GenomeNet

Database: UniProt
Entry: A0A340X4X7_LIPVE
LinkDB: A0A340X4X7_LIPVE
Original site: A0A340X4X7_LIPVE 
ID   A0A340X4X7_LIPVE        Unreviewed;      3319 AA.
AC   A0A340X4X7;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Cadherin EGF LAG seven-pass G-type receptor 1 {ECO:0000313|RefSeq:XP_007454150.1};
GN   Name=CELSR1 {ECO:0000313|RefSeq:XP_007454150.1};
OS   Lipotes vexillifer (Yangtze river dolphin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Lipotidae; Lipotes.
OX   NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007454150.1};
RN   [1] {ECO:0000313|RefSeq:XP_007454150.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (SEP-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}.
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DR   RefSeq; XP_007454150.1; XM_007454088.1.
DR   STRING; 118797.A0A340X4X7; -.
DR   GeneID; 103085146; -.
DR   KEGG; lve:103085146; -.
DR   CTD; 9620; -.
DR   InParanoid; A0A340X4X7; -.
DR   OrthoDB; 4006628at2759; -.
DR   Proteomes; UP000265300; Unplaced.
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:InterPro.
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; 9.
DR   CDD; cd00054; EGF_CA; 4.
DR   CDD; cd00055; EGF_Lam; 1.
DR   CDD; cd00110; LamG; 2.
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; 1.
DR   Pfam; PF16489; GAIN; 1.
DR   Pfam; PF01825; GPS; 1.
DR   Pfam; PF02793; HRM; 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; 8.
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; 1.
DR   PROSITE; PS00232; CADHERIN_1; 6.
DR   PROSITE; PS50268; CADHERIN_2; 8.
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   ECO:0000313|RefSeq:XP_007454150.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265300};
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..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..3319
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016302377"
FT   TRANSMEM        2488..2511
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2523..2541
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2547..2569
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2590..2610
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2630..2650
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2671..2693
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2699..2722
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          264..371
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          372..477
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          478..583
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          584..705
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          706..807
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          808..910
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          911..1017
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          1018..1119
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          1321..1379
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1381..1417
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1421..1459
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1460..1664
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          1667..1703
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1707..1888
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          1890..1926
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1927..1964
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          2021..2068
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          2053..2126
FT                   /note="G-protein coupled receptors family 2 profile 1"
FT                   /evidence="ECO:0000259|PROSITE:PS50227"
FT   DOMAIN          2486..2723
FT                   /note="G-protein coupled receptors family 2 profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50261"
FT   REGION          227..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2307..2348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2780..3071
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3109..3135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3237..3319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2810..2828
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2830..2846
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2896..2921
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2963..2977
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3025..3039
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        1369..1378
