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Database: UniProt
Entry: A0A369RRM9_9METZ
LinkDB: A0A369RRM9_9METZ
Original site: A0A369RRM9_9METZ 
ID   A0A369RRM9_9METZ        Unreviewed;      1576 AA.
AC   A0A369RRM9;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Latrophilin Cirl {ECO:0000256|ARBA:ARBA00015543};
GN   ORFNames=TrispH2_011054 {ECO:0000313|EMBL:RDD36892.1};
OS   Trichoplax sp. H2.
OC   Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC   Trichoplax.
OX   NCBI_TaxID=287889 {ECO:0000313|EMBL:RDD36892.1, ECO:0000313|Proteomes:UP000253843};
RN   [1] {ECO:0000313|EMBL:RDD36892.1, ECO:0000313|Proteomes:UP000253843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Panama {ECO:0000313|EMBL:RDD36892.1,
RC   ECO:0000313|Proteomes:UP000253843};
RC   TISSUE=Whole clonal animals {ECO:0000313|EMBL:RDD36892.1};
RX   PubMed=30042472; DOI=10.1038/s41598-018-29400-y;
RA   Kamm K., Osigus H.J., Stadler P.F., DeSalle R., Schierwater B.;
RT   "Trichoplax genomes reveal profound admixture and suggest stable wild
RT   populations without bisexual reproduction.";
RL   Sci. Rep. 8:11168-11168(2018).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RDD36892.1}.
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DR   EMBL; NOWV01000299; RDD36892.1; -; Genomic_DNA.
DR   STRING; 287889.A0A369RRM9; -.
DR   Proteomes; UP000253843; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:InterPro.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR   CDD; cd15040; 7tmB2_Adhesion; 1.
DR   CDD; cd00037; CLECT; 3.
DR   Gene3D; 2.60.220.50; -; 1.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 5.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR018378; C-type_lectin_CS.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR046338; GAIN_dom_sf.
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   Pfam; PF00059; Lectin_C; 3.
DR   PRINTS; PR00249; GPCRSECRETIN.
DR   SMART; SM00034; CLECT; 5.
DR   SUPFAM; SSF56436; C-type lectin-like; 5.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 5.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR   PROSITE; PS50221; GPS; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000313|EMBL:RDD36892.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253843};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1294..1317
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1329..1349
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1361..1378
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1398..1417
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1437..1459
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1480..1503
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1509..1528
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          65..187
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          223..347
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          359..463
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          511..609
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          611..736
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          1295..1533
FT                   /note="G-protein coupled receptors family 2 profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50261"
SQ   SEQUENCE   1576 AA;  174118 MW;  400B036648DBD211 CRC64;
     MVRAKLSVFQ CVVFVIVADF IPVLSNYSSI FACGIPCAIL PSTSLAENDY GHTKVSVADD
     LWYSHNSKRY FFSQTTLTFQ AAVNYCRDTY GGSLLEISGH NENTVIRNML ISENAPSAIF
     WIGIQDSSGI FANAVWHHSN ASVGDWNLWY QDIVVDPSKL CTGGFEIFGT FVWKNLRCSD
     PYRFICQIDL NTTTSNFILA SYLFASYPRP PHENVCKAPN IVFNNTCLSP HNTLLPFNLS
     INYCKAIGKR LLQVESQAKS QVLNSIISST MEVWIGLRSH LSKSVSKKDF TWLYDDPNLL
     ASNFTAWEKF TPITINNPIS GKCATIKRDS LLWKNRPCQS FYPFICQQEM TCPAGWLQFR
     DSCYQVMNPY GVGTYWLGAF LSCKFSYSSG LAIIASKDEM KFIESVALSL NRPLWIAMKA
     DGKGLRWNSK ENITNHYQIP PNAYCMLVKP TGNRVTWEFS SCSTGIGAYP LCQKAATPIT
     LNNSEGLTTA AIVDSIGKDI FPTCPDNWLL YRNYCYYLET TTGNYLQGKN RCKNNLEAYP
     AIINDAEKEM IIRSILGIDD EVWIGLEGTS NNFTWYENLA SINYTNLVAH ACYPENSCEL
     QTNCPTDWNI NGVNCIQITF QKLRFYNARE FCSYHKSDLI SLSSIDLEQV TQNLIEQKAV
     NQLVNITGVS FWIGLYKVNN TFQWLQDSTA VQENSKLEFR STAGTSQLRC AVMEYMHLNG
     TWVWYTVDCV SHRAYLICRK TIDLESDTST FPMVQSTTQV PVTTEDSETG AISFAIDAVI
     ANTEDSSTTD ISTNTIVTTP NISTTTTENS TTSNIFTTTS AVTAAVENST TLNVSATTNA
     ATATTENSIT TKISITTSAA TAAVEDSTTL SIPAATNTAT ATTENSTTTK ISTTTSAATS
     AVEDSTTLSI PAATNTATAT TENSTTTKIS TTTSAATAAL GDSTTPNIST TTNTATVTTE
     NSTTKKISTT TNTTTATIED STTPTISTTN NAATLTTKDS KTVNISITTD AKTATIEDSP
     IVNVSTTKNG VIATIEDSTI ANISVTTNVA TTTTEDSTTS SFSTATNNAV TTNTVPITKR
     NPRTIKALTN IGTTTTTMLS TVSTLSTRVA TNRNQTYDNI DEVVDNAGLE LAGKLSLFAN
     SNNSQVSYYY QKLEEVSAVQ ESDTGHPLKV KVPTSIIDNK YEGQFQIAIG IYKSTQFQQR
     NRIQQPLKYA VSCQIRPIMK GTLKEPVVFF YEIKEGSNKQ PSCAYWKKNH WATDGLKLEK
     INATTIKCLS YHLTSFSVLL RFNNYSSPKI HDKILSITTY IGLSISLLCL IVTFLTFTAI
     RQFHSIRGLI HANMAASMII STTVFLLGIQ WTNSPAICKS IAAILHFSLL ATFLWMLIEG
     IATFKMSTHN LESRNSSISY LLLGWGIPMV IVLISFLSGS TYYGTTTYCW IQPGKHLLYA
     FGIPTSIIVC INVILMIRIA RSLVGIRAIA TKSNIQKVRA LLRASAALLP LLGITWVVGF
     LAYNHQTLIL DYFFVILNSF QGVFIFYFHC YNYKGVKRYY ARRFIHSAYS PRNQISKASN
     TDLMTRSKRR KSAWEG
//
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