ID   TNNI2_CHICK             Reviewed;         183 AA.
AC   P68246; P02644;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Troponin I, fast skeletal muscle;
DE   AltName: Full=Troponin I, fast-twitch isoform;
GN   Name=TNNI2;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pectoralis muscle;
RX   PubMed=8318890; DOI=10.1002/pro.5560020618;
RA   Quaggio R.B., Ferro J.A., Monteiro P.B., Reinach F.C.;
RT   "Cloning and expression of chicken skeletal muscle troponin I in
RT   Escherichia coli: the role of rare codons on the expression level.";
RL   Protein Sci. 2:1053-1056(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-183, AND ACETYLATION AT SER-2.
RX   PubMed=624283; DOI=10.1111/j.1432-1033.1978.tb12043.x;
RA   Wilkinson J.M., Grand R.J.A.;
RT   "The amino-acid sequence of chicken fast-skeletal-muscle troponin I.";
RL   Eur. J. Biochem. 82:493-501(1978).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 86-183.
RX   PubMed=3010234; DOI=10.1093/nar/14.8.3377;
RA   Nikovits W. Jr., Kuncio G., Ordahl C.P.;
RT   "The chicken fast skeletal troponin I gene: exon organization and
RT   sequence.";
RL   Nucleic Acids Res. 14:3377-3390(1986).
RN   [4] {ECO:0007744|PDB:1YTZ, ECO:0007744|PDB:1YV0}
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 2-183.
RX   PubMed=15784741; DOI=10.1073/pnas.0408882102;
RA   Vinogradova M.V., Stone D.B., Malanina G.G., Karatzaferi C., Cooke R.,
RA   Mendelson R.A., Fletterick R.J.;
RT   "Ca(2+)-regulated structural changes in troponin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:5038-5043(2005).
CC   -!- FUNCTION: Troponin I is the inhibitory subunit of troponin, the thin
CC       filament regulatory complex which confers calcium-sensitivity to
CC       striated muscle actomyosin ATPase activity.
CC   -!- SUBUNIT: Binds to actin and tropomyosin.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the troponin I family. {ECO:0000305}.
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DR   EMBL; U19926; AAA61952.1; -; mRNA.
DR   EMBL; X03832; CAA27447.1; -; mRNA.
DR   PIR; A24918; TPCHIS.
DR   RefSeq; NP_990748.1; NM_205417.1.
DR   PDB; 1VDI; NMR; -; A=132-183.
DR   PDB; 1VDJ; NMR; -; A=132-183.
DR   PDB; 1YTZ; X-ray; 3.00 A; I=2-183.
DR   PDB; 1YV0; X-ray; 7.00 A; I=2-138.
DR   PDB; 2W49; EM; 35.00 A; 2/5/8/Z=4-144.
DR   PDB; 2W4U; EM; 35.00 A; 2/5/8/Z=4-144.
DR   PDBsum; 1VDI; -.
DR   PDBsum; 1VDJ; -.
DR   PDBsum; 1YTZ; -.
DR   PDBsum; 1YV0; -.
DR   PDBsum; 2W49; -.
DR   PDBsum; 2W4U; -.
DR   AlphaFoldDB; P68246; -.
DR   BMRB; P68246; -.
DR   SMR; P68246; -.
DR   IntAct; P68246; 1.
DR   STRING; 9031.ENSGALP00000010627; -.
DR   iPTMnet; P68246; -.
DR   PaxDb; P68246; -.
DR   GeneID; 396386; -.
DR   KEGG; gga:396386; -.
DR   CTD; 7136; -.
DR   VEuPathDB; HostDB:geneid_396386; -.
DR   eggNOG; KOG3977; Eukaryota.
DR   HOGENOM; CLU_098686_1_0_1; -.
DR   InParanoid; P68246; -.
DR   OrthoDB; 1566919at2759; -.
DR   PhylomeDB; P68246; -.
DR   EvolutionaryTrace; P68246; -.
DR   PRO; PR:P68246; -.
DR   Proteomes; UP000000539; Unplaced.
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   DisProt; DP01871; -.
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   1: Evidence at protein level;
KW   3D-structure; Acetylation; Actin-binding; Direct protein sequencing;
KW   Muscle protein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:624283"
FT   CHAIN           2..183
FT                   /note="Troponin I, fast skeletal muscle"
FT                   /id="PRO_0000186147"
FT   REGION          2..48
FT                   /note="Involved in binding TNC"
FT   REGION          97..117
FT                   /note="Involved in binding TNC and actin"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:624283"
FT   HELIX           8..48
FT                   /evidence="ECO:0007829|PDB:1YTZ"
FT   HELIX           58..96
FT                   /evidence="ECO:0007829|PDB:1YTZ"
FT   TURN            97..104
FT                   /evidence="ECO:0007829|PDB:1YTZ"
FT   HELIX           119..127
FT                   /evidence="ECO:0007829|PDB:1YTZ"
FT   HELIX           133..141
FT                   /evidence="ECO:0007829|PDB:1VDI"
FT   STRAND          142..153
FT                   /evidence="ECO:0007829|PDB:1VDI"
FT   HELIX           159..167
FT                   /evidence="ECO:0007829|PDB:1VDI"
FT   HELIX           170..178
FT                   /evidence="ECO:0007829|PDB:1VDI"
SQ   SEQUENCE   183 AA;  21234 MW;  E33F7517E84BB09E CRC64;
     MSDEEKKRRA ATARRQHLKS AMLQLAVTEI EKEAAAKEVE KQNYLAEHCP PLSLPGSMQE
     LQELCKKLHA KIDSVDEERY DTEVKLQKTN KELEDLSQKL FDLRGKFKRP PLRRVRMSAD
     AMLRALLGSK HKVNMDLRAN LKQVKKEDTE KEKDLRDVGD WRKNIEEKSG MEGRKKMFEA
     GES