ID A0A340W9N3_LIPVE Unreviewed; 1305 AA.
AC A0A340W9N3;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Latrophilin-3-like isoform X9 {ECO:0000313|RefSeq:XP_007446143.1};
GN Name=LPHN3 {ECO:0000313|RefSeq:XP_007446143.1};
OS Lipotes vexillifer (Yangtze river dolphin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Lipotidae; Lipotes.
OX NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007446143.1};
RN [1] {ECO:0000313|RefSeq:XP_007446143.1}
RP IDENTIFICATION.
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_007446143.1; XM_007446081.1.
DR GeneID; 103087945; -.
DR CTD; 103087945; -.
DR OrthoDB; 1114672at2759; -.
DR Proteomes; UP000265300; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
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 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:UP000265300};
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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1305
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016346503"
FT TRANSMEM 953..976
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 988..1006
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1012..1034
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1055..1075
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1095..1118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1139..1162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1168..1191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 109..198
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
FT DOMAIN 208..467
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000259|PROSITE:PS51132"
FT DOMAIN 572..628
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 951..1192
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 59..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1210..1234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 209..391
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ SEQUENCE 1305 AA; 145771 MW; C65BF1626D2AE8FB CRC64;
MPENITMWPS QLLVFLMLLA PIVHGGKHSE RHPALAAPLR HAERNPGGAL PPRHLLQQPA
AERATAHRGQ GPRGAARGVR GPGAQGAQIS AQAFSRAPIP MAVVRRELSC ESYPIELRCP
GTDVIMIESA NYGRTDDKIC DSDPAQMENI RCYLPDAYKI MSQRCNNRTQ CAVVAGPDVF
PDPCPGTYKY LEVQYECVPY KVEQKVFLCP GLLKGVYQSE HLFESDHQSG AWCKDPLQAS
DKIYYMPWTP YRTDTLTEYS SKDDFIAGRP TTTYKLPHRV DGTGFVVYDG ALFFNKERTR
NIVKFDLRTR IKSGEAIIAN ANYHDTSPYR WGGKSDIDLA VDENGLWVIY ATEQNNGKIV
ISQLNPYTLR IEGTWDTAYD KRSASNAFMI CGILYVVKSV YEDDDNEATG NKIDYIYNTD
QSKDSLVDVP FPNSYQYIAA VDYNPRDNLL YVWNNYHVVK YSLDFGPLDS RSGQAHHGQV
PYISPPIHLD SELERPPVRD ISTAGPLGTG STTTSTTLRT TTWNPGRSTT PSVSGRRNRN
TSTPSPAAEV LDDITTHLLS GSSQIPALEE SCEAVEAREI MWFKTRQGQM AKQPCPAGTI
GVSTYLCLAP DGIWDPQGPD LSNCSSPWVS HITQKLKSGE TAANIARELA EQTRNHLNAG
DITYSVRAMD QLVGLLDVQL RNLTPGGKDS AARSLNKLQK RERSCRAYVQ AMVETVNNLL
QPQALNAWRD LTTSDQLRAA TMLLDTVEES AFVLADNLLK TDIVRENTDN IQLEVARLST
EGNLEDLKFP ENMGHGSTIQ LSANTLKQNG RNGEIRVAFV LYNNLGPYLS TENASMKLGT
EAMSTNHSVI VNSPVITAAI NKEFSNKVYL ADPVVFTVKH IKQSEENFNP NCSFWSYSKR
TMTGYWSTQG CRLLTTNKTH TTCSCNHLTN FAVLMAHVEV KHSDAVHDLL LDVITWVGIL
LSLVCLLICI FTFCFFRGLQ SDRNTIHKNL CISLFVAELL FLIGINRTDQ PIACAVFAAL
LHFFFLAAFT WMFLEGVQLY IMLVEVFESE HSRRKYFYLV GYGMPALIVA VSAAVDYRSY
GTDKVCWLRL DTYFIWSFIG PATLIIMLNV IFLGIALYKM FHHTAILKPE SGCLDNIKSW
VIGAIALLCL LGLTWAFGLM YINESTVIMA YLFTIFNSLQ GMFIFIFHCV LQKKVRKEYG
KCLRTHCCSG KSTESSIGSG KTSGSRTPGR YSTGSQSRIR RMWNDTVRKQ SESSFITGDI
NSSASLNREP YRETSMGVKL NIAYQIGASE QCQGYKCHGY STTEW
//