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1407..1416
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1693..1702
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1916..1925
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1954..1963
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        2021..2033
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        2023..2040
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        2042..2051
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ   SEQUENCE   3319 AA;  361480 MW;  ADC1A29E71F4D833 CRC64;
     MAPPPPPVLP ALLLLAAVAA LPVLGLRAAA WELRVPGGAR AFALGPGWTY ALDAALTPRA
     LRELLDVSRD GRLAGRRRGP GAGLRGCARL GGRPLPLHVR LAARSAQTAL SLRLRARAHG
     PGCSARPRRG RAPGAELRAR AVLTVPGPGA VFCFPGPGGG GGGGATLHSA LEALTTFPAC
     SCPPRAGSRC PRRPVCLPPG GSARLRLLCA LRRAAGTIRV ELALEAASGT PSPSLSPPSL
     PQVGAGAARR ARRGAGGSTT PQFQLPSYQV SVPENEPAGT AVIELRAHDP DEGEAGRLSY
     QMEALFDERS NGYFLIDSDT GLVSTARALD RETKDTHVLK VSAVDHGSPR RSAATYLTVT
     VSDTNDHSPV FEQSEYRERV RENLEVGYEV LTIRATDGDA PSNANMRYRL LEGAGGVFEI
     DERSGVVRTR AVVDREEEAS YQLLVEANDQ GRNPGPLSAT ATVHIVVEDE NDNYPQFSEK
     RYVVQVPEDV AVNTPVLRVQ ATDRDQGQNA AIHYSIISGN LKGQFYLHSL SGSLDVINPL
     DFEAIREYTL RIKAQDGGRP PLINSSGLVS VQVLDVNDNA PIFVSSPFQA AVLENVPLGH
     SVLHIQAVDA DAGENARLRY RLVDTASASV GSGGAGPQGP ASAADFPFHI HNSSGWITVC
     AELDREELEH YSFGVEAVDH GSPPMSSSAS VAITVLDVND NDPMFTQPVY ELRLNEDAAV
     GSSVLTLRAL DRDANSVITY QLTGGNTRNR FALSSQSGGG LITLALPLDY KQERQYVLAV
     TASDGMRAHT AQVFINVTDA NTHRPVFQSS HYTVSVSEDR PVGTSIATIS ATDEDTGENA
     RITYVLEDPV PQFRIDPDTG TIYTVTELDY ESQAAYTLGI TARDNGVPQK SDTTSLEILV
     LDANDNAPRF LRDFYQGSVF EDAPPSTSVL QVSATDRDSG PNGRLLYTFQ GGDDGDGDFY
     IEPTSGVIRT QRRLDRENVA VYNLRALAVD RGSPVPLSAS VEIQVTVLDI NDNPPVFERD
     ELELFVEENS PVGSVVARIR ARDPDEGPNA QVMYQIVEGN VPEVFQLDLL SGDLRALVEL
     DFEARREYVL VVQATSAPLV SRATVRIRLV DQNDNPPVLP DFQILFNNYV TNKSNSFPTG
     VIGRIPAHDP DLLDSLNYTF LQGNELQLLL LDPASGELQL SPDLNNNRPL EALMEVSVSD
     GIHSVAALCT LRVTVITDDM LTNSITVRLE NMSQEKFLSP LLSRFVEGVA TVLSTTKDAI
     FVFNIQNDTD VSSNILNVTF SALLPGGVRD KFFPSEDLQE QIYLNRTLLT AVSTQRVLPF
     DDNICLREPC ENYMKCVSVL KFDSSAPFIS SPTVLFRPIH PVNGLRCRCP PGFTGDYCET
     EIDLCYSSPC GAHGRCRSRE GGYTCECQED FTGEHCEVNA RSGRCTNGVC KNGGTCVNLL
     IGGFHCVCPP GAFERPYCEV ATRSFPPQSF VTFRGLRQRF HFTVALAFAT QERNALLLYN
     GRFNEKHDFI ALEIVDEQVQ LTFSAGETTT MVAPQVPGGV SDGRWHSVQV QYYNKPNIGR
     LGLPHGPSGE KVAMVTVDDC DTAVAVRFGS FVGNYSCAAQ GTQSGSKKSL DLTGPLLLGG
     VPNLPEDFPV QNRQFVGCMR NLSIDGRNVD MASFIANNGT RAGCAAQRNF CDGTWCQNGG
     TCVSGWNTYL CECPLRFGGK NCEQVMPHPQ RFSGESIVSW SDLDITISVP WYLGLMFRTR
     KEDGVLMEAT AGVSSRLHLQ ILNNYVQFEV SHGPSDVVSM RLSRSRVTDG EWHHLLIELK
     NAKEGKDIKY LAVMTLDYGV DQDTVQIGNQ LPGLRMRSLI VGGVSEDKVS VRRGFRGCMQ
     GVRMGETATN IATLNMKDAL KVRVKDGCDM EDPCSSSPCP QHSQCHNTWD GYSCICDRGY
     FGRKCVDVCH VNPCKHVAAC VHSPDSPRGY VCECGSGHYG QYCENRIDLP CPRGWWGNPV
     CGPCHCAVSK GFDPDCNKTN GQCQCKENYY RPPVQDTCLP CDCFPHGSHS RACDMDTGQC
     SCKPGVIGRQ CNRCDNPFAE VTVLGCEVIY NGCPRAFEAG IWWPQTKFGQ PAAVPCPKGS
     VGNAVRHCSG EKGWLPPELF NCTTVSFVDL KAMNEKLSRN ETRMDGDRSL WLARALRNAT
     RHTDGLFGND VRTAYQLLGR VLLHESSQQG FELAATRDAD FHEDIVQAGS ALLAPGTKAA
     WEQIQRSEGG TAQLLRRFEA YFSNMARNLR RTYLRPFVII TPNMILAVDV FDKLNFTGAW
     VPQFKHLRGE VPKDLESSVF FSEDLFKPPE RKEGPTVRPA GRRAAPQTAR PQPSAEMDAP
     FKRRKRHPEE PGQFAIALVI IYRTLGQLLP ERYDPDRRSL RLPNRPVINT PVVSAVVYSE
     GAPLPSPLER PVLVEYTLLE TEERTKPVCV FWNHSITIGG TGGWSAKGCE LLSRNRTHVT
     CQCSHATSSA VLMDVSRREH GEVLPLKIVT YAAVSLSLAA LLAAFVLLAL VQTLRSNLHG
     IHRNLIGALF FSQLVFVIGI AQTENPFLCT VIAILLHYMY MSTFAWTFVE SLHIYRMLTE
     VRNIDAGPMR FYYVVGWGIP AIVTGLAVGL DPQGYGNPDF CWLSLRDTLI WSFAGPIGTV
     IVVNTVIFVL SAKASCQRKR HYYERKRVVS LVRTAFVLLL LISATWLLGL LAVNSDALTF
     RYLFAVFGCL QGLAVLLLHC VFNREVRKHL KGVLAGKKPY PDDSATTRAT LLTRSLNCNN
     TYGEEPDVFR TALGESTASL DSTIRDKGGQ KLSVSSGLAR GGHGEPDASF VPRSTKKPHG
     HDSDSDSELS LDEQSSSYAS SRSSDSEDDG VAAEDRWDPA QGPVHSTPKV DSVANHVPAG
     WPDESLAGSD SEGPGEQPRL KVETKVSVEL HLDEQGNHCS ERIPARESGG SRPAAAPPSQ
     PPEQRKGILK NKVTYPPPLT ERMLRSRLRE KLAEREQSPA SSRPSSLASS DGVRAPDGAV
     PAKTLHWEPG REHLNGVAMN VRAGSAQAHG SSSEPRAQRR AQAKAQGLRW ASTRERAPAR
     DQEAGGSAPS PVPLLTLTCQ ECLVMNVIEY HHLKPEVLLK GDTCEESSPP LKGAATPESL
     RHCPEASQSQ SAVPPERRWY CSPEAAMGAA KHDVESTCRA VVSLPAASGQ HLPGPAPLEQ
     PPSPPPPAHR AYFFIWITEM VLEATWREWA SVPPQDWAPL SRGWGERWAQ LSVTLTQGHT
     QPAVGPSPPR APAPGRQGHG VRLEAGPPGR RQPLRRPGAS PKRGVRSRTP VLLPRPRVAE
     PGCAGGRPLS ARERSIPTR
//
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