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O35161

- CELR1_MOUSE

UniProt

O35161 - CELR1_MOUSE

Protein

Cadherin EGF LAG seven-pass G-type receptor 1

Gene

Celsr1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      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: UniProtKB
    2. G-protein coupled receptor activity Source: UniProtKB
    3. protein binding Source: IntAct
    4. protein dimerization activity Source: UniProtKB
    5. transmembrane signaling receptor activity Source: UniProtKB

    GO - Biological processi

    1. anterior/posterior pattern specification Source: MGI
    2. apical protein localization Source: MGI
    3. cell-cell signaling Source: UniProtKB
    4. central nervous system development Source: UniProtKB
    5. establishment of body hair planar orientation Source: MGI
    6. establishment of planar polarity Source: UniProtKB
    7. establishment of planar polarity of embryonic epithelium Source: MGI
    8. gastrulation with mouth forming second Source: UniProtKB
    9. G-protein coupled receptor signaling pathway Source: UniProtKB
    10. hair follicle development Source: MGI
    11. homophilic cell adhesion Source: InterPro
    12. inner ear morphogenesis Source: MGI
    13. lateral sprouting involved in lung morphogenesis Source: MGI
    14. locomotory behavior Source: MGI
    15. neural tube closure Source: UniProtKB
    16. neuron migration Source: MGI
    17. neuropeptide signaling pathway Source: InterPro
    18. orthogonal dichotomous subdivision of terminal units involved in lung branching morphogenesis Source: MGI
    19. planar cell polarity pathway involved in neural tube closure Source: MGI
    20. planar dichotomous subdivision of terminal units involved in lung branching morphogenesis Source: MGI
    21. protein localization involved in establishment of planar polarity Source: MGI
    22. regulation of actin cytoskeleton organization Source: MGI
    23. regulation of neurotransmitter secretion Source: UniProtKB
    24. Rho protein signal transduction Source: MGI
    25. signal transduction Source: UniProtKB
    26. wound healing Source: MGI

    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 1
    Gene namesi
    Name:Celsr1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:1100883. Celsr1.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of plasma membrane Source: UniProtKB
    2. membrane Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2929Sequence AnalysisAdd
    BLAST
    Chaini30 – 30343005Cadherin EGF LAG seven-pass G-type receptor 1PRO_0000012915Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi236 – 2361N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi561 – 5611N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi649 – 6491N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi793 – 7931N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1129 – 11291N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1154 – 11541N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1228 – 12281N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1264 – 12641N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1274 – 12741N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1302 – 13021N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1322 ↔ 1333By similarity
    Disulfide bondi1327 ↔ 1364By similarity
    Disulfide bondi1366 ↔ 1375By similarity
    Disulfide bondi1382 ↔ 1393By similarity
    Disulfide bondi1387 ↔ 1402By similarity
    Disulfide bondi1404 ↔ 1413By similarity
    Disulfide bondi1422 ↔ 1433By similarity
    Disulfide bondi1427 ↔ 1443By similarity
    Disulfide bondi1445 ↔ 1455By similarity
    Glycosylationi1591 – 15911N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1635 ↔ 1661By similarity
    Glycosylationi1638 – 16381N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1655 – 16551N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1668 ↔ 1679By similarity
    Disulfide bondi1673 ↔ 1688By similarity
    Modified residuei1681 – 16811(3R)-3-hydroxyasparagineSequence Analysis
    Disulfide bondi1690 ↔ 1699By similarity
    Disulfide bondi1855 ↔ 1885By similarity
    Disulfide bondi1891 ↔ 1902By similarity
    Disulfide bondi1896 ↔ 1911By similarity
    Modified residuei1904 – 19041(3R)-3-hydroxyaspartateSequence Analysis
    Disulfide bondi1913 ↔ 1922By similarity
    Disulfide bondi1926 ↔ 1937By similarity
    Disulfide bondi1931 ↔ 1949By similarity
    Disulfide bondi1951 ↔ 1960By similarity
    Disulfide bondi1968 ↔ 1981By similarity
    Disulfide bondi1983 ↔ 1993By similarity
    Glycosylationi1994 – 19941N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2000 ↔ 2015By similarity
    Disulfide bondi2002 ↔ 2018By similarity
    Disulfide bondi2020 ↔ 2030By similarity
    Disulfide bondi2039 ↔ 2048By similarity
    Disulfide bondi2051 ↔ 2063By similarity
    Glycosylationi2118 – 21181N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2137 – 21371N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2144 – 21441N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2155 – 21551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2160 – 21601N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2272 – 22721N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2430 – 24301N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2452 – 24521N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2538 – 25381N-linked (GlcNAc...)Sequence Analysis
    Modified residuei2779 – 27791PhosphoserineBy similarity

