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UniProtKB - O88278 (CELR3_RAT)
Protein
Cadherin EGF LAG seven-pass G-type receptor 3
Gene
Celsr3
Organism
Rattus norvegicus (Rat)
Status
Functioni
Receptor that may have an important role in cell/cell signaling during nervous system formation.
GO - Molecular functioni
- calcium ion binding Source: InterPro
- G protein-coupled receptor activity Source: UniProtKB-KW
GO - Biological processi
- axonal fasciculation Source: RGD
- cell-cell adhesion Source: GO_Central
- cilium assembly Source: RGD
- dopaminergic neuron axon guidance Source: RGD
- homophilic cell adhesion via plasma membrane adhesion molecules Source: InterPro
- neuron migration Source: RGD
- planar cell polarity pathway involved in axon guidance Source: RGD
- regulation of protein localization Source: RGD
- regulation of protein phosphorylation Source: RGD
- serotonergic neuron axon guidance Source: RGD
Keywordsi
Molecular function | Developmental protein, G-protein coupled receptor, Receptor, Transducer |
Ligand | Calcium |
Names & Taxonomyi
Protein namesi | Recommended name: Cadherin EGF LAG seven-pass G-type receptor 3Alternative name(s): Multiple epidermal growth factor-like domains protein 2 Short name: Multiple EGF-like domains protein 2 |
Gene namesi | Name:Celsr3 Synonyms:Megf2 |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 621787, Celsr3 |
Subcellular locationi
Plasma membrane
Plasma Membrane
- plasma membrane Source: UniProtKB-SubCell
Other locations
- integral component of membrane Source: UniProtKB-KW
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 32 – 2538 | ExtracellularSequence analysisAdd BLAST | 2507 | |
Transmembranei | 2539 – 2559 | Helical; Name=1Sequence analysisAdd BLAST | 21 | |
Topological domaini | 2560 – 2570 | CytoplasmicSequence analysisAdd BLAST | 11 | |
Transmembranei | 2571 – 2591 | Helical; Name=2Sequence analysisAdd BLAST | 21 | |
Topological domaini | 2592 – 2599 | ExtracellularSequence analysis | 8 | |
Transmembranei | 2600 – 2620 | Helical; Name=3Sequence analysisAdd BLAST | 21 | |
Topological domaini | 2621 – 2641 | CytoplasmicSequence analysisAdd BLAST | 21 | |
Transmembranei | 2642 – 2662 | Helical; Name=4Sequence analysisAdd BLAST | 21 | |
Topological domaini | 2663 – 2679 | ExtracellularSequence analysisAdd BLAST | 17 | |
Transmembranei | 2680 – 2700 | Helical; Name=5Sequence analysisAdd BLAST | 21 | |
Topological domaini | 2701 – 2724 | CytoplasmicSequence analysisAdd BLAST | 24 | |
Transmembranei | 2725 – 2745 | Helical; Name=6Sequence analysisAdd BLAST | 21 | |
Topological domaini | 2746 – 2752 | ExtracellularSequence analysis | 7 | |
Transmembranei | 2753 – 2773 | Helical; Name=7Sequence analysisAdd BLAST | 21 | |
Topological domaini | 2774 – 3313 | CytoplasmicSequence analysisAdd BLAST | 540 |
Keywords - Cellular componenti
Cell membrane, MembranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 31 | Sequence analysisAdd BLAST | 31 | |
ChainiPRO_0000012920 | 32 – 3313 | Cadherin EGF LAG seven-pass G-type receptor 3Add BLAST | 3282 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 623 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 838 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1173 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1213 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1308 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1318 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1370 ↔ 1381 | By similarity | ||
Disulfide bondi | 1375 ↔ 1412 | By similarity | ||
Disulfide bondi | 1414 ↔ 1423 | By similarity | ||
Disulfide bondi | 1430 ↔ 1441 | By similarity | ||
Disulfide bondi | 1435 ↔ 1450 | By similarity | ||
Disulfide bondi | 1452 ↔ 1461 | By similarity | ||
Disulfide bondi | 1470 ↔ 1481 | By similarity | ||
Disulfide bondi | 1475 ↔ 1491 | By similarity | ||
Disulfide bondi | 1493 ↔ 1504 | By similarity | ||
Glycosylationi | 1640 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1684 ↔ 1710 | By similarity | ||
Glycosylationi | 1704 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1717 ↔ 1728 | By similarity | ||
Disulfide bondi | 1722 ↔ 1737 | By similarity | ||
Disulfide bondi | 1739 ↔ 1748 | By similarity | ||
Glycosylationi | 1761 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1906 ↔ 1935 | By similarity | ||
Disulfide bondi | 1941 ↔ 1952 | By similarity | ||
Disulfide bondi | 1946 ↔ 1961 | By similarity | ||
Modified residuei | 1954 | (3R)-3-hydroxyaspartateSequence analysis | 1 | |
Disulfide bondi | 1963 ↔ 1972 | By similarity | ||
Disulfide bondi | 1976 ↔ 1987 | By similarity | ||
Disulfide bondi | 1981 ↔ 1999 | By similarity | ||
Disulfide bondi | 2001 ↔ 2010 | By similarity | ||
Disulfide bondi | 2018 ↔ 2031 | By similarity | ||
Disulfide bondi | 2033 ↔ 2043 | By similarity | ||
Glycosylationi | 2044 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 2050 ↔ 2065 | By similarity | ||
Disulfide bondi | 2052 ↔ 2068 | By similarity | ||
Disulfide bondi | 2070 ↔ 2080 | By similarity | ||
Disulfide bondi | 2089 ↔ 2098 | By similarity | ||
Disulfide bondi | 2101 ↔ 2113 | By similarity | ||
Modified residuei | 2117 | PhosphotyrosineCombined sources | 1 | |
Glycosylationi | 2173 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 2192 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 2382 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 2472 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 2504 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 3050 | PhosphotyrosineCombined sources | 1 | |
Modified residuei | 3098 | PhosphoserineCombined sources | 1 |
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, PhosphoproteinProteomic databases
PaxDbi | O88278 |
PRIDEi | O88278 |
PTM databases
GlyGeni | O88278, 15 sites |
iPTMneti | O88278 |
PhosphoSitePlusi | O88278 |
Expressioni
Tissue specificityi
Expressed in the brain. Expressed in cerebellum, olfactory bulb, cerebral cortex, hippocampus and brain stem.
