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Database: UniProt
Entry: A0A340W9N3_LIPVE
LinkDB: A0A340W9N3_LIPVE
Original site: A0A340W9N3_LIPVE 
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}.
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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
//
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