ID A0A3Q3GEM8_9LABR Unreviewed; 742 AA.
AC A0A3Q3GEM8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Adhesion G protein-coupled receptor L4 {ECO:0000313|Ensembl:ENSLBEP00000031651.1};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000031651.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000031651.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- 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 AlphaFoldDB; A0A3Q3GEM8; -.
DR STRING; 56723.ENSLBEP00000031651; -.
DR Ensembl; ENSLBET00000033077.1; ENSLBEP00000031651.1; ENSLBEG00000023885.1.
DR GeneTree; ENSGT00940000158252; -.
DR InParanoid; A0A3Q3GEM8; -.
DR OrthoDB; 1114672at2759; -.
DR Proteomes; UP000261660; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:InterPro.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd15437; 7tmB2_ETL; 1.
DR CDD; cd00054; EGF_CA; 2.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
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; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR032471; GAIN_dom_N.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like_7TM.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR InterPro; IPR000203; GPS.
DR PANTHER; PTHR12011:SF59; ADHESION G PROTEIN-COUPLED RECEPTOR L4; 1.
DR PANTHER; PTHR12011; ADHESION G-PROTEIN COUPLED RECEPTOR; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF16489; GAIN; 1.
DR Pfam; PF01825; GPS; 1.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00303; GPS; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000261660};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
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..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..742
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018552567"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 517..536
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 548..576
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 585..603
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 623..646
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 667..691
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 697..719
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 66..107
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 116..153
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 479..720
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
SQ SEQUENCE 742 AA; 82957 MW; E449C350525E8459 CRC64;
MESLLKSPMK LVVLTAWLFS VMNPCSLSDI CDSCHQLATC KALNGSNNAC FCNQGYTGDG
TTFCNDDNEC QNVTDICGDR GICTNTAGSY YCTCVSGYTS TGLDQFQPND GTECIDVDEC
KSGQVCGPNS HCHNTNGSFY CTCQRDYIPT SGSNHFHPGR GASCKDHPQK FCHDNIRCIT
QTVNKTLEYM KNLTDPQSVL KEIAKQTSGE LTSVEVIAYI EALSQSASTL ADYTVKPSLV
NSTLTKLVKA VNNLVEKDEL VAWSRMKEER REHTITKLLH TVEESALTLA KKYKTPTELQ
IKAPEMELKL FTFDVRHTKA KLSASMAGDQ ITLTPKLRAE EDRNGSVSVV FVRYDSLNDI
LKPSSDPGVT DYLRYAGTGE ITVNSQVIAA AVKPADVYQL DHVTFTLRHN EPIDTKADVT
KCAFWEYEPD SLQGRWATHG CKTVHFNSNA TTCSCSHLTH FAVLMSSGRA NLVAHHTILT
RITQLGMIIS LICLSMCIFT FWFFSEIQST RTTIHKNLCC SLFMAEFIFL VGINMNTHKL
FCSVIAGLLH YFFLAAFAWM CIEGIHLYLI VVGVIYNKGF LHRNFYIFGY GSPAVVVAIS
ATLGSKYYGT DKVCWLSTEN HFIWSFIGPA CLIILVNLLA FIVIIYKVYR HTAVKKPEIS
HYENIRSCAR GALALLFVLG ATWTFGVLHI LNETTLTAYL FTITNAFQGM FIFIFLCVLS
RKIQEEYYRL FKNVPCCFEC LR
//