ID   B3SC58_TRIAD            Unreviewed;       936 AA.
AC   B3SC58;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=Latrophilin Cirl {ECO:0000256|ARBA:ARBA00015543};
GN   ORFNames=TRIADDRAFT_61848 {ECO:0000313|EMBL:EDV19661.1};
OS   Trichoplax adhaerens (Trichoplax reptans).
OC   Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC   Trichoplax.
OX   NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV19661.1, ECO:0000313|Proteomes:UP000009022};
RN   [1] {ECO:0000313|EMBL:EDV19661.1, ECO:0000313|Proteomes:UP000009022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV19661.1,
RC   ECO:0000313|Proteomes:UP000009022};
RX   PubMed=18719581; DOI=10.1038/nature07191;
RA   Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA   Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA   Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA   Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA   Rokhsar D.S.;
RT   "The Trichoplax genome and the nature of placozoans.";
RL   Nature 454:955-960(2008).
CC   -!- SUBUNIT: Forms a heterodimer, consisting of a large extracellular
CC       region non-covalently linked to a seven-transmembrane moiety.
CC       {ECO:0000256|ARBA:ARBA00011834}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; DS985268; EDV19661.1; -; Genomic_DNA.
DR   RefSeq; XP_002117818.1; XM_002117782.1.
DR   AlphaFoldDB; B3SC58; -.
DR   STRING; 10228.B3SC58; -.
DR   EnsemblMetazoa; TriadT61848; TriadP61848; TriadG61848.
DR   GeneID; 6759031; -.
DR   KEGG; tad:TRIADDRAFT_61848; -.
DR   CTD; 6759031; -.
DR   eggNOG; KOG4193; Eukaryota.
DR   HOGENOM; CLU_313159_0_0_1; -.
DR   InParanoid; B3SC58; -.
DR   OrthoDB; 1114672at2759; -.
DR   PhylomeDB; B3SC58; -.
DR   Proteomes; UP000009022; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   InterPro; IPR000203; GPS.
DR   PANTHER; PTHR12011; ADHESION G-PROTEIN COUPLED RECEPTOR; 1.
DR   PANTHER; PTHR12011:SF347; LATROPHILIN CIRL; 1.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF01825; GPS; 1.
DR   PRINTS; PR00249; GPCRSECRETIN.
DR   SMART; SM00303; GPS; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR   PROSITE; PS50221; GPS; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009022};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        704..727
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        739..759
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        779..806
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        827..850
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        856..879
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          633..880
FT                   /note="G-protein coupled receptors family 2 profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50261"
SQ   SEQUENCE   936 AA;  104810 MW;  E2B19FA7015A5A6A CRC64;
     MPKDSVILYE LLPSLLSEIS VVALIMVQDQ SRSCFHIASD EQLDIISQPQ VSSRKFIITS
     WLEHSQIDIK ESMLSMNDVI MNEVKIFTSP DISVSNQSLQ DLAAESIHLQ KDATISPELR
     TQEPMFSLKS SLDLTNQLDL SEVSLVSNID SVAIFSEADG VDVITISSEL TVQEPPMNFP
     KSSLNLADKP DLSVLEVSNI YSMTIFSEIN KVEENLRLCQ IDHEDLSSVT VDADARLILT
     EIIQLQNPTA DLQSELGDIQ SQSWPLLTDL SCDLDIDKRV YWSDILQMQP SSSSCIISIL
     ESSMDSAGDV CDQANNCPEY YTTLPSQQEP DCSTINPLKS PIKNSISNLS SRTLYDTTLD
     MTYRTPTPSS TTKYITQRKN TGHATSTFNG SQANQILASF NQNISKTTVN TAKVLGYSRT
     LHEIIDKIDM KSLSTAETTD LSEFVVKIVK KLVTAGINGS NQDKIASDYM QLLDHYFLRV
     AEKLSYGETF NFTDVETGDV TMVISVQQVE AYNSTNYEFV FNSKSALRKS DDVLINLSNI
     MFRKNETVKI IAGIYWFLQD TVARVNDQLT LSSDIISCKI EPYPVFQDNA IFQYHVSYPN
     KASKNSGNNW KCMYWDLQSR SWNNTGCTTN LNLNKVVCVC NHLTHFALLL QIKNVQAFFS
     LYRINSERFV IHKNLLVALM FSQICIITAS QATKFEVLCK VMAIISHFFC LASFSWMLVE
     AAHLYFLIIS VFNHRSKMIL YFIFGWGIPI IVVGVTVAVQ HENYGRDQIC WLSTKNGFTW
     AFIGPVVAII AINFVVMIAV VKIAVASSTK NIFANHGIKN KLRGIKTMVK AISILCPILG
     LTWLIGLIPI TQETIAVAYV FVILNSSQGI SIFIFHCLYN SEINSNVISS PKFSTSSNKI
     AKLKDDLNLS YKIIPLARAI TKPINEQEEG RLNCAY
//