GenomeNet

Database: UniProt
Entry: TRPG_DROME
LinkDB: TRPG_DROME
Original site: TRPG_DROME 
ID   TRPG_DROME              Reviewed;        1128 AA.
AC   Q9VJJ7; A4V0S8; Q9N6L1;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 2.
DT   27-SEP-2017, entry version 144.
DE   RecName: Full=Transient receptor potential-gamma protein;
DE            Short=TRPgamma;
DE   AltName: Full=Transient receptor potential cation channel gamma;
GN   Name=Trpgamma; ORFNames=CG5996;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH TRP AND TRPL,
RP   AND TISSUE SPECIFICITY.
RC   TISSUE=Head;
RX   PubMed=10896160; DOI=10.1016/S0896-6273(00)81201-5;
RA   Xu X.-Z.S., Chien F., Butler A., Salkoff L., Montell C.;
RT   "TRPgamma, a Drosophila TRP-related subunit, forms a regulated cation
RT   channel with TRPL.";
RL   Neuron 26:647-657(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
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.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   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.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   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.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
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.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
CC   -!- FUNCTION: A light-sensitive calcium channel that is required for
CC       inositide-mediated Ca(2+) entry in the retina during phospholipase
CC       C (PLC)-mediated phototransduction (By similarity). Forms a
CC       regulated cation channel when heteromultimerized with trpl.
CC       {ECO:0000250, ECO:0000269|PubMed:10896160}.
CC   -!- SUBUNIT: Interacts preferentially with trpl and interacts to a
CC       lower extent with trp. {ECO:0000269|PubMed:10896160}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in the rhabdomeres of
CC       photoreceptor cells. {ECO:0000269|PubMed:10896160}.
CC   -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family.
CC       STrpC subfamily. {ECO:0000305}.
DR   EMBL; AJ277967; CAB96204.1; -; mRNA.
DR   EMBL; AJ277968; CAB96205.1; -; mRNA.
DR   EMBL; AE014134; AAF53548.2; -; Genomic_DNA.
DR   EMBL; AE014134; AAN10950.1; -; Genomic_DNA.
DR   RefSeq; NP_609802.1; NM_135958.5.
DR   RefSeq; NP_723983.1; NM_165169.5.
DR   ProteinModelPortal; Q9VJJ7; -.
DR   SMR; Q9VJJ7; -.
DR   BioGrid; 60999; 1.
DR   IntAct; Q9VJJ7; 3.
DR   STRING; 7227.FBpp0080498; -.
DR   PaxDb; Q9VJJ7; -.
DR   PRIDE; Q9VJJ7; -.
DR   EnsemblMetazoa; FBtr0080945; FBpp0080498; FBgn0032593.
DR   EnsemblMetazoa; FBtr0080946; FBpp0080499; FBgn0032593.
DR   GeneID; 34991; -.
DR   KEGG; dme:Dmel_CG5996; -.
DR   UCSC; CG5996-RA; d. melanogaster.
DR   CTD; 34991; -.
DR   FlyBase; FBgn0032593; Trpgamma.
DR   eggNOG; KOG3609; Eukaryota.
DR   eggNOG; ENOG410XQ0Y; LUCA.
DR   GeneTree; ENSGT00760000119180; -.
DR   InParanoid; Q9VJJ7; -.
DR   KO; K04967; -.
DR   OrthoDB; EOG091G029I; -.
DR   PhylomeDB; Q9VJJ7; -.
DR   Reactome; R-DME-3295583; TRP channels.
DR   SignaLink; Q9VJJ7; -.
DR   GenomeRNAi; 34991; -.
DR   PRO; PR:Q9VJJ7; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0032593; -.
DR   ExpressionAtlas; Q9VJJ7; differential.
DR   Genevisible; Q9VJJ7; DM.
DR   GO; GO:0034703; C:cation channel complex; IPI:FlyBase.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0043025; C:neuronal cell body; IDA:FlyBase.
DR   GO; GO:1990635; C:proximal dendrite; IDA:FlyBase.
DR   GO; GO:0016028; C:rhabdomere; IDA:UniProtKB.
DR   GO; GO:0005262; F:calcium channel activity; ISS:UniProtKB.
DR   GO; GO:0005261; F:cation channel activity; IDA:FlyBase.
DR   GO; GO:0022833; F:mechanically gated channel activity; IDA:FlyBase.
DR   GO; GO:0015279; F:store-operated calcium channel activity; IBA:GO_Central.
DR   GO; GO:0007628; P:adult walking behavior; IMP:FlyBase.
DR   GO; GO:0006816; P:calcium ion transport; ISS:UniProtKB.
DR   GO; GO:0006812; P:cation transport; IDA:FlyBase.
DR   GO; GO:0050908; P:detection of light stimulus involved in visual perception; ISS:UniProtKB.
DR   GO; GO:0006828; P:manganese ion transport; IBA:GO_Central.
DR   GO; GO:0050884; P:neuromuscular process controlling posture; IMP:FlyBase.
DR   GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR   GO; GO:0009416; P:response to light stimulus; ISS:UniProtKB.
DR   CDD; cd00204; ANK; 1.
