ID A0A3Q3GDA9_9LABR Unreviewed; 1525 AA.
AC A0A3Q3GDA9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Adhesion G protein-coupled receptor L1-like {ECO:0000313|Ensembl:ENSLBEP00000031057.1};
GN Name=ADGRL1 {ECO:0000313|Ensembl:ENSLBEP00000031057.1};
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:ENSLBEP00000031057.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000031057.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR Ensembl; ENSLBET00000032474.1; ENSLBEP00000031057.1; ENSLBEG00000023389.1.
DR GeneTree; ENSGT00940000159684; -.
DR Proteomes; UP000261660; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
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; cd16007; 7tmB2_Latrophilin-1; 1.
DR CDD; cd22844; Gal_Rha_Lectin_LPHN1; 1.
DR Gene3D; 1.25.40.610; -; 1.
DR Gene3D; 2.60.120.740; -; 1.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
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; IPR003924; GPCR_2_latrophilin.
DR InterPro; IPR003334; GPCR_2_latrophilin_rcpt_C.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR031234; Latrophilin-1_TM.
DR InterPro; IPR000922; Lectin_gal-bd_dom.
DR InterPro; IPR043159; Lectin_gal-bd_sf.
DR InterPro; IPR003112; Olfac-like_dom.
DR PANTHER; PTHR12011:SF62; ADHESION G PROTEIN-COUPLED RECEPTOR L1; 1.
DR PANTHER; PTHR12011; ADHESION G-PROTEIN COUPLED RECEPTOR; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF16489; GAIN; 1.
DR Pfam; PF02140; Gal_Lectin; 1.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF02793; HRM; 1.
DR Pfam; PF02354; Latrophilin; 1.
DR Pfam; PF02191; OLF; 1.
DR PRINTS; PR00249; GPCRSECRETIN.
DR PRINTS; PR01444; LATROPHILIN.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00008; HormR; 1.
DR SMART; SM00284; OLF; 1.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 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; PS51132; OLF; 1.
DR PROSITE; PS50228; SUEL_LECTIN; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00446};
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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:UP000261660};
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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1525
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018541021"
FT TRANSMEM 843..870
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 882..899
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 911..938
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 950..969
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 989..1012
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1033..1056
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1062..1085
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 40..129
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
FT DOMAIN 134..393
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000259|PROSITE:PS51132"
FT DOMAIN 468..524
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 845..1086
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 404..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1205..1224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1313..1362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1410..1525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1205..1220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1410..1452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 135..317
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ SEQUENCE 1525 AA; 169412 MW; A54ABB689AF24212 CRC64;
MARAVWIIFT CAVAFSNISP SSQALSRSMM PFGLMRRELA CEGYPIELRC PGSDVIMIET
ANYGRTDDKI CDADPFQMEN VQCYLPDAFK IMSQRCNNRT QCVVVAGSDV FPDPCPGTYK
YLEIQYECVP YIFVCPGTLL RVQAASSLQE AEHQAGAWCK DPLQSGDRLY VMPWTPYRTD
MLFEYASWED FKQNRATTTY KLPNRVDGTG FVVYDGAVFY NKERTRNIVK YDLRTRIKSG
EAIITNANYH DTSPYRWGGK SDIDLAVDEN GLWVIYATES NNGRLVVSQV NPYTLRFEGT
WETSFDKRMA SNAFMACGVL YAVRSVYQDD DSEAGGDLVM YAYNTNHARE EPVNIPFPNP
YQYISSVDYN PRDNQLYVWN NYNVLRYALE FGPPDPTTGP LTTTPVTTTL PARPFTSSAS
PTTARPLAPT SRPIGSINKH PDLRPITATV PVTRRPPRPP QGPEPHVCEA KQVRGVQWPT
TQRGETVDRP CPKGSLGIAS FQCLEEQVMW NPRGPDLSNC TSPWVNQVAQ KIKSGENAAN
IAGELVNHTR GRVQAGDVSS SVRLIEQLLD ILDAQLQALR PGNKESAARN YNKLQKRERT
CRAYIQAVVQ TVDNLLRPEA LESWQDMNST EQAHTATMLL DVLEKGAFLL ANNMYGNHFS
DRAPSIELEV HVLNTEMDLQ DLSFPQNYAG DSTIQLSAST IKQYSRNGQV KVVFILYKNL
GSFLSTENAT VKMEVEGPSH DKKRLAVNSH VIAASINKES SRVFLTEPVV FTLKRLQMDN
YYTPNCSFWN YSERSMTGQW SSQGCRLLDT NSTHTTCSCS HLTNFAVLMA HHEPDYQGRM
HELILFVITW VGIVISLVCL AICISTFCFL RGLQTDRNTI HKNLCINLFI AELLFLIGID
KTEYHIACPI FAGLLHFFFL AAFSWMCLEG VQLYLMLVEV FESEYSRKKY YYLCGYCFPA
LVVGISAAID YRSYGTKKAC WLRVDNYFIW SFIGPVSFVI MLNLIFLMIT LHKMIRNSSA
LKPDSSRLDN IKSWALGAIA LLFLLGLTWA FGLLFINENT VIMAYLFTTF NAFQGMFIFI
FHCALQKKVH KEYSKCLRHS YCCSRTSTTS SHGSLKNSGL RANNRYYSGS QARHAAAHRQ
SRIRRMWNDT VRKQTESSFM AGDINSTPTL NRATMGNHLL TNPVLQTRTG TSPYNTLLAE
SFTPPSPGVF NSTGTFRDPK STLSKAREPC GMETLPLNGN FNNSYSLRSG PGGGGGGSCD
FLGGGGGDSP PALFNARGSE TMGGGGIRRN LSDAAAFEKM IISELVHNNL RGGVGGSGGG
GGDVGDRMCG SLARGRPHGG VGQGTTGVGP EPSISMDEDE DYLREGRQRT PQDVELLYKA
LEEPLLLQRA QSVLYQSDPE ESESYTADLT ESLGHSGHSG QSNSVQGGNR APDSPARDSL
YTSITNLRDS PYPDSSPEPL EVVPRSAQPP EELYYSSGRP ALGSRGAPMQ TFYQAQARRP
SGEGHAAQEP AHSEGDGQMQ LVTSL
//
