIYHTLAGLL PHNYDPDKRS LRVPKRPVIN TPAVSISVHD DEELLPRALD
2310 2320 2330 2340 2350
KPVTVQFRLL ETEERTKPIC VFWNHSILVS GTGGWSARGC EVVFRNESHV
2360 2370 2380 2390 2400
SCQCNHMTSF AVLMDMSRRE NGEILPLKTL TYVALGVTLA ALMLTFLFLT
2410 2420 2430 2440 2450
LLRALRSNQH GIRRNLTAAL GLAQLVFLLG INQADLPFAC TVIAILLHFL
2460 2470 2480 2490 2500
YLCTFSWALL EALHLYRALT EVRDVNASPM RFYYMLGWGV PAFITGLAVG
2510 2520 2530 2540 2550
LDPEGYGNPD FCWLSVYDTL IWSFAGPVAF AVSMSVFLYI LSARASCAAQ
2560 2570 2580 2590 2600
RQGFEKKGPV SGLRSSFTVL LLLSATWLLA LLSVNSDTLL FHYLFAACNC
2610 2620 2630 2640 2650
VQGPFIFLSY VVLSKEVRKA LKFACSRKPS PDPALTTKYT LTSSYNCPSP
2660 2670 2680 2690 2700
YADGRLYQPY GDSAGSLHSA SRSGKSQPSY IPFLLREEST LNPGQVPPGL
2710 2720 2730 2740 2750
GDPSGLFLEG QAQQHDPDTD SDSDLSLEDD QSGSYASTHS SDSEEEEEEA
2760 2770 2780 2790 2800
AFPGEQGWDS LLGPGAERLP LHSTPKDGGP GSGKVPWLGD FGTTTKENSG
2810 2820 2830 2840 2850
SGALEERPRE NGDALTREGS LGPLPGPSTQ PHKGILKKKC LPTISEKSSL
2860 2870 2880 2890 2900
LRLPLEQGTG SSRGSSISEG SRHGPPPRPP PRQSLQEQLN GVMPVAMSIN
2910 2920
AGTVDEDSSG SEFLFFNFLH
Length:2,920
Mass (Da):317,593
Last modified:August 2, 2002 - v2
Checksum:iB412317C916E73A9
GO
Isoform 2 (identifier: Q9R0M0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2913-2920: Missing.

Note: No experimental confirmation available.
Show »
Length:2,912
Mass (Da):316,527
Checksum:iF8539CB86350C0E3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti2199V → L in AAH05499 (PubMed:15489334).Curated1
Sequence conflicti2283A → V in AAH05499 (PubMed:15489334).Curated1
Sequence conflicti2535S → R in BAA84070 (PubMed:10490098).Curated1
Sequence conflicti2571L → R in AAC68837 (PubMed:10790539).Curated1
Sequence conflicti2639Y → S in AAH05499 (PubMed:15489334).Curated1
Sequence conflicti2761L → C in BAA84070 (PubMed:10490098).Curated1
Sequence conflicti2796K → R in AAC68837 (PubMed:10790539).Curated1
Sequence conflicti2803A → P in AAH05499 (PubMed:15489334).Curated1
Sequence conflicti2900N → K in AAH05499 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0257652913 – 2920Missing in isoform 2. 1 Publication8

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB028499 mRNA. Translation: BAA84070.1.
AF031573 mRNA. Translation: AAC68837.1.
BC005499 mRNA. Translation: AAH05499.1.
UniGeneiMm.39728.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB028499 mRNA. Translation: BAA84070.1.
AF031573 mRNA. Translation: AAC68837.1.
BC005499 mRNA. Translation: AAH05499.1.
UniGeneiMm.39728.

3D structure databases

ProteinModelPortaliQ9R0M0.
SMRiQ9R0M0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9R0M0. 1 interactor.
MINTiMINT-5202369.
STRINGi10090.ENSMUSP00000088046.

Protein family/group databases

MEROPSiP02.006.
GPCRDBiSearch...

PTM databases

iPTMnetiQ9R0M0.
PhosphoSitePlusiQ9R0M0.

Proteomic databases

PaxDbiQ9R0M0.
PRIDEiQ9R0M0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:1858235. Celsr2.

Phylogenomic databases

eggNOGiKOG4289. Eukaryota.
ENOG410XTGH. LUCA.
HOGENOMiHOG000231346.
HOVERGENiHBG050887.
InParanoidiQ9R0M0.
PhylomeDBiQ9R0M0.

Miscellaneous databases

ChiTaRSiCelsr2. mouse.
PROiQ9R0M0.
SOURCEiSearch...

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. 1 hit.
PF16489. GAIN. 1 hit.
PF01825. GPS. 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. 1 hit.
PS00232. CADHERIN_1. 6 hits.
PS50268. CADHERIN_2. 9 hits.
PS00022. EGF_1. 6 hits.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 5 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 nameiCELR2_MOUSE
AccessioniPrimary (citable) accession number: Q9R0M0
Secondary accession number(s): Q99K26, Q9Z2R4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: August 2, 2002
Last modified: November 2, 2016
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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.