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TNNC3_DROME
ID   TNNC3_DROME             Reviewed;         155 AA.
AC   P47949; C8VV65; Q9VVE1;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 2.
DT   03-AUG-2022, entry version 165.
DE   RecName: Full=Troponin C, isoform 3;
GN   Name=TpnC73F; Synonyms=TnC73F; ORFNames=CG7930;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7980384; DOI=10.1007/bf00554420;
RA   Fyrberg C., Parker H., Hutchison B., Fyrberg E.A.;
RT   "Drosophila melanogaster genes encoding three troponin-C isoforms and a
RT   calmodulin-related protein.";
RL   Biochem. Genet. 32:119-135(1994).
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., 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   [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., 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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Larva, and Pupae;
RA   Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- TISSUE SPECIFICITY: Present in both larval and adult muscles.
CC   -!- SIMILARITY: Belongs to the troponin C family. {ECO:0000305}.
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DR   EMBL; X76042; CAA53627.1; -; mRNA.
DR   EMBL; AE014296; AAF49371.1; -; Genomic_DNA.
DR   EMBL; BT099811; ACV91648.1; -; mRNA.
DR   PIR; S38878; S38878.
DR   RefSeq; NP_001287091.1; NM_001300162.1.
DR   RefSeq; NP_524122.2; NM_079398.4.
DR   AlphaFoldDB; P47949; -.
DR   SMR; P47949; -.
DR   BioGRID; 65208; 2.
DR   DIP; DIP-23693N; -.
DR   IntAct; P47949; 1.
DR   STRING; 7227.FBpp0088546; -.
DR   PaxDb; P47949; -.
DR   PRIDE; P47949; -.
DR   DNASU; 39916; -.
DR   EnsemblMetazoa; FBtr0089585; FBpp0088546; FBgn0010424.
DR   EnsemblMetazoa; FBtr0345120; FBpp0311345; FBgn0010424.
DR   GeneID; 39916; -.
DR   KEGG; dme:Dmel_CG7930; -.
DR   CTD; 39916; -.
DR   FlyBase; FBgn0010424; TpnC73F.
DR   VEuPathDB; VectorBase:FBgn0010424; -.
DR   eggNOG; KOG0027; Eukaryota.
DR   HOGENOM; CLU_061288_2_4_1; -.
DR   InParanoid; P47949; -.
DR   OMA; HELDIMI; -.
DR   OrthoDB; 1340191at2759; -.
DR   PhylomeDB; P47949; -.
DR   Reactome; R-DME-111932; CaMK IV-mediated phosphorylation of CREB.
DR   Reactome; R-DME-111933; Calmodulin induced events.
DR   Reactome; R-DME-111957; Cam-PDE 1 activation.
DR   Reactome; R-DME-114608; Platelet degranulation.
DR   Reactome; R-DME-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR   Reactome; R-DME-163615; PKA activation.
DR   Reactome; R-DME-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR   Reactome; R-DME-2025928; Calcineurin activates NFAT.
DR   Reactome; R-DME-203615; eNOS activation.
DR   Reactome; R-DME-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR   Reactome; R-DME-2871809; FCERI mediated Ca+2 mobilization.
DR   Reactome; R-DME-4086398; Ca2+ pathway.
DR   Reactome; R-DME-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR   Reactome; R-DME-442729; CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde.
DR   Reactome; R-DME-451308; Activation of Ca-permeable Kainate Receptor.
DR   Reactome; R-DME-5218920; VEGFR2 mediated vascular permeability.
DR   Reactome; R-DME-5578775; Ion homeostasis.
DR   Reactome; R-DME-5607763; CLEC7A (Dectin-1) induces NFAT activation.
DR   Reactome; R-DME-5673000; RAF activation.
DR   Reactome; R-DME-6798695; Neutrophil degranulation.
DR   Reactome; R-DME-70221; Glycogen breakdown (glycogenolysis).
DR   Reactome; R-DME-8876725; Protein methylation.
DR   Reactome; R-DME-9009391; Extra-nuclear estrogen signaling.
DR   Reactome; R-DME-936837; Ion transport by P-type ATPases.
DR   Reactome; R-DME-9619229; Activation of RAC1 downstream of NMDARs.
DR   Reactome; R-DME-9648002; RAS processing.
DR   BioGRID-ORCS; 39916; 0 hits in 1 CRISPR screen.
DR   ChiTaRS; TpnC73F; fly.
DR   GenomeRNAi; 39916; -.
DR   PRO; PR:P47949; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0010424; Expressed in oviduct (Drosophila) and 27 other tissues.
DR   ExpressionAtlas; P47949; baseline and differential.
DR   Genevisible; P47949; DM.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR   CDD; cd00051; EFh; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   Pfam; PF13499; EF-hand_7; 2.
DR   SMART; SM00054; EFh; 4.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 4.
PE   2: Evidence at transcript level;
KW   Calcium; Metal-binding; Muscle protein; Reference proteome; Repeat.
FT   CHAIN           1..155
FT                   /note="Troponin C, isoform 3"
FT                   /id="PRO_0000073688"
FT   DOMAIN          11..46
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          47..82
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          87..122
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          123..155
FT                   /note="EF-hand 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         60
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         62
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         64
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         66
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         71
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         136
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         138
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         140
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         142
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         147
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   CONFLICT        93
FT                   /note="R -> A (in Ref. 1; CAA53627)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   155 AA;  17696 MW;  F45FCF78438C4D0B CRC64;
     MSSVDEDLTP EQIAVLQKAF NSFDHQKTGS IPTEMVADIL RLMGQPFDKK ILEELIEEVD
     EDKSGRLEFG EFVQLAAKFI VEEDAEAMQK ELREAFRLYD KQGNGFIPTT CLKEILKELD
     DQLTEQELDI MIEEIDSDGS GTVDFDEFME MMTGE
 
 
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