    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

    PaxDbiO35161.
    PRIDEiO35161.

    PTM databases

    PhosphoSiteiO35161.

    Expressioni

    Tissue specificityi

    Expressed in the brain, where it is localized principally in the ependymal cell layer, choroid plexus and the area postrema. Also found in spinal chord and in the eye.1 Publication

    Developmental stagei

    First detected at E6. 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 in the vicinity of the primitive streak, and becomes predominant in that area at late gastrulation. At E10, detected in ventricular zones (VZ), but not in marginal zones (MZ), and weakly in other structures. Between E12 and E15, a high expression is present in the VZ in all brain areas. No expression in differentiated neuronal fields. In the newborn and postnatal stages, expression remains restricted to the VZ. Also found weakly in fetal lungs, kidney and epithelia.1 Publication

    Gene expression databases

    BgeeiO35161.
    GenevestigatoriO35161.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    atp6ap2Q7T0S32EBI-8294650,EBI-8294706From a different organism.

    Protein-protein interaction databases

    IntActiO35161. 1 interaction.
    MINTiMINT-5312768.
    STRINGi10090.ENSMUSP00000016172.

    Structurei

    3D structure databases

    ProteinModelPortaliO35161.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini30 – 24842455ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini2506 – 251611CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini2538 – 25425ExtracellularSequence Analysis
    Topological domaini2564 – 258724CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini2609 – 262517ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini2647 – 267024CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini2692 – 26943ExtracellularSequence Analysis
    Topological domaini2716 – 3034319CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei2485 – 250521Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei2517 – 253721Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei2543 – 256321Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei2588 – 260821Helical; Name=4Sequence AnalysisAdd
    BLAST
    Transmembranei2626 – 264621Helical; Name=5Sequence AnalysisAdd
    BLAST
    Transmembranei2671 – 269121Helical; Name=6Sequence AnalysisAdd
    BLAST
    Transmembranei2695 – 271521Helical; Name=7Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini261 – 368108Cadherin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini369 – 474106Cadherin 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini475 – 580106Cadherin 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini581 – 702122Cadherin 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini703 – 804102Cadherin 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini805 – 907103Cadherin 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini908 – 1014107Cadherin 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini1015 – 1116102Cadherin 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini1121 – 1239119Cadherin 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini1318 – 137659EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1378 – 141437EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1418 – 145639EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1457 – 1661205Laminin G-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1664 – 170037EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1704 – 1885182Laminin G-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1887 – 192236EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1923 – 196139EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1962 – 199433EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1996 – 203136EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini2018 – 206548Laminin EGF-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini2423 – 247553GPSPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi2674 – 26785Poly-Leu

    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.
    InParanoidiO35161.
    KOiK04600.
    OMAiEYERPYC.
    OrthoDBiEOG7BP81K.
    TreeFamiTF323983.

    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.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR002049. EGF_laminin.
    IPR017981. GPCR_2-like.
    IPR001879. GPCR_2_extracellular_dom.
    IPR000832. GPCR_2_secretin-like.
    IPR000203. GPS.
    IPR009030. Growth_fac_rcpt_N_dom.
    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.
    SSF57184. SSF57184. 2 hits.
    PROSITEiPS00010. ASX_HYDROXYL. 2 hits.
    PS00232. CADHERIN_1. 7 hits.
    PS50268. CADHERIN_2. 9 hits.
    PS00022. EGF_1. 6 hits.
    PS01186. EGF_2. 2 hits.
    PS50026. EGF_3. 6 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]

    Sequencei

    Sequence statusi: Complete.

