ID A0A1S3LY79_SALSA Unreviewed; 1200 AA.
AC A0A1S3LY79;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Adhesion G protein-coupled receptor L2-like isoform X6 {ECO:0000313|RefSeq:XP_013995639.1};
GN Name=LOC106569141 {ECO:0000313|RefSeq:XP_013995639.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013995639.1};
RN [1] {ECO:0000313|RefSeq:XP_013995639.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013995639.1};
RG RefSeq;
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 RefSeq; XP_013995639.1; XM_014140164.1.
DR AlphaFoldDB; A0A1S3LY79; -.
DR GeneID; 106569141; -.
DR OrthoDB; 1114672at2759; -.
DR Proteomes; UP000087266; Chromosome ssa14.
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; cd22845; Gal_Rha_Lectin_LPHN2; 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:SF61; ADHESION G PROTEIN-COUPLED RECEPTOR L2; 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 SUPFAM; SSF111418; Hormone receptor domain; 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 ECO:0000313|RefSeq:XP_013995639.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1200
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010310155"
FT TRANSMEM 859..880
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 892..909
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 921..946
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 958..977
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 997..1020
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1041..1064
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1070..1093
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 42..131
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
FT DOMAIN 141..400
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000259|PROSITE:PS51132"
FT DOMAIN 478..535
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 853..1094
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 438..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1111..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1172..1200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1112..1130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 142..324
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ SEQUENCE 1200 AA; 134917 MW; 2764315AB0D1457B CRC64;
MAPAAWRCLV LHGLLLTLIH LHCSEGFSRA ALPFGLVRRE LSCEGYAIDL RCPGADVIMI
ETANYGRTDD KICDADPFQM ENINCYLPDA YKIISQRCNN RTQCVVLTGS DVFPDPCPGT
YKYLEVQYEC VPYKVEQKVF ICPGTLKEVG EPTFVFEVEQ QAGAWSKDPL QAGDKVFFMP
WTPYRTDTLI EYASLEDLKN GRQTTTYKLP HRVDGTGFVA YDGAIFFNKE RTRNIVKFDL
RTRIKSGEAI VANANYHDTS PYRWGGKTDI DLAVDERGLW VIYATEQNNG RIVVSQLNPY
TLRFEATWET AYDKRSASNA FMVCGVLHVV RSTYEENESE TAKSHIDYIY NTKLSQGEYT
DILFPNQYQY IAAVDYNPRD NQLYVWNNFY ILRYDLEFDA EKDPADVPTI EDVSLSSALP
ETTTIITTTM AIVRVPVNTT VPADPRDGRE REAGKPAEDP HGTADPTTPE IPPTPRRFCE
GAMRRGISWP QTHTGATVER PCPKGTRGIA SYLCTVAGGT WNPKGPDLSN CTSHWVAQVA
QKIRSGENAA NLANELAHHT QGPVFAGDVS SSVRLMEQLV DILDAQLQEL RPSEKDSAGR
SFNKLQKRER TCRAYMKAIV DTVDNLLRLE ALKSWEDMNS TEQTHAATML LDTLEEGAFV
LADNLIEPAV VKVPADNIML DVYVLSTDGQ VQDFRFPQTS KGGASIQLSA NTVKVNSKNG
VAKLVFVLYK HLGQFLSTEN ATLRGGGRNL SDLTVNSHIL AASITKESSR VFVSDPVIFT
LEHLDKEHYY NPNCSFWNYS ERSMIGYWST QGCKLLDTNK SHTTCSCSHL TNFAILMAHR
GNVAEGSVHE LLLTVITRMG IAVSLVCLAV SLFTFCFFRG LQSDRNTIHK NLCLNLFIAE
LVFLVGINMT EPKLVCSIIA VVLHFFFLAA FAWMCLEGVQ LYLMLVEVFE SEFSRRKYYY
ASGYLFPAVV VGISAAIDYR SYGTPRACWL RVDNHFIWSF IGPVTFIIML NLIFLVVTMY
KMVKHSTSMK PDSTRLGGIR SWVLGAFALL FLLGLTWSFG LFFLNESSVV MAYLFTIFNT
LQGMFIFIFH CLLQKKVRKE YSKCFRQSQC CGGLPSEGSH SSAKTATSRS TARYSSATQV
QYILESYQED VERHSEEAVR ILLHLRRHQQ HLHPQPPGAA LSDPQQGHQC HGHPPPQRKL
//
