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Troponin I, fast skeletal muscle (Troponin I, fast-twitch isoform)

 TNNI2_CHICK             Reviewed;         183 AA.
P68246; P02644;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 89.
RecName: Full=Troponin I, fast skeletal muscle;
AltName: Full=Troponin I, fast-twitch isoform;
Name=TNNI2;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Pectoralis muscle;
PubMed=8318890; DOI=10.1002/pro.5560020618;
Quaggio R.B., Ferro J.A., Monteiro P.B., Reinach F.C.;
"Cloning and expression of chicken skeletal muscle troponin I in
Escherichia coli: the role of rare codons on the expression level.";
Protein Sci. 2:1053-1056(1993).
[2]
PROTEIN SEQUENCE OF 2-183, AND ACETYLATION AT SER-2.
PubMed=624283; DOI=10.1111/j.1432-1033.1978.tb12043.x;
Wilkinson J.M., Grand R.J.A.;
"The amino-acid sequence of chicken fast-skeletal-muscle troponin I.";
Eur. J. Biochem. 82:493-501(1978).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 86-183.
PubMed=3010234; DOI=10.1093/nar/14.8.3377;
Nikovits W. Jr., Kuncio G., Ordahl C.P.;
"The chicken fast skeletal troponin I gene: exon organization and
sequence.";
Nucleic Acids Res. 14:3377-3390(1986).
[4]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 2-182, AND CALCIUM-BINDING
SITES.
PubMed=15784741; DOI=10.1073/pnas.0408882102;
Vinogradova M.V., Stone D.B., Malanina G.G., Karatzaferi C., Cooke R.,
Mendelson R.A., Fletterick R.J.;
"Ca(2+)-regulated structural changes in troponin.";
Proc. Natl. Acad. Sci. U.S.A. 102:5038-5043(2005).
-!- FUNCTION: Troponin I is the inhibitory subunit of troponin, the
thin filament regulatory complex which confers calcium-sensitivity
to striated muscle actomyosin ATPase activity.
-!- SUBUNIT: Binds to actin and tropomyosin.
-!- PTM: The N-terminus is blocked.
-!- SIMILARITY: Belongs to the troponin I family. {ECO:0000305}.
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EMBL; U19926; AAA61952.1; -; mRNA.
EMBL; X03832; CAA27447.1; -; mRNA.
PIR; A24918; TPCHIS.
RefSeq; NP_990748.1; NM_205417.1.
UniGene; Gga.5232; -.
UniGene; Gga.700; -.
PDB; 1VDI; NMR; -; A=132-183.
PDB; 1VDJ; NMR; -; A=132-183.
PDB; 1YTZ; X-ray; 3.00 A; I=2-183.
PDB; 1YV0; X-ray; 7.00 A; I=2-138.
PDB; 2W49; EM; 35.00 A; 2/5/8/Z=4-144.
PDB; 2W4U; EM; 35.00 A; 2/5/8/Z=4-144.
PDBsum; 1VDI; -.
PDBsum; 1VDJ; -.
PDBsum; 1YTZ; -.
PDBsum; 1YV0; -.
PDBsum; 2W49; -.
PDBsum; 2W4U; -.
ProteinModelPortal; P68246; -.
SMR; P68246; -.
IntAct; P68246; 1.
STRING; 9031.ENSGALP00000032067; -.
iPTMnet; P68246; -.
PaxDb; P68246; -.
PRIDE; P68246; -.
GeneID; 396386; -.
KEGG; gga:396386; -.
CTD; 7136; -.
eggNOG; KOG3977; Eukaryota.
eggNOG; ENOG410Y9IX; LUCA.
HOGENOM; HOG000293300; -.
HOVERGEN; HBG052737; -.
InParanoid; P68246; -.
KO; K12043; -.
OrthoDB; EOG091G0NOD; -.
PhylomeDB; P68246; -.
EvolutionaryTrace; P68246; -.
PRO; PR:P68246; -.
Proteomes; UP000000539; Unplaced.
Bgee; ENSGALG00000006591; -.
GO; GO:0005861; C:troponin complex; IBA:GO_Central.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0060048; P:cardiac muscle contraction; IBA:GO_Central.
GO; GO:0003009; P:skeletal muscle contraction; IBA:GO_Central.
InterPro; IPR001978; Troponin.
Pfam; PF00992; Troponin; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Actin-binding; Calcium; Complete proteome;
Direct protein sequencing; Metal-binding; Muscle protein;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:624283}.
CHAIN 2 183 Troponin I, fast skeletal muscle.
/FTId=PRO_0000186147.
CA_BIND 105 116
REGION 2 48 Involved in binding TNC.
REGION 97 117 Involved in binding TNC and actin.
MOD_RES 2 2 N-acetylserine.
{ECO:0000269|PubMed:624283}.
HELIX 8 48 {ECO:0000244|PDB:1YTZ}.
HELIX 58 96 {ECO:0000244|PDB:1YTZ}.
TURN 97 104 {ECO:0000244|PDB:1YTZ}.
HELIX 119 127 {ECO:0000244|PDB:1YTZ}.
HELIX 133 141 {ECO:0000244|PDB:1VDI}.
STRAND 142 153 {ECO:0000244|PDB:1VDI}.
HELIX 159 167 {ECO:0000244|PDB:1VDI}.
HELIX 170 178 {ECO:0000244|PDB:1VDI}.
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


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