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

    O35161-1 [UniParc]FASTAAdd to Basket

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    MAPSSPRVLP ALVLLAAAAL PALELGAAAW ELRVPGGARA FALGPGWSYR     50
    LDTTRTPREL LDVSREGPAA GRRLGLGAGT LGCARLAGRL LPLQVRLVAR 100
    GAPTAPSLVL RARAYGARCG VRLLRRSARG AELRSPAVRS VPGLGDALCF 150
    PAAGGGAASL TSVLEAITNF PACSCPPVAG TGCRRGPICL RPGGSAELRL 200
    VCALGRAAGA VWVELVIEAT SGTPSESPSV SPSLLNLSQP RAGVVRRSRR 250
    GTGSSTSPQF PLPSYQVSVP ENEPAGTAVI ELRAHDPDEG DAGRLSYQME 300
    ALFDERSNGY FLIDAATGAV TTARSLDRET KDTHVLKVSA VDHGSPRRSA 350
    ATYLTVTVSD TNDHSPVFEQ SEYRERIREN LEVGYEVLTI RATDGDAPSN 400
    ANMRYRLLEG AGGVFEIDAR SGVVRTRAVV DREEAAEYQL LVEANDQGRN 450
    PGPLSASATV HIVVEDENDN YPQFSEKRYV VQVPEDVAVN TAVLRVQATD 500
    RDQGQNAAIH YSIVSGNLKG QFYLHSLSGS LDVINPLDFE AIREYTLRIK 550
    AQDGGRPPLI NSSGLVSVQV LDVNDNAPIF VSSPFQAAVL ENVPLGHSVL 600
    HIQAVDADAG ENARLQYRLV DTASTIVGGS SVDSENPASA PDFPFQIHNS 650
    SGWITVCAEL DREEVEHYSF GVEAVDHGSP AMSSSASVSI TVLDVNDNDP 700
    MFTQPVYELR LNEDAAVGSS VLTLRARDRD ANSVITYQLT GGNTRNRFAL 750
    SSQSGGGLIT LALPLDYKQE RQYVLAVTAS DGTRSHTAQV FINVTDANTH 800
    RPVFQSSHYT VSVSEDRPVG TSIATISATD EDTGENARIT YVLEDPVPQF 850
    RIDPDTGTIY TMTELDYEDQ AAYTLAITAQ DNGIPQKSDT TSLEILILDA 900
    NDNAPRFLRD FYQGSVFEDA PPSTSVLQVS ATDRDSGPNG RLLYTFQGGD 950
    DGDGDFYIEP TSGVIRTQRR LDRENVAVYN LWALAVDRGS PNPLSASVGI 1000
    QVSVLDINDN PPVFEKDELE LFVEENSPVG SVVARIRAND PDEGPNAQIM 1050
    YQIVEGNVPE VFQLDLLSGD LRALVELDFE VRRDYMLVVQ ATSAPLVSRA 1100
    TVHIRLLDQN DNPPELPDFQ ILFNNYVTNK SNSFPSGVIG RIPAHDPDLS 1150
    DSLNYTFLQG NELSLLLLDP ATGELQLSRD LDNNRPLEAL MEVSVSDGIH 1200
    SVTALCTLRV TIITDDMLTN SITVRLENMS QEKFLSPLLS LFVEGVATVL 1250
    STTKDDIFVF NIQNDTDVSS NILNVTFSAL LPGGTRGRFF PSEDLQEQIY 1300
    LNRTLLTTIS AQRVLPFDDN ICLREPCENY MKCVSVLRFD SSAPFISSTT 1350
    VLFRPIHPIT GLRCRCPPGF TGDYCETEID LCYSNPCGAN GRCRSREGGY 1400
    TCECFEDFTG EHCQVNVRSG RCASGVCKNG GTCVNLLIGG FHCVCPPGEY 1450
    EHPYCEVSTR SFPPQSFVTF RGLRQRFHFT VSLAFATQDR NALLLYNGRF 1500
    NEKHDFIALE IVEEQLQLTF SAGETTTTVT PQVPGGVSDG RWHSVLVQYY 1550
    NKPNIGHLGL PHGPSGEKVA VVTVDDCDAA VAVHFGSYVG NYSCAAQGTQ 1600
    SGSKKSLDLT GPLLLGGVPN LPEDFPVHSR QFVGCMRNLS IDGRIVDMAA 1650
    FIANNGTRAG CASQRNFCDG TSCQNGGTCV NRWNTYLCEC PLRFGGKNCE 1700
    QAMPHPQRFT GESVVLWSDL DITISVPWYL GLMFRTRKED GVLMEATAGT 1750
    SSRLHLQILN SYIRFEVSYG PSDVASMQLS KSRITDGGWH HLLIELRSAK 1800
