ID H0YZU3_TAEGU Unreviewed; 2909 AA.
AC H0YZU3;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Cadherin EGF LAG seven-pass G-type receptor 1 {ECO:0000313|Ensembl:ENSTGUP00000003828.2};
GN Name=CELSR1 {ECO:0000313|Ensembl:ENSTGUP00000003828.2};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000003828.2, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000003828.2, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000003828.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Receptor that may have an important role in cell/cell
CC signaling during nervous system formation.
CC {ECO:0000256|ARBA:ARBA00002066}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC Adhesion G-protein coupled receptor (ADGR) subfamily.
CC {ECO:0000256|ARBA:ARBA00007343}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. LN-TM7
CC subfamily. {ECO:0000256|ARBA:ARBA00010933}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR STRING; 59729.ENSTGUP00000021134; -.
DR Ensembl; ENSTGUT00000003870.2; ENSTGUP00000003828.2; ENSTGUG00000003678.2.
DR GeneTree; ENSGT00940000159839; -.
DR HOGENOM; CLU_000158_1_0_1; -.
DR TreeFam; TF323983; -.
DR Proteomes; UP000007754; Chromosome 1A.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR CDD; cd11304; Cadherin_repeat; 8.
DR CDD; cd00054; EGF_CA; 5.
DR CDD; cd00055; EGF_Lam; 1.
DR CDD; cd00110; LamG; 2.
DR Gene3D; 1.25.40.610; -; 1.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 2.60.40.60; Cadherins; 9.
DR Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1.
DR Gene3D; 2.10.25.10; Laminin; 6.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR032471; GAIN_dom_N.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like_7TM.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR24026:SF36; CADHERIN EGF LAG SEVEN-PASS G-TYPE RECEPTOR 1; 1.
DR PANTHER; PTHR24026; FAT ATYPICAL CADHERIN-RELATED; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF00028; Cadherin; 8.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF16489; GAIN; 1.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF00053; Laminin_EGF; 1.
DR Pfam; PF02210; Laminin_G_2; 2.
DR PRINTS; PR00205; CADHERIN.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00112; CA; 9.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00179; EGF_CA; 4.
DR SMART; SM00180; EGF_Lam; 1.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00008; HormR; 1.
DR SMART; SM00282; LamG; 2.
DR SUPFAM; SSF49313; Cadherin-like; 9.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS00232; CADHERIN_1; 5.
DR PROSITE; PS50268; CADHERIN_2; 9.
DR PROSITE; PS00022; EGF_1; 5.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 6.
DR PROSITE; PS01248; EGF_LAM_1; 1.
DR PROSITE; PS50027; EGF_LAM_2; 1.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000007754};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transducer {ECO:0000256|ARBA:ARBA00023224};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..2909
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025336105"
FT TRANSMEM 2408..2433
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2454..2474
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2494..2515
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2535..2557
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2563..2586
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 136..244
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 245..352
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 353..458
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 459..574
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 575..676
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 677..779
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 780..885
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 886..987
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1010..1110
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1189..1247
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1249..1285
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1289..1327
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1328..1532
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1535..1571
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1575..1756
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1758..1794
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1795..1832
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1889..1936