DR   Gene3D; 1.25.40.20; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR004729; TRP_channel.
DR   InterPro; IPR013555; TRP_dom.
DR   InterPro; IPR002153; TRPC_channel.
DR   PANTHER; PTHR10117; PTHR10117; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF08344; TRP_2; 1.
DR   PRINTS; PR01097; TRNSRECEPTRP.
DR   SMART; SM00248; ANK; 2.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   TIGRFAMs; TIGR00870; trp; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
PE   1: Evidence at protein level;
KW   ANK repeat; Calcium; Calcium channel; Calcium transport;
KW   Complete proteome; Ion channel; Ion transport; Membrane;
KW   Reference proteome; Repeat; Sensory transduction; Transmembrane;
KW   Transmembrane helix; Transport; Vision.
FT   CHAIN         1   1128       Transient receptor potential-gamma
FT                                protein.
FT                                /FTId=PRO_0000215358.
FT   TOPO_DOM      1    325       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    326    346       Helical. {ECO:0000255}.
FT   TOPO_DOM    347    403       Extracellular. {ECO:0000255}.
FT   TRANSMEM    404    424       Helical. {ECO:0000255}.
FT   TOPO_DOM    425    444       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    445    465       Helical. {ECO:0000255}.
FT   TOPO_DOM    466    492       Extracellular. {ECO:0000255}.
FT   TRANSMEM    493    513       Helical. {ECO:0000255}.
FT   TOPO_DOM    514    535       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    536    556       Helical. {ECO:0000255}.
FT   TOPO_DOM    557    629       Extracellular. {ECO:0000255}.
FT   TRANSMEM    630    650       Helical. {ECO:0000255}.
FT   TOPO_DOM    651   1128       Cytoplasmic. {ECO:0000255}.
FT   REPEAT       57     86       ANK 1.
FT   REPEAT      131    160       ANK 2.
FT   CONFLICT    195    195       S -> G (in Ref. 1; CAB96204/CAB96205).
FT                                {ECO:0000305}.
FT   CONFLICT    222    222       F -> L (in Ref. 1; CAB96204/CAB96205).
FT                                {ECO:0000305}.
FT   CONFLICT   1053   1053       D -> N (in Ref. 1; CAB96204/CAB96205).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1128 AA;  127109 MW;  A0B519C7DFBE5983 CRC64;
     MMEEENTIRP HQEIRQLTLE EKKFLLAVER GDMAGTRRML QKAQDTEYIN VNCVDPLGRT
     ALLMAIDNEN LEMVELLINY NVDTKDALLH SISEEFVEAV EVLLDHENVT FHSEGNHSWE
     SASEDTSTFT PDITPLILAA HRDNYEIIKI LLDRGAVLPM PHDVRCGCDE CVQSRQEDSL
     RHSRSRINAY RALASPSLIA LSSKDPILTA FELSWELRRL SFLEHEFKNE YQELRKQCQD
     FATALLDHTR TSHELEILLN HDPTGPVYEH GERMHLNRLK LAIKLRQKKF VAHSNVQQLL
     ASIWYEGLPG FRRKNMALQA VDIIRIGIMF PIFSLAYILA PYSSIGQTMR KPFIKFICHS
     ASYFTFLFLL MLASQRIETF IGGWFFADSS GMLNTMEELP TKRGAKPTFI EWLILAWVSG
     LIWSEVKQLW DVGLQEYLND MWNVIDFVTN SLYVATVALR VVSFFQVQKE MIYNSHATDL
     PRERWDAWDP MLISEGLFSA ANIFSSLKLV YIFSVNPHLG PLQVSLSRMV MDIMKFFFLY
     VLVLFAFGSG LNQLLWYYAD LEKKRCPEVS PMSALLNMNG TNDPNACIVW RRFSNLFETT
     QTLFWAVFGL IDLDSFELDG IKIFTRFWGM LMFGTYSVIN IVVLLNLLIA MMNHSYQLIS
     ERADVEWKFA RSKLWISYFE EGGTCPPPFN IIPTPKSIWY AIKWMRRVFC SGSSAARREH
     LKTIRRKAQQ ASDRDFKYQQ IMRNLVRRYV TVEQRKAESQ GVTEDDVNEI KQDISAFRCE
     LVEILKNSGM DTNVTAGQGG GGGGKKNRQK ERRLMKGFNI APPGSTGSLA PVAEFSTSLD
     NYDNQHEILS STLSTLFTPN FMHKRQQSQA GSGGGGSESP TTPTAPQGTQ GAAMTASSQV
     TKYNKSALKP YNKRIAGHKK RWGTLIEAAK VGNVSKMLGR SKSEDSVCNS SHTSTPVHGQ
     MRVTYAQNSP QQEYGYHGET SSTTISTPTP TISVVSNSPA AHAGVGSHFF HTTSGLTAIA
     ALKRKRKKFS SSKNICPVTE SVAAANAAEI LNDKTLKRVS SYPAAEAGVQ HNPAQLVKPR
     RHEQTQSQHD SVETNSTFTL SIDPSNTSVN SREPLISTSC VSTTGAIG
//
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