    EGKDIKYLAV MTLDYGMDQS TVQIGNQLPG LKMRTIVIGG VTEDKVSVRH 1850
    GFRGCMQGVR MGETSTNIAT LNMNDALKVR VKDGCDVEDP CASSPCPPHS 1900
    HCRDTWDSYS CICDRGYFGK KCVDACLLNP CKHVAACVRS PNTPRGYSCE 1950
    CGPGHYGQYC ENKVDLPCPK GWWGNPVCGP CHCAVSQGFD PDCNKTNGQC 2000
    QCKENYYKPP AQDACLPCDC FPHGSHSRAC DMDTGQCACK PGVIGRQCNR 2050
    CDNPFAEVTS LGCEVIYNGC PRAFEAGIWW PQTKFGQPAA VPCPKGSVGN 2100
    AVRHCSGEKG WLPPELFNCT SGSFVDLKAL NEKLNRNETR MDGNRSLRLA 2150
    KALRNATQGN STLFGNDVRT AYQLLARILQ HESRQQGFDL AATREANFHE 2200
    DVVHTGSALL APATEASWEQ IQRSEAGAAQ LLRHFEAYFS NVARNVKRTY 2250
    LRPFVIVTAN MILAVDIFDK LNFTGAQVPR FEDIQEELPR ELESSVSFPA 2300
    DTFKPPEKKE GPVVRLTNRR TTPLTAQPEP RAERETSSSR RRRHPDEPGQ 2350
    FAVALVVIYR TLGQLLPEHY DPDHRSLRLP NRPVINTPVV SAMVYSEGTP 2400
    LPSSLQRPIL VEFSLLETEE RSKPVCVFWN HSLDTGGTGG WSAKGCELLS 2450
    RNRTHVTCQC SHSASCAVLM DISRREHGEV LPLKIITYAA LSLSLVALLV 2500
    AFVLLSLVRT LRSNLHSIHK NLITALFFSQ LIFMVGINQT ENPFLCTVVA 2550
    ILLHYVSMGT FAWTLVENLH VYRMLTEVRN IDTGPMRFYH VVGWGIPAIV 2600
    TGLAVGLDPQ GYGNPDFCWL SLQDTLIWSF AGPVGTVIII NTVIFVLSAK 2650
    VSCQRKHHYY ERKGVVSMLR TAFLLLLLVT ATWLLGLLAV NSDTLSFHYL 2700
    FAAFSCLQGI FVLLFHCVAH REVRKHLRAV LAGKKLQLDD SATTRATLLT 2750
    RSLNCNNTYS EGPDMLRTAL GESTASLDST TRDEGVQKLS VSSGPARGNH 2800
    GEPDASFIPR NSKKAHGPDS DSDSELSLDE HSSSYASSHT SDSEDDGGEA 2850
    EDKWNPAGGP AHSTPKADAL ANHVPAGWPD ESLAGSDSEE LDTEPHLKVE 2900
    TKVSVELHRQ AQGNHCGDRP SDPESGVLAK PVAVLSSQPQ EQRKGILKNK 2950
    VTYPPPLPEQ PLKSRLREKL ADCEQSPTSS RTSSLGSGDG VHATDCVITI 3000
    KTPRREPGRE HLNGVAMNVR TGSAQANGSD SEKP 3034
    Length:3,034
    Mass (Da):330,471
    Last modified:July 27, 2011 - v3
    Checksum:iFD9C4812AA1F0BCD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti218 – 2181E → Q in AAC68836. (PubMed:9858697)Curated
    Sequence conflicti1050 – 10501M → I in AAC68836. (PubMed:9858697)Curated
    Sequence conflicti1900 – 19012SH → RP in AAC68836. (PubMed:9858697)Curated
    Sequence conflicti2524 – 25241T → A in AAC68836. (PubMed:9858697)Curated
    Sequence conflicti2805 – 28051A → T in AAC68836. (PubMed:9858697)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF031572 mRNA. Translation: AAC68836.1.
    AC116764 Genomic DNA. No translation available.
    AC139513 Genomic DNA. No translation available.
    CCDSiCCDS37172.1.
    PIRiT14119.
    RefSeqiNP_034016.2. NM_009886.2.
    UniGeneiMm.22680.

