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Database: UniProt
Entry: B3RZ84_TRIAD
LinkDB: B3RZ84_TRIAD
Original site: B3RZ84_TRIAD 
ID   B3RZ84_TRIAD            Unreviewed;       683 AA.
AC   B3RZ84;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=G-protein coupled receptors family 2 profile 2 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=TRIADDRAFT_57362 {ECO:0000313|EMBL:EDV23799.1};
OS   Trichoplax adhaerens (Trichoplax reptans).
OC   Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC   Trichoplax.
OX   NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV23799.1, ECO:0000313|Proteomes:UP000009022};
RN   [1] {ECO:0000313|EMBL:EDV23799.1, ECO:0000313|Proteomes:UP000009022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV23799.1,
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; DS985246; EDV23799.1; -; Genomic_DNA.
DR   RefSeq; XP_002113325.1; XM_002113289.1.
DR   AlphaFoldDB; B3RZ84; -.
DR   STRING; 10228.B3RZ84; -.
DR   EnsemblMetazoa; TriadT57362; TriadP57362; TriadG57362.
DR   GeneID; 6754538; -.
DR   KEGG; tad:TRIADDRAFT_57362; -.
DR   CTD; 6754538; -.
DR   eggNOG; KOG4193; Eukaryota.
DR   HOGENOM; CLU_402993_0_0_1; -.
DR   InParanoid; B3RZ84; -.
DR   OMA; RTWENIA; -.
DR   OrthoDB; 1114672at2759; -.
DR   PhylomeDB; B3RZ84; -.
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   CDD; cd15933; 7tmB2_GPR133-like_Adhesion_V; 1.
DR   CDD; cd00037; CLECT; 1.
DR   Gene3D; 2.60.220.50; -; 1.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
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; 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; IPR017983; GPCR_2_secretin-like_CS.
DR   InterPro; IPR000203; GPS.
DR   PANTHER; PTHR12011; ADHESION G-PROTEIN COUPLED RECEPTOR; 1.
DR   PANTHER; PTHR12011:SF437; GPS DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF01825; GPS; 1.
DR   PRINTS; PR00249; GPCRSECRETIN.
DR   SMART; SM00303; GPS; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR   PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 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   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        359..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        395..417
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        429..451
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        463..484
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        504..530
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        551..573
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        579..602
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          6..69
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          360..603
FT                   /note="G-protein coupled receptors family 2 profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50261"
FT   REGION          625..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   683 AA;  77446 MW;  DB4F22E2F7643AE9 CRC64;
     MQYHGLWIGL RSQHSFNNIS NYAYKWIDGS NTSLFHNWLT TPLVGSISTE LCVATLRPLG
     WKWFQYNCNT TFLDGFICEK FAIPVKISPE KHLQYVSNTI RNQIYANETS DKSIGQLEAA
     SQLLSRTWEN IAISRKNDTL KFIVLNESIE ITQVLFNKAE TLIRAGWKNA LDPILATMKN
     LEKLTVRVAG TPLRNPIVIQ TTRMELRMEK IDTPYSTYIG LQTTTNNWLQ LHYDTNLVNK
     SNVVVIIYKN YRLFSELPSE SSLDVNTNIV SCSLVSTINS SKIQPTEFQY LLSNYKERVA
     LSDIQCSYWN FNQSNWSTSG CNFVRQYYGR THCRCNHLTH FAALMIVTNT TVNQYHSKIL
     GTIGIAGVVT SAVFLLFTLI ILVSLRNLRS DRFFIHKNLC LALLLANVSA VITSQAYLHH
     TACKVSAIIQ HFLFTAAFTW MLVEGLHLYL LMVKVFTSGR SKTFLYVFVG WGIPVIIVAT
     SIAIRFNDYG SNRICWLSIK NGLIWAFVGP VIAIITINFV IFILVARIIC RSSSPVAIEQ
     KTADFATIKS TLRGAVILVP ILGLTWIFGV LTINEQTLFF DYIFVITNSL QGFFIFLFHC
     ALNSEVQNAL KNRIGQYDAV KQLNNSPQNN SNGKQGKNTG NNVESWNGHH SSTLNKFKSE
     FYQNNTGNHD DLVVVRKSFE SKS
//
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