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1921..1994
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 2413..2587
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 48..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2647..2878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2647..2677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2678..2695
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2709..2725
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2760..2804
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2805..2821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2847..2878
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1237..1246
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1275..1284
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1561..1570
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1784..1793
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1822..1831
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1889..1901
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1891..1908
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1910..1919
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 2909 AA; 321703 MW; 2EDFB73F48155C53 CRC64;
MPRLLSAAAC VSWAALLCAL ASAGGRDPRP PRAAPLLHLP AGAAGRPAAA AAAAAEPPAL
PPAGRLRAAG TAPRRAPPAE PRGPRGGGPG PRRARHRAAA EPRGAAAGCA PLPGKEGGGR
RGARRARSLN SPPQFQLPSY QVSIPENEPA GTAVIVLRAQ DPDEGEAGRL AYSMEALFDE
RSNDYFTIDA ETGSVVTARS LDRETKDTHV LKVTASDHGS PRRRSATTYL TVTVSDTNDH
EPVFEQPEYR ESIRENLEVG YEVLTIRATD GDAPANANML YRLLEPGAGD GVFEIDPRSG
VVRTRASVDR EEVSEYHLVV EANDQGKDPG PRSATAMVHI TVEDENDNYP QFSEKRYLVQ
VPEDAPVNSQ ILQVQATDRD RGSNAQVHYS IVSGNLKGQF YIHSFSGAID LINPLDYETI
REYTLRIKAQ DGGRPPLINS SGMVSVQVVD VNDNAPIFVS TPFQATVLEN VPLGYSVLHI
QAVDADSGEN ARLEYKLIEM APSTGGAPVA GDSGFPFQIN NSTGWITVAA ELDRETVENY
HFGVEARDHG VPVMTSSASV SITVLDVNDN NPTFTEKVYH LRLNEDAAVG SSVLTLTAVD
RDVNSVVTYQ ITSGNTRNRF AITSQSGGGL ITLALPLDYK QERQYVLTVT ASDGTRFDTV
QVFINVTDAN THRPVFQSSH YTVSVSEDKP IGTSIVTISA TDEDTGENAR ITYILDDNIP
QFRIDPDTGT ITTLMELDYE DQASYTLAIT AHDNGIPQKS DTTYVEILIL DANDNAPRFL
RDRYQGSVFE DVPLSTSVLQ LSATDRDSGL NGRLLYTFQG GDDGDGDFYI EPTSGVIRTL
RKLDRENVAV YSLRAFAVDR GSPPLKASVD IQVTVLDIND NPPVFEKDEF DIFVEENSPV
GSIVARISAA DPDEGTNAQI MYQIVEGNIP EVFQLDLLNG DLTALMDLDY ESRTEYVIVV
QATSAPLVSR ATVHIRLLDQ NDNPPVLQDF QILFNNYVTN KSNSFPSGVI GKIPAHDPDV
SDSLAYTFVQ GNELNLLLLD SVTGELKLSR DLDNNRPLEA LMKVSVSDGV HSVTAVCTLR
VTIITDDMLT NSITVRLENM SQERFLSPLL SLFVEGVATV LSTAKDGIFV FNIQNDTDVT
SNILNVTFSA LLPGGIRNKF FPSEDLQEQI YLNRTLLTMI STQRVLPFDD NICLREPCEN
YMKCVSVLKF DSSAPFISSN TVLFRPIHPI NGLRCRCPPG FTGDYCETEI DLCYSNPCGS
NGLCRSREGG YTCECYEDYT GESCEVNARS GRCAPGVCKN GGTCVNLLIG GFKCECPPGE
YERPYCEMTT RSFPPQSFIT FKGLRQRFHF TVSLMFATRE RNALLLYNGR FNEKHDFIAL
EIIEEQIQLT FSAGETTTTV APFIVGGVSD GQWHSVQVQY YNKPNIGRLG IPHGPSGEKV
AVVTVDDCDT AVAVRFGSLI GNYTCAAQGT QTGSKKSLDL TGPLLLGGVP NLPEDFPVHN
RQFIGCMRNL SIDSKPIDMA GFIANNGTLP GCAAQRNYCE TNWCQNGGTC INKWSTYICE
CPVRYGGKNC EQAMPSPQRF SGESIIIWSD LDITISVPWY IGLMFRTRKV NGMLMQANAG
AASKINIQIL NSYVQFEVYS GLSQVASLKM SQSRVSDGEW HHILVELKSA KDGKDLKYLA
VMSLDYGMYQ STVQIGNQLP GLKMKSIIVG GVSGDQVSVQ QGFYGCMQGV RMGETSTNIA
TLNMKQAIKI NVREGCEVDN PCDSNPCPQH SYCSDDWDSY SCVCDPGYFG RDCVDVCNLN
PCEHVSTCVH KPSSSHGYTC ECGQSYYGQY CESKIDLPCP RGWWGNPICG PCNCETSKGF
DSDCNKTNGE CHCKANYYRP QSSDTCYPCD CFPSGSHTRA CDMETGQCPC KPGVIGRQCN
RCDNPFAEVT VRGCEVIYNG CPKAFEAGIW WPQTKFGQPA AVPCPKGSVG NAVRHCNIEK
GWLPPELFNC TTNTFVDLKI MNEKLHHNET KLDGDKTIRI VRALQNATQY THNLYGNDVR
TAYQIMIRVL QYESQQQGFD LAATRDVEFN ENIIKVGSAL LDRSNKEHWE QIQRTEGGTA
HLLRHYEEYF NNVAQNMKKT YMRPFVIVAT NMIIAVDIFD KSNFTGARIP RFHEIKEDYP
KDLESSVVFP DTLFRPSERK AVPTMKPSNQ KTPSKLNGDV FSPESAFAKR KKRHPDIETH
HTVAMVIIYR SLGQLLPENY DPDRRSLRLP NRPIINTPVV STAIHSDGEF PPNLVEKPVI
VEYAMLETEE RTKPVCVFWN HSIMIGGTGA WSSRGCELFS RNHSHIACQC NHITSSAVLM
DISKREVGDV RLMIFGDFGF QGLWLRSLVI HFTLKNQNLS QYEQLYLNSE KIKGSIFKSN
SNFPALSLLQ FVCTVIAILL HYFYMSTFAW MFVEQLHIYR MLTEVRNINF GHMRFYYVVG
WGIPAIITGL AVGLDPQGYG NPDFCWLSVH DTLIWSFAGP IVMVVIINTV IFILAMKASC
RRRQRSFEKT GVISVLRTAF LLLLLISATW LLGLMAVNSD VMTFHYLFAI FSCLQGLFIF
FFHCVFNKEV RKHLKNTLTG KKPLPDDSTA TRATLLTRSL NCNNTYIEEP NMYRTTMGES
TVSLESTVRD EAAHKLSGSS SQVRAGQTEA DSSIFHRNPS KSNEHDSDSD SELSLDEHSS
SYASSHSSDS EEDGLETEKK WNTSTSKNNE HGPLHSTPKV DTLPNHVKPY WPTECVTASD
GEDPGRKQKL KVETKVNVEL HRENQVNHSN EAPQDKENEG QQKENRPLAH QNNQQPEQRK
GILKNKVTYP PPLVDKNMKN RLREKLSDYN QSTVSSRTTS LGTNEGVRSP SDSGVTVKNV
RREQSRDQLN GMAMTLHVGT GHADTSDSE
//
