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Troponin I, cardiac muscle (Cardiac troponin I)

 TNNI3_RABIT             Reviewed;         211 AA.
P02646;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
13-SEP-2004, sequence version 2.
30-AUG-2017, entry version 79.
RecName: Full=Troponin I, cardiac muscle;
AltName: Full=Cardiac troponin I;
Name=TNNI3;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
PROTEIN SEQUENCE.
PubMed=1008822; DOI=10.1042/bj1590633;
Grand R.J.A., Wilkinson J.M., Mole L.E.;
"The amino acid sequence of rabbit cardiac troponin I.";
Biochem. J. 159:633-641(1976).
[2]
SEQUENCE REVISION.
PubMed=588250; DOI=10.1042/bj1670183;
Grand R.J.A., Wilkinson J.M.;
"The amino acid sequence of rabbit slow-muscle troponin I.";
Biochem. J. 167:183-192(1977).
[3]
PROTEIN SEQUENCE OF 6-36, ACETYLATION AT ALA-1, AND PHOSPHORYLATION AT
SER-22 AND SER-23.
TISSUE=Heart;
PubMed=2226863; DOI=10.1016/0014-5793(90)81046-Q;
Mittmann K., Jaquet K., Heilmeyer L.M.G. Jr.;
"A common motif of two adjacent phosphoserines in bovine, rabbit and
human cardiac troponin I.";
FEBS Lett. 273:41-45(1990).
[4]
PHOSPHORYLATION AT SER-22.
PubMed=958429; DOI=10.1038/262615a0;
Solaro R.J., Moir A.J.G., Perry S.V.;
"Phosphorylation of troponin I and the inotropic effect of adrenaline
in the perfused rabbit heart.";
Nature 262:615-617(1976).
-!- 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: Interacts with TRIM63 (By similarity). Binds to actin and
tropomyosin. Interacts with STK4/MST1 (By similarity).
{ECO:0000250}.
-!- INTERACTION:
Q96RG2:PASK (xeno); NbExp=2; IntAct=EBI-8614386, EBI-1042651;
-!- PTM: Phosphorylated at Ser-22 and Ser-23 by PRKD1; phosphorylation
reduces myofilament calcium sensitivity. Phosphorylated
preferentially at Thr-31. Phosphorylation by STK4/MST1 alters its
binding affinity to TNNC1 (cardiac Tn-C) and TNNT2 (cardiac Tn-T).
Phosphorylated at Ser-42 and Ser-44 by PRKCE; phosphorylation
increases myocardium contractile dysfunction (By similarity). Ser-
22 is one of three sites in the region of residues 1-48 that are
phosphorylated by phosphorylase kinase. {ECO:0000250,
ECO:0000269|PubMed:2226863, ECO:0000269|PubMed:958429}.
-!- SIMILARITY: Belongs to the troponin I family. {ECO:0000305}.
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PIR; A90296; TPRBIC.
ProteinModelPortal; P02646; -.
SMR; P02646; -.
IntAct; P02646; 1.
MINT; MINT-8146737; -.
iPTMnet; P02646; -.
PRIDE; P02646; -.
HOVERGEN; HBG052737; -.
InParanoid; P02646; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0005861; C:troponin complex; IEA:InterPro.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
InterPro; IPR001978; Troponin.
InterPro; IPR021666; Troponin-I_N.
Pfam; PF00992; Troponin; 1.
Pfam; PF11636; Troponin-I_N; 1.
1: Evidence at protein level;
Acetylation; Actin-binding; Calcium; Complete proteome;
Direct protein sequencing; Metal-binding; Muscle protein;
Phosphoprotein; Reference proteome.
CHAIN 1 211 Troponin I, cardiac muscle.
/FTId=PRO_0000186154.
CA_BIND 137 149 {ECO:0000250}.
REGION 32 79 Involved in binding TNC.
REGION 129 150 Involved in binding TNC and actin.
SITE 80 80 Involved in TNI-TNT interactions.
SITE 97 97 Involved in TNI-TNT interactions.
MOD_RES 1 1 N-acetylalanine.
{ECO:0000269|PubMed:2226863}.
MOD_RES 4 4 Phosphoserine.
{ECO:0000250|UniProtKB:P19429}.
MOD_RES 22 22 Phosphoserine; by PHK, PKA and PKD/PRKD1.
{ECO:0000305|PubMed:2226863,
ECO:0000305|PubMed:958429}.
MOD_RES 23 23 Phosphoserine; by PKA and PKD/PRKD1.
{ECO:0000305|PubMed:2226863}.
MOD_RES 26 26 Phosphotyrosine.
{ECO:0000250|UniProtKB:P19429}.
MOD_RES 31 31 Phosphothreonine; by STK4/MST1.
{ECO:0000250|UniProtKB:P19429}.
MOD_RES 42 42 Phosphoserine; by PKC/PRKCE.
{ECO:0000250|UniProtKB:P48787}.
MOD_RES 44 44 Phosphoserine; by PKC/PRKCE.
{ECO:0000250|UniProtKB:P48787}.
MOD_RES 51 51 Phosphothreonine; by STK4/MST1.
{ECO:0000250|UniProtKB:P19429}.
MOD_RES 77 77 Phosphoserine.
{ECO:0000250|UniProtKB:P19429}.
MOD_RES 78 78 Phosphothreonine.
{ECO:0000250|UniProtKB:P19429}.
MOD_RES 129 129 Phosphothreonine; by STK4/MST1.
{ECO:0000250|UniProtKB:P19429}.
MOD_RES 143 143 Phosphothreonine; by STK4/MST1.
{ECO:0000250|UniProtKB:P19429}.
MOD_RES 151 151 Phosphoserine; by PAK3.
{ECO:0000250|UniProtKB:P19429}.
MOD_RES 182 182 Phosphothreonine.
{ECO:0000250|UniProtKB:P19429}.
MOD_RES 200 200 Phosphoserine.
{ECO:0000250|UniProtKB:P19429}.
CONFLICT 17 17 Missing (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 21 26 RSSANY -> SD (in Ref. 1; AA sequence).
{ECO:0000305}.
SEQUENCE 211 AA; 24123 MW; A15B2683C53B2F1C CRC64;
ADESRDAAGE ARPAPAPVRR RSSANYRAYA TEPHAKSKKK ISASRKLQLK TLMLQIAKQE
LEREAEERRG EKGRALSTRC QPLELAGLGF AELQDLCRQL HARVDKVDEE RYDVEAKVTK
NITEIADLTQ KIFDLRGKFK RPTLRLRVRI SADAMMQALL GTRAKETLDL RAHLKQVKKE
DTEKENREVG DWRKNIDLLS GMEGRKKKFE G


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