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Database: UniProt
Entry: T1KSM5_TETUR
LinkDB: T1KSM5_TETUR
Original site: T1KSM5_TETUR 
ID   T1KSM5_TETUR            Unreviewed;       637 AA.
AC   T1KSM5;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:tetur20g00140.1};
OS   Tetranychus urticae (Two-spotted spider mite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC   Tetranychoidea; Tetranychidae; Tetranychus.
OX   NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur20g00140.1, ECO:0000313|Proteomes:UP000015104};
RN   [1] {ECO:0000313|Proteomes:UP000015104}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA   Rombauts S.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:tetur20g00140.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family.
CC       {ECO:0000256|ARBA:ARBA00008077}.
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DR   EMBL; CAEY01000505; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; T1KSM5; -.
DR   STRING; 32264.T1KSM5; -.
DR   EnsemblMetazoa; tetur20g00140.1; tetur20g00140.1; tetur20g00140.
DR   eggNOG; KOG3577; Eukaryota.
DR   HOGENOM; CLU_007873_2_1_1; -.
DR   OMA; NCAIPCY; -.
DR   Proteomes; UP000015104; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR   CDD; cd07456; CRD_FZ5_like; 1.
DR   Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR015526; Frizzled/SFRP.
DR   InterPro; IPR000539; Frizzled/Smoothened_7TM.
DR   InterPro; IPR020067; Frizzled_dom.
DR   InterPro; IPR036790; Frizzled_dom_sf.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
DR   PANTHER; PTHR11309; FRIZZLED; 1.
DR   PANTHER; PTHR11309:SF126; FRIZZLED-2; 1.
DR   Pfam; PF01534; Frizzled; 1.
DR   Pfam; PF01392; Fz; 1.
DR   PRINTS; PR00489; FRIZZLED.
DR   SMART; SM00063; FRI; 1.
DR   SMART; SM01330; Frizzled; 1.
DR   SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR   PROSITE; PS50038; FZ; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00090}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015104};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        279..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        312..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        345..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        373..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        443..471
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        491..516
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        545..563
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          49..170
FT                   /note="FZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50038"
FT   DOMAIN          277..570
FT                   /note="G-protein coupled receptors family 2 profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50261"
FT   REGION          171..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        54..115
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        62..108
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        99..137
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        126..167
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        130..154
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ   SEQUENCE   637 AA;  72085 MW;  14CEAA2697F4917D CRC64;
     MNNLISEISV YQCELAVNHS ASIDIKMHFF TLFIYILFVP SILTSTESDG RSKCEEITVP
     MCRGIGYNMT SMPNQFHHEK QDEAGMEAHQ FWPLVEISCS DDLRFFLCSM YTPICMEDYT
     ERLPVCRSVC ERAQAGCAAI MLQYGFPWPE SMDCNNFPVF GSQEQLCMDH KNGETPGPGT
     VSTQASIPSK PPPPHYPSTT FYSLSTAPTS TIYPTFNSST KNVDITGSRC HCECKPPMIS
     INVQSDYYNH INERGVIDCA QPCHTNLFFT KQEQSKSSLM ITIAAFSCLL GSIMVIFTYL
     TGRERFCYPE RSIIFLSACY LIVSIGFLYP KLTNSETIAC DSDKLLYAGF GTPTWNCTFV
     FILIYFFSMA ASLWWIILTF SWFLSASLKW TVEIINDYSI YFHFIAWSIP AVKSYLAITM
     KAIDGEPLAG ICLVGNLNSQ LLVRFIIAPL CAYLIVGVFF LLAGLFSILR IRKSIRKQIR
     QINDKCGLDK LMVRIIIFSI LHIVPILVVI ACNYYQYSHG SIWEPYHHCL CNPYRLETPY
     VTIHLVKYIM LLVPGITTCF WILSGKTLES WWNFLAQKFC CCLTIAPPNP RGQLIGSTSG
     GSSQYIVNSQ RSYKQINHIA QLSASGQPHR KISLSHV
//
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