ID A0A1S3SD72_SALSA Unreviewed; 1543 AA.
AC A0A1S3SD72;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Latrophilin-3-like {ECO:0000313|RefSeq:XP_014062290.1};
GN Name=LOC106608716 {ECO:0000313|RefSeq:XP_014062290.1};
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_014062290.1};
RN [1] {ECO:0000313|RefSeq:XP_014062290.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014062290.1};
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}.
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 RefSeq; XP_014062290.1; XM_014206815.1.
DR PaxDb; 8030-ENSSSAP00000113508; -.
DR KEGG; sasa:106608716; -.
DR OrthoDB; 1114672at2759; -.
DR Proteomes; UP000087266; Chromosome ssa07.
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: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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1543
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010182774"
FT TRANSMEM 867..890
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 902..920
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 926..948
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 969..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 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 486..543
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 418..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1351..1404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1420..1439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1466..1543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1387..1404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1496..1510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 135..317
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ SEQUENCE 1543 AA; 171751 MW; 7542FF65802F3ED6 CRC64;
MLTARLLLFA SLFAPAALAF SRAPIPMAVV 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 SNSFMICGIL YVVKSVYEDD DNEATGNKID YIYNTELSKD GFLDIPFPNS
YQYIAAVDYN PRDNLLYVWN NYHVVKYSLD FGALDGRPES SSSVIVFMDT TTTRTTTRPA
TVSMTTTPTT SSTTTTRASA TTSVAQRPRT TSTTLPPPLP PAEGNVPEGN TRSSPSSKLP
NVGIEYCNPM IMSDVSWPKT RQGLVTRQPC PTGTIGVAMY LCMGPEGYWD PQGPDLSNCT
SPWVNVITQK LKAGETAAVI ARELSEQTKS NLQAGDITYT VKAMGQLVDL LDVQLRNLTP
GGKDSAARSL NKLQKRERSC RFYVQAMVET VNNLLQPQAQ SAWRDLSTGE QLRAATMLLD
TVEQGAFVLA DNLLKTDIVQ ENTDNIQLEV ARMSTEGNLP DLKFPQSGGH GNSISLSSST
LKQHGRNGEI RMAFVLYKHI GAYLSTENAS MKLGREAMAT NYSVIVNSPV ITAAINKENN
KVYLSEPVIF TLKHLQQSKE SFNPNCSFWS YSKRTMTGYW STQDCRLLGT NRTHTTCSCT
HLTNFAVLMA HVEVKNTDPV HDLLLDVITW VGILLSLVCL LISLFTFCFF RGLQSDRNTI
HKNLCISLFI AESLFLVGIN RADQPIACAV FAALLHFFFL AAFTWMFLEG VQLYIMLVEV
FESEHSRKRY FYLVGYGVPA LIVAVSAAVD YRSYGTDRVC WLRLDTYFIW SFIGPATLII
MLNVIFLGIA LYKMFHHTAI LKPDSGCLDN IKSWVIGAIA LLCLLGLTWA FGLMYINEST
VIMAYLFTIF NSLQGMFIFI FHCVLQKKVR KEYGKCLRTH CCSGKSVESS IGSGKSSSRI
RRMWNDTVRK QSESSFITGD INSSASLNRG AMANHLITNA LLRPHGTNNP YNTLLGDSAV
YNNPSVGMYN TQEGILNNAR DTSVMDTLPL NGNHGYSIAS ADYMSDCVQI IDRGYNHKET
TLEKKILKEL TSNYIPSYLN NHDRSAEQNR NLMNKLVNNM SNGGKDVGLG GMGMGGMNVA
LDLDEHSSFP PHLHDEGLGL ELIREESNAP LLPQRPPLLP PVDNLHHNHL HNQGPPHQPP
LPHHHPAFSS ATTTSSASRR RIPQENSESF FPLLTNEHTL DVEPTSPSHH PHHLHHPRDS
LYTSMPVLAG LPDTTDTGTT TTTTTILADK DAGEGHPAGG KSPEASQDDV YYKSMPNLGS
RNQLHSYYQL GRGSSDGFIV PPNKEDLSPE ESPQEPSHLV TSL
//