Gene expression databases
Bgeei | ENSRNOG00000053889, Expressed in frontal cortex and 12 other tissues |
Genevisiblei | O88278, RN |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 317 – 424 | Cadherin 1PROSITE-ProRule annotationAdd BLAST | 108 | |
Domaini | 425 – 536 | Cadherin 2PROSITE-ProRule annotationAdd BLAST | 112 | |
Domaini | 537 – 642 | Cadherin 3PROSITE-ProRule annotationAdd BLAST | 106 | |
Domaini | 643 – 747 | Cadherin 4PROSITE-ProRule annotationAdd BLAST | 105 | |
Domaini | 748 – 849 | Cadherin 5PROSITE-ProRule annotationAdd BLAST | 102 | |
Domaini | 850 – 952 | Cadherin 6PROSITE-ProRule annotationAdd BLAST | 103 | |
Domaini | 953 – 1058 | Cadherin 7PROSITE-ProRule annotationAdd BLAST | 106 | |
Domaini | 1059 – 1160 | Cadherin 8PROSITE-ProRule annotationAdd BLAST | 102 | |
Domaini | 1161 – 1257 | Cadherin 9PROSITE-ProRule annotationAdd BLAST | 97 | |
Domaini | 1366 – 1424 | EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 59 | |
Domaini | 1426 – 1462 | EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 1466 – 1505 | EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 40 | |
Domaini | 1506 – 1710 | Laminin G-like 1PROSITE-ProRule annotationAdd BLAST | 205 | |
Domaini | 1713 – 1749 | EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 1753 – 1935 | Laminin G-like 2PROSITE-ProRule annotationAdd BLAST | 183 | |
Domaini | 1937 – 1972 | EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 36 | |
Domaini | 1973 – 2011 | EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 2012 – 2044 | EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 33 | |
Domaini | 2046 – 2081 | EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 36 | |
Domaini | 2068 – 2115 | Laminin EGF-likePROSITE-ProRule annotationAdd BLAST | 48 | |
Domaini | 2475 – 2527 | GPSPROSITE-ProRule annotationAdd BLAST | 53 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 148 – 187 | DisorderedSequence analysisAdd BLAST | 40 | |
Regioni | 205 – 269 | DisorderedSequence analysisAdd BLAST | 65 | |
Regioni | 2356 – 2395 | DisorderedSequence analysisAdd BLAST | 40 | |
Regioni | 2887 – 2927 | DisorderedSequence analysisAdd BLAST | 41 | |
Regioni | 2977 – 3004 | DisorderedSequence analysisAdd BLAST | 28 | |
Regioni | 3091 – 3242 | DisorderedSequence analysisAdd BLAST | 152 | |
Regioni | 3255 – 3313 | DisorderedSequence analysisAdd BLAST | 59 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 2360 – 2386 | Polar residuesSequence analysisAdd BLAST | 27 | |
Compositional biasi | 2978 – 2999 | Polar residuesSequence analysisAdd BLAST | 22 | |
Compositional biasi | 3109 – 3124 | Basic and acidic residuesSequence analysisAdd BLAST | 16 | |
Compositional biasi | 3197 – 3211 | Basic and acidic residuesSequence analysisAdd BLAST | 15 | |
Compositional biasi | 3255 – 3303 | Polar residuesSequence analysisAdd BLAST | 49 |
Sequence similaritiesi
Keywords - Domaini
EGF-like domain, Laminin EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG4289, Eukaryota |
GeneTreei | ENSGT00940000160077 |
HOGENOMi | CLU_000158_1_0_1 |
InParanoidi | O88278 |
OMAi | CNTCDNP |
OrthoDBi | 23882at2759 |
PhylomeDBi | O88278 |
Family and domain databases
CDDi | cd00055, EGF_Lam, 2 hits cd00110, LamG, 2 hits |
Gene3Di | 4.10.1240.10, 1 hit |
InterProi | View protein in InterPro IPR002126, Cadherin-like_dom IPR015919, Cadherin-like_sf IPR020894, Cadherin_CS IPR013320, ConA-like_dom_sf IPR001881, EGF-like_Ca-bd_dom IPR000742, EGF-like_dom IPR032471, GAIN_dom_N IPR017981, GPCR_2-like IPR036445, GPCR_2_extracell_dom_sf IPR001879, GPCR_2_extracellular_dom IPR000832, GPCR_2_secretin-like IPR017983, GPCR_2_secretin-like_CS IPR000203, GPS IPR001791, Laminin_G IPR002049, LE_dom |
