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O88278

- CELR3_RAT

UniProt

O88278 - CELR3_RAT

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
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    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 Source: InterPro
    4. neuron migration Source: Ensembl
    5. neuropeptide signaling pathway Source: InterPro
    6. regulation of protein localization Source: Ensembl

    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

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell

    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...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini32 – 25382507ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini2560 – 257011CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini2592 – 25998ExtracellularSequence Analysis
    Topological domaini2621 – 264121CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini2663 – 267917ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini2701 – 272424CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini2746 – 27527ExtracellularSequence Analysis
    Topological domaini2774 – 3313540CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei2539 – 255921Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei2571 – 259121Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei2600 – 262021Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei2642 – 266221Helical; Name=4Sequence AnalysisAdd
    BLAST
    Transmembranei2680 – 270021Helical; Name=5Sequence AnalysisAdd
    BLAST
    Transmembranei2725 – 274521Helical; Name=6Sequence AnalysisAdd
    BLAST
    Transmembranei2753 – 277321Helical; Name=7Sequence AnalysisAdd
    BLAST

    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.
    GeneTreeiENSGT00750000117340.
    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.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    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

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    MARRPLWWGL PGPSTPLLLL LLFSLFPSSR EEMGGGGDQG WDPGVATATG     50
    PRAQIGSGAV ALCPESPGVW EDGDPGLGVR EPVFMKLRVG RQNARNGRGA 100
    PEQPNREPVV QALGSREQEA GQGSGYLLCW HPEISSCGRT GHLRRGSLPL 150
    DALSPGDSDL RNSSPHPSEL LAQPDSPRPV AFQRNGRRSI RKRVETFRCC 200
    GKLWEPGHKG QGERSATSTV DRGPLRRDCL PGSLGSGLGE DSAPRAVRTA 250
    PAPGSAPHES RTAPERMRSR GLFRRGFLFE RPGPRPPGFP TGAEAKRILS 300
    TNQARSRRAA NRHPQFPQYN YQTLVPENEA AGTAVLRVVA QDPDPGEAGR 350
    LVYSLAALMN SRSLELFSID PQSGLIRTAA ALDRESMERH YLRVTAQDHG 400
    SPRLSATTMV AVTVADRNDH APVFEQAQYR ETLRENVEEG YPILQLRATD 450
    GDAPPNANLR YRFVGSPAAR TAAAAAFEID PRSGLISTSG RVDREHMESY 500
    ELVVEASDQG QEPGPRSATV RVHITVLDEN DNAPQFSEKR YVAQVREDVR 550
    PHTVVLRVTA TDKDKDANGL VHYNIISGNS RGHFAIDSLT GEIQVMAPLD 600
    FEAEREYALR IRAQDAGRPP LSNNTGLASI QVVDINDHSP IFVSTPFQVS 650
    VLENAPLGHS VIHIQAVDAD HGENSRLEYS LTGVASDTPF VINSATGWVS 700
    VSGPLDRESV EHYFFGVEAR DHGSPPLSAS ASVTVTVLDV NDNRPEFTMK 750
    EYHLRLNEDA AVGTSVVSVT AVDRDANSAI SYQITGGNTR NRFAISTQGG 800
    MGLVTLALPL DYKQERYFKL VLTASDRALH DHCYVHINIT DANTHRPVFQ 850
    SAHYSVSMNE DRPVGSTVVV ISASDDDVGE NARITYLLED NLPQFRIDAD 900
    SGAITLQAPL DYEDQVTYTL AITARDNGIP QKADTTYVEV MVNDVNDNAP 950
    QFVASHYTGL VSEDAPPFTS VLQISATDRD AHANGRVQYT FQNGEDGDGD 1000
    FTIEPTSGIV RTVRRLDREA VPVYELTAYA VDRGVPPLRT PVSIQVTVQD 1050
