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TNNC2_CAEEL
ID   TNNC2_CAEEL             Reviewed;         160 AA.
AC   Q09665;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Troponin C, isoform 2;
GN   Name=tnc-2; ORFNames=ZK673.7;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Bristol N2; TISSUE=Pharyngeal muscle;
RA   Terami H., Kagawa H.;
RT   "Functional characterization of the pharyngeal troponin C of Caenorhabditis
RT   elegans.";
RL   Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- TISSUE SPECIFICITY: Pharyngeal muscle.
CC   -!- MISCELLANEOUS: This protein binds two calcium ions. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the troponin C family. {ECO:0000305}.
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DR   EMBL; AB079299; BAB84566.1; -; Genomic_DNA.
DR   EMBL; Z48585; CAA88482.1; -; Genomic_DNA.
DR   PIR; T27963; T27963.
DR   RefSeq; NP_496251.1; NM_063850.5.
DR   AlphaFoldDB; Q09665; -.
DR   SMR; Q09665; -.
DR   BioGRID; 39930; 13.
DR   DIP; DIP-25700N; -.
DR   IntAct; Q09665; 3.
DR   STRING; 6239.ZK673.7; -.
DR   EPD; Q09665; -.
DR   PaxDb; Q09665; -.
DR   PeptideAtlas; Q09665; -.
DR   EnsemblMetazoa; ZK673.7.1; ZK673.7.1; WBGene00006583.
DR   GeneID; 174612; -.
DR   KEGG; cel:CELE_ZK673.7; -.
DR   UCSC; ZK673.7.1; c. elegans.
DR   CTD; 174612; -.
DR   WormBase; ZK673.7; CE01719; WBGene00006583; tnc-2.
DR   eggNOG; KOG0027; Eukaryota.
DR   GeneTree; ENSGT00940000172595; -.
DR   HOGENOM; CLU_061288_2_4_1; -.
DR   InParanoid; Q09665; -.
DR   OMA; MGQAFED; -.
DR   OrthoDB; 1340191at2759; -.
DR   PhylomeDB; Q09665; -.
DR   Reactome; R-CEL-111932; CaMK IV-mediated phosphorylation of CREB.
DR   Reactome; R-CEL-111933; Calmodulin induced events.
DR   Reactome; R-CEL-111957; Cam-PDE 1 activation.
DR   Reactome; R-CEL-114608; Platelet degranulation.
DR   Reactome; R-CEL-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR   Reactome; R-CEL-163615; PKA activation.
DR   Reactome; R-CEL-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR   Reactome; R-CEL-203615; eNOS activation.
DR   Reactome; R-CEL-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR   Reactome; R-CEL-2672351; Stimuli-sensing channels.
DR   Reactome; R-CEL-2871809; FCERI mediated Ca+2 mobilization.
DR   Reactome; R-CEL-4086398; Ca2+ pathway.
DR   Reactome; R-CEL-418359; Reduction of cytosolic Ca++ levels.
DR   Reactome; R-CEL-425561; Sodium/Calcium exchangers.
DR   Reactome; R-CEL-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR   Reactome; R-CEL-442729; CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde.
DR   Reactome; R-CEL-451308; Activation of Ca-permeable Kainate Receptor.
DR   Reactome; R-CEL-5218920; VEGFR2 mediated vascular permeability.
DR   Reactome; R-CEL-5578775; Ion homeostasis.
DR   Reactome; R-CEL-5607763; CLEC7A (Dectin-1) induces NFAT activation.
DR   Reactome; R-CEL-5626467; RHO GTPases activate IQGAPs.
DR   Reactome; R-CEL-6798695; Neutrophil degranulation.
DR   Reactome; R-CEL-70221; Glycogen breakdown (glycogenolysis).
DR   Reactome; R-CEL-9009391; Extra-nuclear estrogen signaling.
DR   Reactome; R-CEL-936837; Ion transport by P-type ATPases.
DR   Reactome; R-CEL-9619229; Activation of RAC1 downstream of NMDARs.
DR   Reactome; R-CEL-9648002; RAS processing.
DR   PRO; PR:Q09665; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00006583; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR   GO; GO:0031013; F:troponin I binding; IPI:WormBase.
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; Reference proteome; Repeat.
FT   CHAIN           1..160
FT                   /note="Troponin C, isoform 2"
FT                   /id="PRO_0000073685"
FT   DOMAIN          15..50
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          51..86
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          92..127
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          128..160
FT                   /note="EF-hand 4"
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         68
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         70
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         75
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         141
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         143
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         145
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   BINDING         152
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ   SEQUENCE   160 AA;  18227 MW;  18552E2D8D5D58CE CRC64;
     MGDVVADALE KLSADQIEQF RKYFNMFDKE GKGYIRATQV GQILRTMGQA FEERDLKQLI
     KEFDADGSGE IEFEEFAAMV ANFVVNNEND EGLEEELREA FRLYDKEGNG YINVSDLRDI
     LRALDDNVSE EELDEMIAEI DADGSGTVDF DEFMEMMSGE
 
 
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