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O88278

- CELR3_RAT

UniProt

O88278 - CELR3_RAT

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Protein

Cadherin EGF LAG seven-pass G-type receptor 3

Gene

Celsr3

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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

  1. calcium ion binding Source: InterPro
  2. G-protein coupled receptor activity Source: UniProtKB-KW

GO - Biological processi

  1. axonal fasciculation Source: Ensembl
  2. cilium assembly Source: Ensembl
  3. homophilic cell adhesion via plasma membrane adhesion molecules Source: InterPro
  4. neuron migration Source: Ensembl
  5. neuropeptide signaling pathway Source: InterPro
  6. regulation of protein localization Source: Ensembl
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
ProteomesiUP000002494: Chromosome 8

Organism-specific databases

RGDi621787. Celsr3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini32 – 25382507ExtracellularSequence AnalysisAdd
BLAST
Transmembranei2539 – 255921Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini2560 – 257011CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei2571 – 259121Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini2592 – 25998ExtracellularSequence Analysis
Transmembranei2600 – 262021Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini2621 – 264121CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei2642 – 266221Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini2663 – 267917ExtracellularSequence AnalysisAdd
BLAST
Transmembranei2680 – 270021Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini2701 – 272424CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei2725 – 274521Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini2746 – 27527ExtracellularSequence Analysis
Transmembranei2753 – 277321Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini2774 – 3313540CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Sequence AnalysisAdd
BLAST
Chaini32 – 33133282Cadherin EGF LAG seven-pass G-type receptor 3PRO_0000012920Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi623 – 6231N-linked (GlcNAc...)Sequence Analysis
Glycosylationi838 – 8381N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1173 – 11731N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1213 – 12131N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1308 – 13081N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1318 – 13181N-linked (GlcNAc...)Sequence Analysis
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
Glycosylationi1640 – 16401N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1684 ↔ 1710By similarity
Glycosylationi1704 – 17041N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1717 ↔ 1728By similarity
Disulfide bondi1722 ↔ 1737By similarity
Disulfide bondi1739 ↔ 1748By similarity
Glycosylationi1761 – 17611N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1906 ↔ 1935By similarity
Disulfide bondi1941 ↔ 1952By similarity
Disulfide bondi1946 ↔ 1961By similarity
Modified residuei1954 – 19541(3R)-3-hydroxyaspartateSequence Analysis
Disulfide bondi1963 ↔ 1972By similarity
Disulfide bondi1976 ↔ 1987By similarity
Disulfide bondi1981 ↔ 1999By similarity
Disulfide bondi2001 ↔ 2010By similarity
Disulfide bondi2018 ↔ 2031By similarity
Disulfide bondi2033 ↔ 2043By similarity
Glycosylationi2044 – 20441N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2050 ↔ 2065By similarity
Disulfide bondi2052 ↔ 2068By similarity
Disulfide bondi2070 ↔ 2080By similarity
Disulfide bondi2089 ↔ 2098By similarity
Disulfide bondi2101 ↔ 2113By similarity
Modified residuei2117 – 21171Phosphotyrosine1 Publication
Glycosylationi2173 – 21731N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2192 – 21921N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2382 – 23821N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2472 – 24721N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2504 – 25041N-linked (GlcNAc...)Sequence Analysis
Modified residuei3050 – 30501Phosphotyrosine1 Publication
Modified residuei3098 – 30981Phosphoserine1 Publication

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

PhosphoSiteiO88278.

Expressioni

Tissue specificityi

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

Gene expression databases

GenevestigatoriO88278.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000041011.

