ID A0A1S3T3I0_SALSA Unreviewed; 1499 AA.
AC A0A1S3T3I0;
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 isoform X19 {ECO:0000313|RefSeq:XP_014071145.1};
GN Name=adgrl2 {ECO:0000313|RefSeq:XP_014071145.1};
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_014071145.1};
RN [1] {ECO:0000313|RefSeq:XP_014071145.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014071145.1};
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_014071145.1; XM_014215670.1.
DR OrthoDB; 1114672at2759; -.
DR Proteomes; UP000087266; Chromosome ssa10.
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 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_014071145.1};
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..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..1499
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010306572"
FT TRANSMEM 871..892
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 904..922
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 934..958
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 970..989
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1009..1032
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1053..1076
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1082..1105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 50..139
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
FT DOMAIN 149..408
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000259|PROSITE:PS51132"
FT DOMAIN 468..544
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 865..1106
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 413..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1301..1320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1392..1442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1392..1418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 150..332
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ SEQUENCE 1499 AA; 167831 MW; CEB3F53E45BD41B7 CRC64;
MQRPSTQGTM ACSLWKLPTF CWLIAMALIQ SSEGFSRAAL PFGLVRRELS CEGYPIDLRC
PGSDVIMIES ANYGRTDDKI CDADPFQMEN INCYLPDAYK IMSQRCNNRT QCIVITGSDV
FPDPCPGTYK YLEVQYECVP YKVEQKVFVC PGTLKAVGDP SFLFEAEQQA GSWCKDPLQA
GDKIYFMPWT PYRTDTLIEY SSLDDFQNAR QTITYKLPHR VDGTGFVVYD GAVFFNKERT
RNIVKFDIRT RIKSGEAIIN NANYHDTSPY KWGGKTDIDL AVDENGLWVI YATEQNNGMM
VISQLNPYTL RFEATWETTY DKRSASNAFM ICGVLYVVRS TYEDNESEVS KSLIDYVYNT
KQNRGEYVDI HFPNQYQYIA AVDYNPRDNQ LYVWNNFYIL RYNLEFGPPD PAHAPPLSEA
TSAPAEPLRT TTTTTTTTAA RNKGVANTMT TTGPKEGNNR GGPKPPLEVP QTTAQPPLES
FPLPERFCET TEKRDIVWPQ TQRGMLVERP CPKGTRGTAS YLCVLATGAW HPKGPDLSNC
TSHWVNQVAQ KIRSGENAAN LANELAKHTK GPIFAGDVSS SVRLMEQLVD ILDAQLQELR
PSEKDSAGRS FNKLQKRERT CRAYMKAIVD TVDNLLRPEA LKSWHDMNST EQTHAATMLL
DTLEEGAFVL ADNLMEPAIV KVPADNIILD VYVLSTDGQV QDFKFPQASK GGVSIQLSSN
TVKLNSRNGV AKLVFVMYKN LGQFLSTDNA TIKMSNDAYG RNVSVAVNSD IIAASINKES
SRVFITDPVI FTLEHIDMDH YFNSNCSFWN YSERSMMGYW STQGCKLLGS NKTHTTCSCS
HLTNFAVLMA HQEISGQVGV HELLLTVITR VGIVVSLVCL AISVFTFCFF RGLQSDRNTI
HKNLCINLFI AELIFLIGID MTEPKIGCSI VAGILHFFFL ASFSWMCLEG VQLYLMMVEV
FESEHSRRKY YYVSGYLLPA IVVGVSAAID YRSYGTKKAC WLRVDNHFIW SFLGPVTFII
MLNLIFLVIT MYKMGKHSTT LKPDSSRLEN IKSWVLGAFA LLCLMGLTWS FGLFFINESS
VVMAYLFTIF NTFQGMFIFI FHCLLQKKVR KEYIKCFRHT YCCGGLPTES SHSSTKTSTT
RTSARYSSGT QSRIRRMWND TVRKQSESSF ISGDINSTST LNQGMTGNYL LTNPLLRPQG
TNNPYNTLLA ETVVCNAPTA PVFNSPGHSH TLNHPRDTSA MDTLPLNGNF NNSYSLRNGD
YGDSVQVVDC GLSLDDAAFE KMLISELVHN NLRACNKSHN HHVERGAPLP PSSKKVNVVG
GSSSEDDVIV ADTSSLVHGH NINTPVGLGI ELHHRELEAP LIPQRTHSLL YQPQKRVKTT
EGGLESYVSQ LTTNEHGDSL QSPNRDSLYT SMPTLRDSPY PESSPDAEEL EDLSSPSKRS
ENEDVYYKSM PNLGAGHQLQ AYYQISRGNS DGYIIPITKE GCIPEGDVRE GQMQLVTSL
//
