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Protein

Cadherin EGF LAG seven-pass G-type receptor 3

Gene

Celsr3

Organism
Rattus norvegicus (Rat)
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

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 3
Alternative name(s):
Multiple epidermal growth factor-like domains protein 2
Short name:
Multiple EGF-like domains protein 2
Gene namesi
Name:Celsr3
Synonyms:Megf2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 8

Organism-specific databases

RGDi621787. Celsr3.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini32 – 2538ExtracellularSequence analysisAdd BLAST2507
Transmembranei2539 – 2559Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini2560 – 2570CytoplasmicSequence analysisAdd BLAST11
Transmembranei2571 – 2591Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini2592 – 2599ExtracellularSequence analysis8
Transmembranei2600 – 2620Helical; Name=3Sequence analysisAdd BLAST21
Topological domaini2621 – 2641CytoplasmicSequence analysisAdd BLAST21
Transmembranei2642 – 2662Helical; Name=4Sequence analysisAdd BLAST21
Topological domaini2663 – 2679ExtracellularSequence analysisAdd BLAST17
Transmembranei2680 – 2700Helical; Name=5Sequence analysisAdd BLAST21
Topological domaini2701 – 2724CytoplasmicSequence analysisAdd BLAST24
Transmembranei2725 – 2745Helical; Name=6Sequence analysisAdd BLAST21
Topological domaini2746 – 2752ExtracellularSequence analysis7
Transmembranei2753 – 2773Helical; Name=7Sequence analysisAdd BLAST21
Topological domaini2774 – 3313CytoplasmicSequence analysisAdd BLAST540

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 31Sequence analysisAdd BLAST31
ChainiPRO_000001292032 – 3313Cadherin EGF LAG seven-pass G-type receptor 3Add BLAST3282

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi623N-linked (GlcNAc...)Sequence analysis1
Glycosylationi838N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1173N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1213N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1308N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1318N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1370 ↔ 1381By similarity
Disulfide bondi1375 ↔ 1412By similarity
Disulfide bondi1414 ↔ 1423By similarity
Disulfide bondi1430 ↔ 1441By similarity
Disulfide bondi1435 ↔ 1450By similarity
Disulfide bondi1452 ↔ 1461By similarity
Disulfide bondi1470 ↔ 1481By similarity
Disulfide bondi1475 ↔ 1491By similarity
Disulfide bondi1493 ↔ 1504By similarity
Glycosylationi1640N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1684 ↔ 1710By similarity
Glycosylationi1704N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1717 ↔ 1728By similarity
Disulfide bondi1722 ↔ 1737By similarity
Disulfide bondi1739 ↔ 1748By similarity
Glycosylationi1761N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1906 ↔ 1935By similarity
Disulfide bondi1941 ↔ 1952By similarity
Disulfide bondi1946 ↔ 1961By similarity
Modified residuei1954(3R)-3-hydroxyaspartateSequence analysis1
Disulfide bondi1963 ↔ 1972By similarity
Disulfide bondi1976 ↔ 1987By similarity
Disulfide bondi1981 ↔ 1999By similarity
Disulfide bondi2001 ↔ 2010By similarity
Disulfide bondi2018 ↔ 2031By similarity
Disulfide bondi2033 ↔ 2043By similarity
Glycosylationi2044N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2050 ↔ 2065By similarity
Disulfide bondi2052 ↔ 2068By similarity
Disulfide bondi2070 ↔ 2080By similarity
Disulfide bondi2089 ↔ 2098By similarity
Disulfide bondi2101 ↔ 2113By similarity
Modified residuei2117PhosphotyrosineCombined sources1
Glycosylationi2173N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2192N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2382N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2472N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2504N-linked (GlcNAc...)Sequence analysis1
Modified residuei3050PhosphotyrosineCombined sources1
Modified residuei3098PhosphoserineCombined 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

PaxDbiO88278.
PRIDEiO88278.

PTM databases

iPTMnetiO88278.
PhosphoSitePlusiO88278.