Pfami | View protein in Pfam PF00002, 7tm_2, 1 hit PF00028, Cadherin, 8 hits PF00008, EGF, 3 hits PF16489, GAIN, 1 hit PF02793, HRM, 1 hit PF00053, Laminin_EGF, 1 hit PF02210, Laminin_G_2, 2 hits |
PRINTSi | PR00205, CADHERIN PR00249, GPCRSECRETIN |
SMARTi | View protein in SMART SM00112, 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 |
SUPFAMi | SSF111418, SSF111418, 1 hit SSF49313, SSF49313, 9 hits SSF49899, SSF49899, 2 hits |
PROSITEi | View protein in PROSITE PS00010, 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 |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
O88278-1 [UniParc]FASTAAdd to basket
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
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AB011528 mRNA Translation: BAA32459.1 |
RefSeqi | NP_112610.1, NM_031320.1 |
Genome annotation databases
Ensembli | ENSRNOT00000084220; ENSRNOP00000068821; ENSRNOG00000053889 |
GeneIDi | 83466 |
KEGGi | rno:83466 |
UCSCi | RGD:621787, rat |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AB011528 mRNA Translation: BAA32459.1 |
RefSeqi | NP_112610.1, NM_031320.1 |
3D structure databases
SMRi | O88278 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 10116.ENSRNOP00000041011 |
Protein family/group databases
GPCRDBi | Search... |
PTM databases
GlyGeni | O88278, 15 sites |
iPTMneti | O88278 |
PhosphoSitePlusi | O88278 |
Proteomic databases
PaxDbi | O88278 |
PRIDEi | O88278 |
Genome annotation databases
Ensembli | ENSRNOT00000084220; ENSRNOP00000068821; ENSRNOG00000053889 |
GeneIDi | 83466 |
KEGGi | rno:83466 |
UCSCi | RGD:621787, rat |
Organism-specific databases
CTDi | 1951 |
RGDi | 621787, Celsr3 |
Phylogenomic databases
eggNOGi | KOG4289, Eukaryota |
GeneTreei | ENSGT00940000160077 |
HOGENOMi | CLU_000158_1_0_1 |
InParanoidi | O88278 |
OMAi | CNTCDNP |
OrthoDBi | 23882at2759 |
PhylomeDBi | O88278 |
Miscellaneous databases
PROi | PR:O88278 |
Gene expression databases
Bgeei | ENSRNOG00000053889, Expressed in frontal cortex and 12 other tissues |
Genevisiblei | O88278, RN |
Family and domain databases
CDDi | cd00055, EGF_Lam, 2 hits cd00110, LamG, 2 hits |
Gene3Di | 4.10.1240.10, 1 hit |
InterProi | View protein in InterPro IPR002126, Cadherin-like_dom IPR015919, Cadherin-like_sf IPR020894, Cadherin_CS IPR013320, ConA-like_dom_sf IPR001881, EGF-like_Ca-bd_dom IPR000742, EGF-like_dom IPR032471, GAIN_dom_N IPR017981, GPCR_2-like IPR036445, GPCR_2_extracell_dom_sf IPR001879, GPCR_2_extracellular_dom IPR000832, GPCR_2_secretin-like IPR017983, GPCR_2_secretin-like_CS IPR000203, GPS IPR001791, Laminin_G IPR002049, LE_dom |
Pfami | View protein in Pfam PF00002, 7tm_2, 1 hit PF00028, Cadherin, 8 hits PF00008, EGF, 3 hits PF16489, GAIN, 1 hit PF02793, HRM, 1 hit PF00053, Laminin_EGF, 1 hit PF02210, Laminin_G_2, 2 hits |
PRINTSi | PR00205, CADHERIN PR00249, GPCRSECRETIN |
SMARTi | View protein in SMART SM00112, 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 |
SUPFAMi | SSF111418, SSF111418, 1 hit SSF49313, SSF49313, 9 hits SSF49899, SSF49899, 2 hits |
PROSITEi | View protein in PROSITE PS00010, 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 |
MobiDBi | Search... |
Entry informationi
Entry namei | CELR3_RAT | |
Accessioni | O88278Primary (citable) accession number: O88278 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 2, 2002 |
Last sequence update: | November 1, 1998 | |
Last modified: | February 23, 2022 | |
This is version 173 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- 7-transmembrane G-linked receptors
List of 7-transmembrane G-linked receptor entries - SIMILARITY comments
Index of protein domains and families