TNNI2_CAEEL
ID TNNI2_CAEEL Reviewed; 242 AA.
AC Q9GYF1; Q5FBV6;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Troponin I 2;
DE Short=CeTNI-2;
DE Short=TnI 2;
DE AltName: Full=Uncoordinated protein 27;
GN Name=unc-27; Synonyms=tni-2; ORFNames=ZK721.2;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Body wall muscle;
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: Expressed in body-wall musculature, with weak
CC expression in late-stage embryos and strong expression during the
CC larval and adult stages. Also expressed in vulval and anal muscles, and
CC weakly expressed in pharyngeal muscle. {ECO:0000269|PubMed:14747334,
CC ECO:0000269|PubMed:15743415}.
CC -!- DISRUPTION PHENOTYPE: Worms exhibit abnormal locomotion, unregulated
CC contraction of the sarcomeres due to small portions of each myofibril
CC shortening irregularly and independently from another causing rigid
CC paralysis. This is due to poorly defined sarcomeric structure, with
CC small islands of thin filaments interspersed within the overlap region
CC of A bands and the H zone. {ECO:0000269|PubMed:14747334}.
CC -!- SIMILARITY: Belongs to the troponin I family. {ECO:0000305}.
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DR EMBL; FO081647; CCD73101.1; -; Genomic_DNA.
DR EMBL; AB107357; BAD89378.1; -; Genomic_DNA.
DR PIR; T27985; T27985.
DR RefSeq; NP_509488.2; NM_077087.6.
DR AlphaFoldDB; Q9GYF1; -.
DR SMR; Q9GYF1; -.
DR BioGRID; 46043; 10.
DR DIP; DIP-26517N; -.
DR IntAct; Q9GYF1; 1.
DR STRING; 6239.ZK721.2; -.
DR iPTMnet; Q9GYF1; -.
DR EPD; Q9GYF1; -.
DR PaxDb; Q9GYF1; -.
DR PeptideAtlas; Q9GYF1; -.
DR EnsemblMetazoa; ZK721.2.1; ZK721.2.1; WBGene00006764.
DR GeneID; 181124; -.
DR KEGG; cel:CELE_ZK721.2; -.
DR UCSC; ZK721.2; c. elegans.
DR CTD; 181124; -.
DR WormBase; ZK721.2; CE40008; WBGene00006764; unc-27.
DR eggNOG; KOG3977; Eukaryota.
DR GeneTree; ENSGT01030000234588; -.
DR HOGENOM; CLU_053937_0_0_1; -.
DR InParanoid; Q9GYF1; -.
DR OMA; KQDFRAN; -.
DR OrthoDB; 1566919at2759; -.
DR PhylomeDB; Q9GYF1; -.
DR Reactome; R-CEL-5578775; Ion homeostasis.
DR PRO; PR:Q9GYF1; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006764; Expressed in larva and 5 other tissues.
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:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0045214; P:sarcomere organization; 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..242
FT /note="Troponin I 2"
FT /id="PRO_0000253017"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..242
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 242 AA; 27560 MW; 5B8B13951A5DA118 CRC64;
MSEEAGEDAQ RKAAEREAKK AEVRKRLEEA GNKKKAKKGF LTPERKKKLR KLLMVKAAED
LKRQQLLKEQ ERQKALADRT ISLPNVDSID DKGQLEKIYN DLWARLTQLE EEKYDINYVV
SQTEAEINSL TIEVNDLRGK FVKPSLKKVS KYDNKFKKSG ESKAGTKEDF RANLKIVKKD
VMEAIVNVKK KDDKPDWSKK NKDAKAEDSA PAAVAPEAEP VAEEAEAEPE AEEEEGEEEE
EE