Expressioni

Tissue specificityi

Expressed in the brain. Expressed in cerebellum, olfactory bulb, cerebral cortex, hippocampus and brain stem.

Gene expression databases

BgeeiENSRNOG00000034005.
GenevisibleiO88278. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000041011.

Structurei

3D structure databases

ProteinModelPortaliO88278.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini317 – 424Cadherin 1PROSITE-ProRule annotationAdd BLAST108
Domaini425 – 536Cadherin 2PROSITE-ProRule annotationAdd BLAST112
Domaini537 – 642Cadherin 3PROSITE-ProRule annotationAdd BLAST106
Domaini643 – 747Cadherin 4PROSITE-ProRule annotationAdd BLAST105
Domaini748 – 849Cadherin 5PROSITE-ProRule annotationAdd BLAST102
Domaini850 – 952Cadherin 6PROSITE-ProRule annotationAdd BLAST103
Domaini953 – 1058Cadherin 7PROSITE-ProRule annotationAdd BLAST106
Domaini1059 – 1160Cadherin 8PROSITE-ProRule annotationAdd BLAST102
Domaini1161 – 1257Cadherin 9PROSITE-ProRule annotationAdd BLAST97
Domaini1366 – 1424EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd BLAST59
Domaini1426 – 1462EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1466 – 1505EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Domaini1506 – 1710Laminin G-like 1PROSITE-ProRule annotationAdd BLAST205
Domaini1713 – 1749EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1753 – 1935Laminin G-like 2PROSITE-ProRule annotationAdd BLAST183
Domaini1937 – 1972EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini1973 – 2011EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini2012 – 2044EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd BLAST33
Domaini2046 – 2081EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini2068 – 2115Laminin EGF-likePROSITE-ProRule annotationAdd BLAST48
Domaini2475 – 2527GPSPROSITE-ProRule annotationAdd BLAST53

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.
InParanoidiO88278.
KOiK04602.
OMAiYRFVGPP.
OrthoDBiEOG091G0039.
PhylomeDBiO88278.

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.
IPR032471. GAIN_dom_N.
IPR017981. GPCR_2-like.
IPR001879. GPCR_2_extracellular_dom.
IPR000832. GPCR_2_secretin-like.
IPR017983. GPCR_2_secretin-like_CS.
IPR000203. GPS.
IPR002049. Laminin_EGF.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF00002. 7tm_2. 1 hit.
PF00028. Cadherin. 8 hits.
PF00008. EGF. 3 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.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS00232. CADHERIN_1. 7 hits.
PS50268. CADHERIN_2. 8 hits.
PS00022. EGF_1. 6 hits.
PS01186. EGF_2. 4 hits.
PS50026. EGF_3. 6 hits.
PS01248. EGF_LAM_1. 1 hit.
PS50027. EGF_LAM_2. 1 hit.
PS00650. G_PROTEIN_RECEP_F2_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.

