ID   TNNI3_CAEEL             Reviewed;         260 AA.
AC   Q9XUN9; Q5FBV4;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Troponin I 3;
DE            Short=CeTNI-3;
DE            Short=TnI 3;
GN   Name=tni-3; ORFNames=T20B3.2;
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], TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=15743415; DOI=10.1111/j.1365-2443.2005.00829.x;
RA   Ruksana R., Kuroda K., Terami H., Bando T., Kitaoka S., Takaya T.,
RA   Sakube Y., Kagawa H.;
RT   "Tissue expression of four troponin I genes and their molecular
RT   interactions with two troponin C isoforms in Caenorhabditis elegans.";
RL   Genes Cells 10:261-276(2005).
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).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=14747334; DOI=10.1016/s0006-3495(04)74174-0;
RA   Burkeen A.K., Maday S.L., Rybicka K.K., Sulcove J.A., Ward J., Huang M.M.,
RA   Barstead R., Franzini-Armstrong C., Allen T.S.;
RT   "Disruption of Caenorhabditis elegans muscle structure and function caused
RT   by mutation of troponin I.";
RL   Biophys. J. 86:991-1001(2004).
CC   -!- FUNCTION: Troponin I is the inhibitory subunit of troponin, the thin
CC       filament regulatory complex which confers calcium-sensitivity to muscle
CC       actomyosin ATPase activity. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in body wall muscle from first larval
CC       stage to adult. In adults expression is predominantly in vulval and
CC       anal muscles, body wall muscle expression is weaker. Also expressed in
CC       vulval muscles of hermaphrodites and the sex muscles of males.
CC       {ECO:0000269|PubMed:14747334, ECO:0000269|PubMed:15743415}.
CC   -!- DISRUPTION PHENOTYPE: Worms exhibit abnormal muscle morphology, egg
CC       laying defects and constipation. {ECO:0000269|PubMed:15743415}.
CC   -!- SIMILARITY: Belongs to the troponin I family. {ECO:0000305}.
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DR   EMBL; AB107359; BAD89380.1; -; Genomic_DNA.
DR   EMBL; Z81593; CAB04737.1; -; Genomic_DNA.
DR   PIR; T25017; T25017.
DR   RefSeq; NP_507250.1; NM_074849.7.
DR   AlphaFoldDB; Q9XUN9; -.
DR   SMR; Q9XUN9; -.
DR   BioGRID; 45113; 8.
DR   DIP; DIP-27192N; -.
DR   IntAct; Q9XUN9; 2.
DR   MINT; Q9XUN9; -.
DR   STRING; 6239.T20B3.2.1; -.
DR   EPD; Q9XUN9; -.
DR   PaxDb; Q9XUN9; -.
DR   PeptideAtlas; Q9XUN9; -.
DR   EnsemblMetazoa; T20B3.2.1; T20B3.2.1; WBGene00006585.
DR   GeneID; 180127; -.
DR   KEGG; cel:CELE_T20B3.2; -.
DR   UCSC; T20B3.2.1; c. elegans.
DR   CTD; 180127; -.
DR   WormBase; T20B3.2; CE20087; WBGene00006585; tni-3.
DR   eggNOG; KOG3977; Eukaryota.
DR   GeneTree; ENSGT01030000234588; -.
DR   HOGENOM; CLU_053937_0_0_1; -.
DR   InParanoid; Q9XUN9; -.
DR   OMA; YEDMFAR; -.
DR   OrthoDB; 1566919at2759; -.
DR   PhylomeDB; Q9XUN9; -.
DR   Reactome; R-CEL-5578775; Ion homeostasis.
DR   PRO; PR:Q9XUN9; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00006585; Expressed in male organism and 17 other tissues.
DR   GO; GO:0030016; C:myofibril; HDA:WormBase.
DR   GO; GO:0030017; C:sarcomere; IDA:WormBase.
DR   GO; GO:0005861; C:troponin complex; IEA:InterPro.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030172; F:troponin C binding; IPI:WormBase.
DR   GO; GO:0006936; P:muscle contraction; IMP:WormBase.
DR   GO; GO:0018991; P:oviposition; IMP:WormBase.
DR   GO; GO:0040032; P:post-embryonic body morphogenesis; IMP:WormBase.
DR   Gene3D; 1.20.5.350; -; 1.
DR   InterPro; IPR001978; Troponin.
DR   InterPro; IPR038077; Troponin_sf.
DR   Pfam; PF00992; Troponin; 1.
DR   SUPFAM; SSF90250; SSF90250; 1.
PE   2: Evidence at transcript level;
KW   Actin-binding; Muscle protein; Reference proteome.
FT   CHAIN           1..260
FT                   /note="Troponin I 3"
FT                   /id="PRO_0000186163"
FT   REGION          192..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..223
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..260
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   260 AA;  29839 MW;  92EC30574A355974 CRC64;
     MLIEDENIRY GGAQADVEDD AARKAQEREL KKAEVRKRME EAAKKGSKKK GFLTPERKKK
     LRKLLMMKAA EDLKQQQMLK EQERQKTLQQ RTIPLPDVDS INDQGQLLKI YEDMFARVCA
     LEEEKFDINF GVSQTEAEIN QLTIQVNDLR GKFVKPTLKK VSKYDNKFKS SGEVKEKSNF
     RNNLKVVKKE TDLDEIMAKK KGTADGKPEW SKKEKKEEEA APVELAAPVE PEAEPEPEAA
     EPAAEEPEAE EEEEEEEEEE