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TRISR_DROME
ID   TRISR_DROME             Reviewed;         669 AA.
AC   Q9VML9; Q9VMM1;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 4.
DT   03-AUG-2022, entry version 168.
DE   RecName: Full=Trissin receptor {ECO:0000312|FlyBase:FBgn0085410};
GN   Name=TrissinR {ECO:0000312|FlyBase:FBgn0085410};
GN   ORFNames=CG34381 {ECO:0000312|FlyBase:FBgn0085410};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN   [1] {ECO:0000312|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2] {ECO:0000312|Proteomes:UP000000803}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3] {ECO:0000312|EMBL:ACJ23469.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL   Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000305}
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=21939639; DOI=10.1016/j.bbrc.2011.09.018;
RA   Ida T., Takahashi T., Tominaga H., Sato T., Kume K., Yoshizawa-Kumagaye K.,
RA   Nishio H., Kato J., Murakami N., Miyazato M., Kangawa K., Kojima M.;
RT   "Identification of the endogenous cysteine-rich peptide trissin, a ligand
RT   for an orphan G protein-coupled receptor in Drosophila.";
RL   Biochem. Biophys. Res. Commun. 414:44-48(2011).
CC   -!- FUNCTION: G-protein coupled receptor which is activated by the Trissin
CC       peptide in vitro, leading to increased intracellular calcium ion
CC       levels. {ECO:0000269|PubMed:21939639}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:21939639};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AE014134; AAF52294.4; -; Genomic_DNA.
DR   EMBL; BT050585; ACJ23469.1; -; mRNA.
DR   RefSeq; NP_001097092.1; NM_001103622.2.
DR   AlphaFoldDB; Q9VML9; -.
DR   IntAct; Q9VML9; 2.
DR   STRING; 7227.FBpp0111531; -.
DR   GlyGen; Q9VML9; 4 sites.
DR   PaxDb; Q9VML9; -.
DR   DNASU; 33812; -.
DR   EnsemblMetazoa; FBtr0112619; FBpp0111531; FBgn0085410.
DR   GeneID; 33812; -.
DR   KEGG; dme:Dmel_CG34381; -.
DR   UCSC; CG34381-RA; d. melanogaster.
DR   CTD; 33812; -.
DR   FlyBase; FBgn0085410; TrissinR.
DR   VEuPathDB; VectorBase:FBgn0085410; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   InParanoid; Q9VML9; -.
DR   PhylomeDB; Q9VML9; -.
DR   BioGRID-ORCS; 33812; 0 hits in 1 CRISPR screen.
DR   ChiTaRS; TrissinR; fly.
DR   GenomeRNAi; 33812; -.
DR   PRO; PR:Q9VML9; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0085410; Expressed in oviduct (Drosophila) and 10 other tissues.
DR   ExpressionAtlas; Q9VML9; differential.
DR   GO; GO:0016021; C:integral component of membrane; ISS:FlyBase.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
DR   GO; GO:0008528; F:G protein-coupled peptide receptor activity; IPI:FlyBase.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR   GO; GO:0008188; F:neuropeptide receptor activity; ISM:FlyBase.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:FlyBase.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..669
FT                   /note="Trissin receptor"
FT                   /id="PRO_0000437961"
FT   TOPO_DOM        1..184
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        185..205
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        206..217
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        218..238
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        239..269
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        270..290
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        291..302
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        303..323
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        324..350
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        351..371
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        372..552
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        553..573
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        574..595
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        596..616
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        617..669
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          1..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          390..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          515..537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          635..669
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..31
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..79
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        390..407
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        414..430
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        655..669
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        66
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        120
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        130
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        241
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        257..340
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   669 AA;  74486 MW;  6A19AC090664A52B CRC64;
     MIMTMMQTVR AWQQESDVEH RKQHKQRWRP DGAHISAAYD LNSDNDDGHH RVVHNQNNGS
     PNSSPNQSTS AFRQRQPHHP PTGQQPPRLP CTVTHFSAHW KTLLILLTLL SASTLTASAN
     VTSTISPPIN GSSTDYILLY GESTTSLVPA LTTGLSGDGS GAVIEDEEDA EKASEYIFDR
     TDVRIIFITL YTLVFCCCFF GNLLVILVVT LSRRLRSITN FFLANLAFAD FCVGLFCVMQ
     NLSIYLIESW VFGEFLCRMY QFVHSLSYTA SIFILVVICM ERYFAIVHPI TCKQILTAAR
     LRMVIVTVWI TSAVYSTPKF VFSKTIKNIH TQDGQEEEIC VLDREMFNSK LLDMINFVLL
     YVMPLLVMTV LYSKIAIALW RSSRGLTPHV VQHQHQQPQQ PSCQDIGMGM HNSMYHHHPH
     HHHHHHQHHQ LQSAASSAGV VGVGLGGGGG GGPGPSLASG GSSTTSLSRK QSSKYEKRGV
     SITESQLDNC KVSLEADRPI VSACRKTSFY HHGHAHHQRA GNASVGGGSG GAGAGATHMS
     HSSSNVLRAR RGVVRMLIIF VLTFALCNLP YHARKMWQYW SRSYRGDSNF NALLTPLTFL
     VTYFNSGVNP LLYAFLSRNF RKGMKELLLC SWKKGKGKSS SNSSMHHKRK ALQTHSLPTD
     TTHIGNEQL
 
 
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