O88278-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARRPLWWGL PGPSTPLLLL LLFSLFPSSR EEMGGGGDQG WDPGVATATG
60 70 80 90 100
PRAQIGSGAV ALCPESPGVW EDGDPGLGVR EPVFMKLRVG RQNARNGRGA
110 120 130 140 150
PEQPNREPVV QALGSREQEA GQGSGYLLCW HPEISSCGRT GHLRRGSLPL
160 170 180 190 200
DALSPGDSDL RNSSPHPSEL LAQPDSPRPV AFQRNGRRSI RKRVETFRCC
210 220 230 240 250
GKLWEPGHKG QGERSATSTV DRGPLRRDCL PGSLGSGLGE DSAPRAVRTA
260 270 280 290 300
PAPGSAPHES RTAPERMRSR GLFRRGFLFE RPGPRPPGFP TGAEAKRILS
310 320 330 340 350
TNQARSRRAA NRHPQFPQYN YQTLVPENEA AGTAVLRVVA QDPDPGEAGR
360 370 380 390 400
LVYSLAALMN SRSLELFSID PQSGLIRTAA ALDRESMERH YLRVTAQDHG
410 420 430 440 450
SPRLSATTMV AVTVADRNDH APVFEQAQYR ETLRENVEEG YPILQLRATD
460 470 480 490 500
GDAPPNANLR YRFVGSPAAR TAAAAAFEID PRSGLISTSG RVDREHMESY
510 520 530 540 550
ELVVEASDQG QEPGPRSATV RVHITVLDEN DNAPQFSEKR YVAQVREDVR
560 570 580 590 600
PHTVVLRVTA TDKDKDANGL VHYNIISGNS RGHFAIDSLT GEIQVMAPLD
610 620 630 640 650
FEAEREYALR IRAQDAGRPP LSNNTGLASI QVVDINDHSP IFVSTPFQVS
660 670 680 690 700
VLENAPLGHS VIHIQAVDAD HGENSRLEYS LTGVASDTPF VINSATGWVS
710 720 730 740 750
VSGPLDRESV EHYFFGVEAR DHGSPPLSAS ASVTVTVLDV NDNRPEFTMK
760 770 780 790 800
EYHLRLNEDA AVGTSVVSVT AVDRDANSAI SYQITGGNTR NRFAISTQGG
810 820 830 840 850
MGLVTLALPL DYKQERYFKL VLTASDRALH DHCYVHINIT DANTHRPVFQ
860 870 880 890 900
SAHYSVSMNE DRPVGSTVVV ISASDDDVGE NARITYLLED NLPQFRIDAD
910 920 930 940 950
SGAITLQAPL DYEDQVTYTL AITARDNGIP QKADTTYVEV MVNDVNDNAP
960 970 980 990 1000
QFVASHYTGL VSEDAPPFTS VLQISATDRD AHANGRVQYT FQNGEDGDGD
1010 1020 1030 1040 1050
FTIEPTSGIV RTVRRLDREA VPVYELTAYA VDRGVPPLRT PVSIQVTVQD
1060 1070 1080 1090 1100
VNDNAPVFPA EEFEVRVKEN SIVGSVVAQI TAVDPDDGPN AHIMYQIVEG
1110 1120 1130 1140 1150
NIPELFQMDI FSGELTALID LDYEARQEYV IVVQATSAPL VSRATVHVRL
1160 1170 1180 1190 1200
VDQNDNSPVL NNFQILFNNY VSNRSDTFPS GIIGRIPAYD PDVSDHLFYS
1210 1220 1230 1240 1250
FERGNELQLL VVNQTSGELR LSRKLDNNRP LVASMLVTVT DGLHSVTAQC
1260 1270 1280 1290 1300
VLRVVIITEE LLANSLTVRL ENMWQERFLS PLLGHFLEGV AAVLATPTED
1310 1320 1330 1340 1350
VFIFNIQNDT DVGGTVLNVS FSALAPRGAG AGAAGPWFSS EELQEQLYVR
1360 1370 1380 1390 1400
RAALAARSLL DVLPFDDNVC LREPCENYMK CVSVLRFDSS APFLASASTL
1410 1420 1430 1440 1450
FRPIQPIAGL RCRCPPGFTG DFCETELDLC YSNPCRNGGA CARREGGYTC
1460 1470 1480 1490 1500
VCRPRFTGED CELDTEAGRC VPGVCRNGGT CTNAPNGGFR CQCPAGGAFE
1510 1520 1530 1540 1550
GPRCEVAARS FPPSSFVMFR GLRQRFHLTL SLSFATVQPS GLLFYNGRLN
1560 1570 1580 1590 1600
EKHDFLALEL VAGQVRLTYS TGESSTVVSP TVPGGLSDGQ WHTVHLRYYN
1610 1620 1630 1640 1650
KPRTDALGGA QGPSKDKVAV LSVDDCNVAV ALRFGAEIGN YSCAAAGVQT
1660 1670 1680 1690 1700
SSKKSLDLTG PLLLGGVPNL PENFPVSRKD FIGCMRDLHI DGRRVDMAAF
1710 1720 1730 1740 1750
VANNGTTAGC QAKSHFCASG PCKNGGLCSE RWGGFSCDCP VGFGGKDCRL
