TNNI1_CAEEL
ID TNNI1_CAEEL Reviewed; 250 AA.
AC Q20334; Q5FBV5;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Troponin I 1;
DE Short=CeTNI-1;
DE Short=TnI 1;
GN Name=tni-1; ORFNames=F42E11.4;
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], AND TISSUE SPECIFICITY.
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, AND DISRUPTION PHENOTYPE.
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: Strongly expressed in body wall muscle during
CC embryogenesis, reduces during the larval stages to adult. In late-stage
CC larvae and adults, expression is evident in the proximal gonad of both
CC hermaphrodites and males. {ECO:0000269|PubMed:14747334,
CC ECO:0000269|PubMed:15743415}.
CC -!- DISRUPTION PHENOTYPE: Worms exhibit abnormal locomotion.
CC {ECO:0000269|PubMed:14747334}.
CC -!- SIMILARITY: Belongs to the troponin I family. {ECO:0000305}.
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DR EMBL; AB107358; BAD89379.1; -; Genomic_DNA.
DR EMBL; Z66562; CAA91466.1; -; Genomic_DNA.
DR PIR; T22093; T22093.
DR RefSeq; NP_509906.1; NM_077505.4.
DR AlphaFoldDB; Q20334; -.
DR SMR; Q20334; -.
DR BioGRID; 46238; 7.
DR DIP; DIP-25521N; -.
DR IntAct; Q20334; 1.
DR STRING; 6239.F42E11.4; -.
DR iPTMnet; Q20334; -.
DR EPD; Q20334; -.
DR PaxDb; Q20334; -.
DR PeptideAtlas; Q20334; -.
DR EnsemblMetazoa; F42E11.4.1; F42E11.4.1; WBGene00006584.
DR GeneID; 181329; -.
DR KEGG; cel:CELE_F42E11.4; -.
DR UCSC; F42E11.4; c. elegans.
DR CTD; 181329; -.
DR WormBase; F42E11.4; CE03311; WBGene00006584; tni-1.
DR eggNOG; KOG3977; Eukaryota.
DR GeneTree; ENSGT01030000234588; -.
DR HOGENOM; CLU_053937_0_0_1; -.
DR InParanoid; Q20334; -.
DR OMA; EICKEYH; -.
DR OrthoDB; 1566919at2759; -.
DR PhylomeDB; Q20334; -.
DR Reactome; R-CEL-5578775; Ion homeostasis.
DR PRO; PR:Q20334; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006584; Expressed in larva and 7 other tissues.
DR GO; GO:0005862; C:muscle thin filament tropomyosin; 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:0043057; P:backward locomotion; IMP:WormBase.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
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..250
FT /note="Troponin I 1"
FT /id="PRO_0000186162"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..250
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 250 AA; 28892 MW; B8D3EA0E0D60539B CRC64;
MSQIDENIRY GGAANETDGE DAQRKAQERE AKKAEVRKRL EEAGQKKQKK GFLTPERKKK
LRKLLMNKAA EDLKTQQLRK EQERVKVLAE RTVALPNVDS IDDHAKLEAI YNDLFSRLCN
LEEEKYDINH ITTETETTIN QLNIEVNDLR GKFVKPSLKK VSKYDNKFKK MAEAKKEDGS
KNLRNNLKTV KKESVFTQIA NKKKSDKPEW SKKKEEKKEE SAPEPVIEPV EEEETAASEG
EEEEEEADEE
