ID A0A3P8YQX3_ESOLU Unreviewed; 1554 AA.
AC A0A3P8YQX3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Adhesion G protein-coupled receptor L3 {ECO:0000313|Ensembl:ENSELUP00000018302.1};
GN Name=ADGRL3 {ECO:0000313|Ensembl:ENSELUP00000018302.1};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000018302.1, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000018302.1, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000018302.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 RefSeq; XP_019899118.1; XM_020043559.1.
DR Ensembl; ENSELUT00000028140.2; ENSELUP00000018302.1; ENSELUG00000017939.2.
DR GeneID; 105020624; -.
DR GeneTree; ENSGT00940000155527; -.
DR OrthoDB; 1114672at2759; -.
DR Proteomes; UP000265140; LG24.
DR Bgee; ENSELUG00000017939; Expressed in brain and 10 other cell types or tissues.
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; cd16005; 7tmB2_Latrophilin-3; 1.
DR CDD; cd22846; Gal_Rha_Lectin_LPHN3; 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; IPR000922; Lectin_gal-bd_dom.
DR InterPro; IPR043159; Lectin_gal-bd_sf.
DR InterPro; IPR003112; Olfac-like_dom.
DR PANTHER; PTHR12011:SF60; ADHESION G PROTEIN-COUPLED RECEPTOR L3; 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 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:UP000265140};
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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1554
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018110166"
FT TRANSMEM 865..888
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 900..918
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 924..946
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 967..987
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1007..1030
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1051..1074
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1080..1103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..124
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 484..541
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 863..1104
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 417..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1122..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1362..1418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1430..1505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1523..1554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1402..1418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 135..317
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ SEQUENCE 1554 AA; 172682 MW; 917BCF133FFD67B8 CRC64;
MWTARLLLLA SLFAPAALAF SRAPVPMAVV RRELSCESYP IELRCPGTDV IMIESANYGR
TDDKICDADP AQMENTRCYL PDAYKIMSQR CNNRTQCAVV AGPDVFPDPC PGTYKYLEVQ
YECVPYKVEQ KVFLCPGLLR GVYQSEHLFE SDHQSGAWCK DPLQASDKIY YMPWTPYRTD
TLTEYSSKED FIAGRPTTTY KLPHRVDGTG FVVYDGALFF NKERTRNIVK FDLRTRIKSG
EAIIANANYH DTSPYRWGGK SDIDLAVDEN GLWVIYATEQ NNGRIVISQL NPYTLRVEGT
WDTAYDKRSA SNAFMICGIL YVVKSVYEDD DNEATGNKID YIYNTELSKD GFLDIPFPNS
YQYIAAVDYN PRDNLLYVWN NYHVVKYSLD FGALDNRQES SSSVMVFMDT TTTRSTTQPT
VISSTTTSAT STTTTTTSTT TPVNQRPRLI STTLPPLPPV EGNAPEVNTR SSPSSKLPNI
GIEYCNPMIM SDVSWPKTRQ GLVARQPCPT GTIGVAMYLC LGPEGFWDPQ GPNLSNCTSP
WVSVITQKLK TGETAAIIAR ELSEQTKSSL QAGDITYTVK AMGQLVDLLD VQLRNLTPGG
KDSAARSLNK LQKRERSCRF YVQAMVETVN NLLQPQAQSA WRDLSTGEQL KAATMLLDTV
EQGAFVLADN LLKTDIVQEN TDNIQLEVAR MSTEGNLPDL KFPQSSGHGN SITLSANTLK
QHGRNGEIRM AFVLYRNIGA YLSTENASMK LGSEAMATNY SVIVNSPVIT AAINKENTKV
YLSDPVIFTL KHLQHSKESF NPNCSFWSYS KRTMTGFWST QDCRLLGTNR SHTTCSCTHL
TNFAILMAHV EVKNTDPVHD MLLDVITWVG ILLSLVCLLI SLFTFCFFRG LQSDRNTIHK
NLCISLFIAE SLFLVGINRA DQPIACAVFA ALLHFFFLAA FTWMFLEGVQ LYIMLVEVFE
SEHSRKRYFY LVGYGVPALI VAVSAAVDYR SYGTDRVCWL RLDTYFIWSF IGPATLIIML
NVIFLGIALY KMFHHTAILK PDSGCLDNIK SWVIGAIALL CLLGLTWAFG LMYVNESTII
MAYLFTIFNS LQGMFIFIFH CVLQKKVRKE YGKCLRTHCC SGKSVESSMG SVKSSASRPP
GRYSTGSQSR IRRMWNDTVR KQSESSFITG DINSSASLNR GVMANHLITN ALLRPHGTNN
PYNTLLGESA VYNNPSVGMY NTQEGILNNA RDSSVMDTLP LNGNHGNSYS IASAEYMSDC
VQIIDRGYNH KETTLEKKIL KELTSNYIPS YLNNHERSAE QSRNLMNKLV NNVSNGGKDV
GLGGVGIGVN VPLGLDDHSS FPPHLHDEGL GLELIREESN APLLPQRPPQ LPPVDGLHHN
HLHQPPPPPH QHQYHHHHPA FSSATAASSS SRRRIPQENS ESFFPLLTNE HTQDGGLASP
GQPPRHPPHP RDSLYTSMPV LAGLPDSTAD AAGPPADQEA GAGQQSGGRS PEPGQDDVYY
KSMPNLGSHN HLNQLHAYYQ LGRGSSDGFI VPPNKEDLSP EEAPQEPSHL VTSL
//
