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
//