    Genome annotation databases

    EnsembliENSMUST00000016172; ENSMUSP00000016172; ENSMUSG00000016028.
    GeneIDi12614.
    KEGGimmu:12614.
    UCSCiuc007xdt.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF031572 mRNA. Translation: AAC68836.1 .
    AC116764 Genomic DNA. No translation available.
    AC139513 Genomic DNA. No translation available.
    CCDSi CCDS37172.1.
    PIRi T14119.
    RefSeqi NP_034016.2. NM_009886.2.
    UniGenei Mm.22680.

    3D structure databases

    ProteinModelPortali O35161.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O35161. 1 interaction.
    MINTi MINT-5312768.
    STRINGi 10090.ENSMUSP00000016172.

    Protein family/group databases

    GPCRDBi Search...

    PTM databases

    PhosphoSitei O35161.

    Proteomic databases

    PaxDbi O35161.
    PRIDEi O35161.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000016172 ; ENSMUSP00000016172 ; ENSMUSG00000016028 .
    GeneIDi 12614.
    KEGGi mmu:12614.
    UCSCi uc007xdt.1. mouse.

    Organism-specific databases

    CTDi 9620.
    MGIi MGI:1100883. Celsr1.

    Phylogenomic databases

    eggNOGi NOG12793.
    GeneTreei ENSGT00750000117340.
    HOGENOMi HOG000231346.
    HOVERGENi HBG050887.
    InParanoidi O35161.
    KOi K04600.
    OMAi EYERPYC.
    OrthoDBi EOG7BP81K.
    TreeFami TF323983.

    Miscellaneous databases

    NextBioi 281774.
    PROi O35161.
    SOURCEi Search...

    Gene expression databases

    Bgeei O35161.
    Genevestigatori O35161.

    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.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR002049. EGF_laminin.
    IPR017981. GPCR_2-like.
    IPR001879. GPCR_2_extracellular_dom.
    IPR000832. GPCR_2_secretin-like.
    IPR000203. GPS.
    IPR009030. Growth_fac_rcpt_N_dom.
    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.
    SSF57184. SSF57184. 2 hits.
    PROSITEi PS00010. ASX_HYDROXYL. 2 hits.
    PS00232. CADHERIN_1. 7 hits.
    PS50268. CADHERIN_2. 9 hits.
    PS00022. EGF_1. 6 hits.
    PS01186. EGF_2. 2 hits.
    PS50026. EGF_3. 6 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 ]
    ProtoNeti Search...

    Publicationsi

    1. "mCelsr1 is an evolutionarily conserved seven-pass transmembrane receptor and is expressed during mouse embryonic development."
      Hadjantonakis A.-K., Formstone C.J., Little P.F.R.
      Mech. Dev. 78:91-95(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "Celsr1, a neural-specific gene encoding an unusual seven-pass transmembrane receptor, maps to mouse chromosome 15 and human chromosome 22qter."
      Hadjantonakis A.-K., Sheward W.J., Harmar A.J., de Galan L., Hoovers J.M.N., Little P.F.R.
      Genomics 45:97-104(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
      Strain: C57BL/6.
      Tissue: Brain.
    4. "Developmental expression profiles of Celsr (Flamingo) genes in the mouse."
      Tissir F., De-Backer O., Goffinet A.M., Lambert de Rouvroit C.A.
      Mech. Dev. 112:157-160(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.

    Entry informationi

    Entry nameiCELR1_MOUSE
    AccessioniPrimary (citable) accession number: O35161
    Secondary accession number(s): E9QK27
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 2, 2002
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 147 of the entry and version 3 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3