1760 1770 1780 1790 1800
TMAHPYHFQG NGTLSWDFGN DMPVSVPWYL GLSFRTRATK GVLMQVQLGP
1810 1820 1830 1840 1850
HSVLLCKLDQ GLLSVTLSRA SGHAVHLLLD QMTVSDGRWH DLRLELQEEP
1860 1870 1880 1890 1900
GGRRGHHIFM VSLDFTLFQD TMAMGSELEG LKVKHLHVGG PPPSSKEEGP
1910 1920 1930 1940 1950
QGLVGCIQGV WTGFTPFGSS ALPPPSHRIN VEPGCTVTNP CASGPCPPHA
1960 1970 1980 1990 2000
NCKDLWQTFS CTCWPGYYGP GCVDACLLNP CQNQGSCRHL QGGPHGYTCD
2010 2020 2030 2040 2050
CASGYFGQHC EHRMDQQCPR GWWGSPTCGP CNCDVHKGFD PNCNKTSGQC
2060 2070 2080 2090 2100
HCKEFHYRPR GSDSCLPCDC YPVGSTSRSC APHSGQCPCR PGALGRQCNS
2110 2120 2130 2140 2150
CDSPFAEVTA SGCRVLYDAC PKSLRSGVWW PQTKFGVLAT VPCPRGALGL
2160 2170 2180 2190 2200
RGTGAAVRLC DEDHGWLEPD FFNCTSPAFR ELSLLLDGLE LNKTALDTVE
2210 2220 2230 2240 2250
AKKLAQRLRE VTGQTDHYFS QDVRVTARLL AYLLAFESHQ QGFGLTATQD
2260 2270 2280 2290 2300
AHFNENLLWA GSALLAPETG DLWAALGQRA PGGSPGSAGL VRHLEEYAAT
2310 2320 2330 2340 2350
LARNMDLTYL NPVGLVTPNI MLSIDRMEQP SSSQGAHRYP RYHSNLFRGQ
2360 2370 2380 2390 2400
DAWDPHTHVL LPSQSPQPSP SEVLPTSSNA ENATASGVVS PPAPLEPESE
2410 2420 2430 2440 2450
PGISIVILLV YRALGGLLPA QFQAERRGAR LPQNPVMNSP VVSVAVFRGR
2460 2470 2480 2490 2500
NFLRGALVSP INLEFRLLQT ANRSKAICVQ WDPPGPADQH GMWTARDCEL
2510 2520 2530 2540 2550
VHRNGSHARC RCSRTGTFGV LMDASPRERL EGDLELLAVF THVVVAASVT
2560 2570 2580 2590 2600
ALVLTAAVLL SLRSLKSNVR GIHANVAAAL GVAELLFLLG IHRTHNQLLC
2610 2620 2630 2640 2650
TVVAILLHYF FLSTFAWLLV QGLHLYRMQV EPRNVDRGAM RFYHALGWGV
2660 2670 2680 2690 2700
PAVLLGLAVG LDPEGYGNPD FCWISIHEPL IWSFAGPIVL VIVMNGIMFL
2710 2720 2730 2740 2750
LAARTSCSTG QREAKKTSVL RTLRSSFLLL LLVSASWLFG LLAVNHSVLA
2760 2770 2780 2790 2800
FHYLHAGLCG LQGLAVLLLF CVLNADARAA WTPACLGKKA APEETRPAPG
2810 2820 2830 2840 2850
PGSGAYNNTA LFEESGLIRI TLGASTVSSV SSARSGRAQD QDSQRGRSYL
2860 2870 2880 2890 2900
RDNVLVRHGS TAEHAEHSLQ AHAGPTDLDV AMFHRDAGAD SDSDSDLSLE
2910 2920 2930 2940 2950
EERSLSIPSS ESEDNGRTRG RFQRPLRRAA QSERLLAHPK DVDGNDLLSY
2960 2970 2980 2990 3000
WPALGECEAA PCALQAWGSE RRLGLDSNKD AANNNQPELA LTSGDETSLG
3010 3020 3030 3040 3050
RAQRQRKGIL KNRLQYPLVP QTRGTPELSW CRAATLGHRA VPAASYGRIY
3060 3070 3080 3090 3100
AGGGTGSLSQ PASRYSSREQ LDLLLRRQLS RERLEEVPVP APVLHPLSRP
3110 3120 3130 3140 3150
GSQERLDTAP ARLEPRDRGS TLPRRQPPRD YPGTMAGRFG SRDALDLGAP
3160 3170 3180 3190 3200
REWLSTLPPP RRNRDLDPQH PPLPLSPQRP LSRDPLLPSR PLDSLSRISN
3210 3220 3230 3240 3250
SRERLDQVPS RHPSREALGP APQLLRARED PASGPSHGPS TEQLDILSSI
3260 3270 3280 3290 3300
LASFNSSALS SVQSSSTPSG PHTTATPSAT ASALGPSTPR SATSHSISEL
3310
SPDSEVPRSE GHS
Length:3,313
Mass (Da):359,355
Last modified:November 1, 1998 - v1
Checksum:iB11DA09517288764
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB011528 mRNA. Translation: BAA32459.1.
RefSeqiNP_112610.1. NM_031320.1.
UniGeneiRn.14558.