    VNDNAPVFPA EEFEVRVKEN SIVGSVVAQI TAVDPDDGPN AHIMYQIVEG 1100
    NIPELFQMDI FSGELTALID LDYEARQEYV IVVQATSAPL VSRATVHVRL 1150
    VDQNDNSPVL NNFQILFNNY VSNRSDTFPS GIIGRIPAYD PDVSDHLFYS 1200
    FERGNELQLL VVNQTSGELR LSRKLDNNRP LVASMLVTVT DGLHSVTAQC 1250
    VLRVVIITEE LLANSLTVRL ENMWQERFLS PLLGHFLEGV AAVLATPTED 1300
    VFIFNIQNDT DVGGTVLNVS FSALAPRGAG AGAAGPWFSS EELQEQLYVR 1350
    RAALAARSLL DVLPFDDNVC LREPCENYMK CVSVLRFDSS APFLASASTL 1400
    FRPIQPIAGL RCRCPPGFTG DFCETELDLC YSNPCRNGGA CARREGGYTC 1450
    VCRPRFTGED CELDTEAGRC VPGVCRNGGT CTNAPNGGFR CQCPAGGAFE 1500
    GPRCEVAARS FPPSSFVMFR GLRQRFHLTL SLSFATVQPS GLLFYNGRLN 1550
    EKHDFLALEL VAGQVRLTYS TGESSTVVSP TVPGGLSDGQ WHTVHLRYYN 1600
    KPRTDALGGA QGPSKDKVAV LSVDDCNVAV ALRFGAEIGN YSCAAAGVQT 1650
    SSKKSLDLTG PLLLGGVPNL PENFPVSRKD FIGCMRDLHI DGRRVDMAAF 1700
    VANNGTTAGC QAKSHFCASG PCKNGGLCSE RWGGFSCDCP VGFGGKDCRL 1750
    TMAHPYHFQG NGTLSWDFGN DMPVSVPWYL GLSFRTRATK GVLMQVQLGP 1800
    HSVLLCKLDQ GLLSVTLSRA SGHAVHLLLD QMTVSDGRWH DLRLELQEEP 1850
    GGRRGHHIFM VSLDFTLFQD TMAMGSELEG LKVKHLHVGG PPPSSKEEGP 1900
    QGLVGCIQGV WTGFTPFGSS ALPPPSHRIN VEPGCTVTNP CASGPCPPHA 1950
    NCKDLWQTFS CTCWPGYYGP GCVDACLLNP CQNQGSCRHL QGGPHGYTCD 2000
    CASGYFGQHC EHRMDQQCPR GWWGSPTCGP CNCDVHKGFD PNCNKTSGQC 2050
    HCKEFHYRPR GSDSCLPCDC YPVGSTSRSC APHSGQCPCR PGALGRQCNS 2100
    CDSPFAEVTA SGCRVLYDAC PKSLRSGVWW PQTKFGVLAT VPCPRGALGL 2150
    RGTGAAVRLC DEDHGWLEPD FFNCTSPAFR ELSLLLDGLE LNKTALDTVE 2200
    AKKLAQRLRE VTGQTDHYFS QDVRVTARLL AYLLAFESHQ QGFGLTATQD 2250
    AHFNENLLWA GSALLAPETG DLWAALGQRA PGGSPGSAGL VRHLEEYAAT 2300
    LARNMDLTYL NPVGLVTPNI MLSIDRMEQP SSSQGAHRYP RYHSNLFRGQ 2350
    DAWDPHTHVL LPSQSPQPSP SEVLPTSSNA ENATASGVVS PPAPLEPESE 2400
    PGISIVILLV YRALGGLLPA QFQAERRGAR LPQNPVMNSP VVSVAVFRGR 2450
    NFLRGALVSP INLEFRLLQT ANRSKAICVQ WDPPGPADQH GMWTARDCEL 2500
    VHRNGSHARC RCSRTGTFGV LMDASPRERL EGDLELLAVF THVVVAASVT 2550
    ALVLTAAVLL SLRSLKSNVR GIHANVAAAL GVAELLFLLG IHRTHNQLLC 2600
    TVVAILLHYF FLSTFAWLLV QGLHLYRMQV EPRNVDRGAM RFYHALGWGV 2650
    PAVLLGLAVG LDPEGYGNPD FCWISIHEPL IWSFAGPIVL VIVMNGIMFL 2700
    LAARTSCSTG QREAKKTSVL RTLRSSFLLL LLVSASWLFG LLAVNHSVLA 2750
    FHYLHAGLCG LQGLAVLLLF CVLNADARAA WTPACLGKKA APEETRPAPG 2800
    PGSGAYNNTA LFEESGLIRI TLGASTVSSV SSARSGRAQD QDSQRGRSYL 2850
    RDNVLVRHGS TAEHAEHSLQ AHAGPTDLDV AMFHRDAGAD SDSDSDLSLE 2900
    EERSLSIPSS ESEDNGRTRG RFQRPLRRAA QSERLLAHPK DVDGNDLLSY 2950
    WPALGECEAA PCALQAWGSE RRLGLDSNKD AANNNQPELA LTSGDETSLG 3000
    RAQRQRKGIL KNRLQYPLVP QTRGTPELSW CRAATLGHRA VPAASYGRIY 3050
    AGGGTGSLSQ PASRYSSREQ LDLLLRRQLS RERLEEVPVP APVLHPLSRP 3100
    GSQERLDTAP ARLEPRDRGS TLPRRQPPRD YPGTMAGRFG SRDALDLGAP 3150
    REWLSTLPPP RRNRDLDPQH PPLPLSPQRP LSRDPLLPSR PLDSLSRISN 3200
    SRERLDQVPS RHPSREALGP APQLLRARED PASGPSHGPS TEQLDILSSI 3250
    LASFNSSALS SVQSSSTPSG PHTTATPSAT ASALGPSTPR SATSHSISEL 3300
    SPDSEVPRSE GHS 3313
    Length:3,313
    Mass (Da):359,355
    Last modified:November 1, 1998 - v1
    Checksum:iB11DA09517288764
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 ENSGT00750000117340.
    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.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    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

    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 1, 2014
    This is version 128 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

    Dasty 3