Structurei

3D structure databases

ProteinModelPortaliO88278.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini317 – 424108Cadherin 1PROSITE-ProRule annotationAdd
BLAST
Domaini425 – 536112Cadherin 2PROSITE-ProRule annotationAdd
BLAST
Domaini537 – 642106Cadherin 3PROSITE-ProRule annotationAdd
BLAST
Domaini643 – 747105Cadherin 4PROSITE-ProRule annotationAdd
BLAST
Domaini748 – 849102Cadherin 5PROSITE-ProRule annotationAdd
BLAST
Domaini850 – 952103Cadherin 6PROSITE-ProRule annotationAdd
BLAST
Domaini953 – 1058106Cadherin 7PROSITE-ProRule annotationAdd
BLAST
Domaini1059 – 1160102Cadherin 8PROSITE-ProRule annotationAdd
BLAST
Domaini1161 – 125797Cadherin 9PROSITE-ProRule annotationAdd
BLAST
Domaini1366 – 142459EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1426 – 146237EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1466 – 150540EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1506 – 1710205Laminin G-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini1713 – 174937EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1753 – 1935183Laminin G-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini1937 – 197236EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1973 – 201139EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2012 – 204433EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2046 – 208136EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2068 – 211548Laminin EGF-likePROSITE-ProRule annotationAdd
BLAST
Domaini2475 – 252753GPSPROSITE-ProRule annotationAdd
BLAST

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

eggNOGiNOG12793.
GeneTreeiENSGT00760000118805.
HOGENOMiHOG000231346.
HOVERGENiHBG050887.
InParanoidiO88278.
KOiK04602.
OMAiYRFVGPP.
OrthoDBiEOG7BP81K.
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.
IPR022624. DUF3497.
IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR002049. EGF_laminin.
IPR017981. GPCR_2-like.
IPR001879. GPCR_2_extracellular_dom.
IPR000832. GPCR_2_secretin-like.
IPR017983. GPCR_2_secretin-like_CS.
IPR000203. GPS.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF00002. 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]
PRINTSiPR00205. CADHERIN.
PR00249. GPCRSECRETIN.
SMARTiSM00112. 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]
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

EnsembliENSRNOT00000040661; ENSRNOP00000041011; ENSRNOG00000034005.
GeneIDi83466.
KEGGirno:83466.
UCSCiRGD:621787. rat.

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.
UniGenei Rn.14558.

3D structure databases

ProteinModelPortali O88278.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000041011.

Protein family/group databases

GPCRDBi Search...

PTM databases

PhosphoSitei O88278.

Proteomic databases

PaxDbi O88278.
PRIDEi O88278.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000040661 ; ENSRNOP00000041011 ; ENSRNOG00000034005 .
GeneIDi 83466.
KEGGi rno:83466.
UCSCi RGD:621787. rat.

Organism-specific databases

CTDi 1951.
RGDi 621787. Celsr3.

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00760000118805.
HOGENOMi HOG000231346.
HOVERGENi HBG050887.
InParanoidi O88278.
KOi K04602.
OMAi YRFVGPP.
OrthoDBi EOG7BP81K.
PhylomeDBi O88278.

Miscellaneous databases

NextBioi 615859.

Gene expression databases

Genevestigatori O88278.

Family and domain databases

Gene3Di 2.60.120.200. 2 hits.
2.60.40.60. 9 hits.
InterProi IPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR013320. ConA-like_dom.
IPR022624. DUF3497.
IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR002049. EGF_laminin.
IPR017981. GPCR_2-like.
IPR001879. GPCR_2_extracellular_dom.
IPR000832. GPCR_2_secretin-like.
IPR017983. GPCR_2_secretin-like_CS.
IPR000203. GPS.
IPR001791. Laminin_G.
[Graphical view ]
Pfami 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 ]
PRINTSi PR00205. CADHERIN.
PR00249. GPCRSECRETIN.
SMARTi 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 ]
SUPFAMi SSF49313. SSF49313. 9 hits.
SSF49899. SSF49899. 2 hits.
PROSITEi 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.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of high-molecular-weight proteins with multiple EGF-like motifs by motif-trap screening."
    Nakayama M., Nakajima D., Nagase T., Nomura N., Seki N., Ohara O.
    Genomics 51:27-34(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Brain.
  2. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
    Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
    Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-2117; TYR-3050 AND SER-3098, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

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: October 29, 2014
This is version 129 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

External Data

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