Genome annotation databases

EnsembliENSRNOT00000084220; ENSRNOP00000068821; ENSRNOG00000053889.
GeneIDi83466.
KEGGirno:83466.
UCSCiRGD:621787. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB011528 mRNA. Translation: BAA32459.1.
RefSeqiNP_112610.1. NM_031320.1.
UniGeneiRn.14558.

3D structure databases

ProteinModelPortaliO88278.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000041011.

Protein family/group databases

GPCRDBiSearch...

PTM databases

iPTMnetiO88278.
PhosphoSitePlusiO88278.

Proteomic databases

PaxDbiO88278.
PRIDEiO88278.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000084220; ENSRNOP00000068821; ENSRNOG00000053889.
GeneIDi83466.
KEGGirno:83466.
UCSCiRGD:621787. rat.

Organism-specific databases

CTDi1951.
RGDi621787. Celsr3.

Phylogenomic databases

eggNOGiKOG4289. Eukaryota.
ENOG410XTGH. LUCA.
GeneTreeiENSGT00760000118805.
HOGENOMiHOG000231346.
HOVERGENiHBG050887.
InParanoidiO88278.
KOiK04602.
OMAiYRFVGPP.
OrthoDBiEOG091G0039.
PhylomeDBiO88278.

Miscellaneous databases

PROiO88278.

Gene expression databases

BgeeiENSRNOG00000034005.
GenevisibleiO88278. RN.

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.
IPR032471. GAIN_dom_N.
IPR017981. GPCR_2-like.
IPR001879. GPCR_2_extracellular_dom.
IPR000832. GPCR_2_secretin-like.
IPR017983. GPCR_2_secretin-like_CS.
IPR000203. GPS.
IPR002049. Laminin_EGF.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF00002. 7tm_2. 1 hit.
PF00028. Cadherin. 8 hits.
PF00008. EGF. 3 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.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS00232. CADHERIN_1. 7 hits.
PS50268. CADHERIN_2. 8 hits.
PS00022. EGF_1. 6 hits.
PS01186. EGF_2. 4 hits.
PS50026. EGF_3. 6 hits.
PS01248. EGF_LAM_1. 1 hit.
PS50027. EGF_LAM_2. 1 hit.
PS00650. G_PROTEIN_RECEP_F2_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 nameiCELR3_RAT
AccessioniPrimary (citable) accession number: O88278
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: November 1, 1998
Last modified: November 2, 2016
This is version 143 of the entry and version 1 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. 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.