TNNI2_RABIT
ID TNNI2_RABIT Reviewed; 182 AA.
AC P02643;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Troponin I, fast skeletal muscle;
DE AltName: Full=Troponin I, fast-twitch isoform;
GN Name=TNNI2;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=1339446; DOI=10.1016/s0021-9258(19)74056-3;
RA Sheng Z., Pan B.S., Miller T., Potter J.D.;
RT "Isolation, expression, and mutation of a rabbit skeletal muscle cDNA clone
RT for troponin I. The role of the NH2 terminus of fast skeletal muscle
RT troponin I in its biological activity.";
RL J. Biol. Chem. 267:25407-25413(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Muscle;
RX PubMed=8173075; DOI=10.3109/10425179309020150;
RA Wu Q.L., Raychowdhury M.K., Du Y., Jha P.K., Leavis P.C., Sarkar S.;
RT "Characterization of a rabbit fast skeletal troponin I cDNA: a comparative
RT sequence analysis of vertebrate isoforms and tissue-specific expression of
RT a single copy gene.";
RL DNA Seq. 4:113-121(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8495752; DOI=10.1016/0014-5793(93)81453-7;
RA Kluwe L., Maeda K., Maeda Y.;
RT "E. coli expression and characterization of a mutant troponin I with the
RT three cysteine residues substituted.";
RL FEBS Lett. 323:83-88(1993).
RN [4]
RP PROTEIN SEQUENCE OF 2-182, AND ACETYLATION AT GLY-2.
RC TISSUE=Skeletal muscle;
RX PubMed=1180911; DOI=10.1042/bj1490493;
RA Wilkinson J.M., Grand R.J.A.;
RT "The amino acid sequence of troponin I from rabbit skeletal muscle.";
RL Biochem. J. 149:493-496(1975).
RN [5]
RP SEQUENCE REVISION.
RX PubMed=146828; DOI=10.1038/271031a0;
RA Wilkinson J.M., Grand R.J.A.;
RT "Comparison of amino acid sequence of troponin I from different striated
RT muscles.";
RL Nature 271:31-35(1978).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-25 AND 166-178.
RX PubMed=6687628; DOI=10.1038/302718a0;
RA Putney S.D., Herlihy W.C., Schimmel P.R.;
RT "A new troponin T and cDNA clones for 13 different muscle proteins, found
RT by shotgun sequencing.";
RL Nature 302:718-721(1983).
RN [7]
RP PHOSPHORYLATION AT THR-12 AND SER-118.
RC TISSUE=Skeletal muscle;
RX PubMed=4369337; DOI=10.1016/0014-5793(74)80739-8;
RA Moir A.J.G., Wilkinson J.M., Perry S.V.;
RT "The phosphorylation sites of troponin I from white skeletal muscle of the
RT rabbit.";
RL FEBS Lett. 42:253-256(1974).
RN [8]
RP PHOSPHORYLATION AT THR-12 AND SER-118.
RC TISSUE=Skeletal muscle;
RX PubMed=4369265; DOI=10.1016/0014-5793(74)80738-6;
RA Huang T.S., Bylund D.B., Stull J.T., Krebs E.G.;
RT "The amino acid sequences of the phosphorylated sites in troponin-I from
RT rabbit skeletal muscle.";
RL FEBS Lett. 42:249-252(1974).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-48 IN COMPLEX WITH TNC.
RX PubMed=9560191; DOI=10.1073/pnas.95.9.4847;
RA Vassylyev D.G., Takeda S., Wakatsuki S., Maeda K., Maeda Y.;
RT "Crystal structure of troponin C in complex with troponin I fragment at
RT 2.3-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:4847-4852(1998).
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. {ECO:0000269|PubMed:9560191}.
CC -!- SIMILARITY: Belongs to the troponin I family. {ECO:0000305}.
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DR EMBL; L04347; AAA31490.1; -; mRNA.
DR EMBL; X14190; CAA32392.1; -; mRNA.
DR EMBL; S61403; AAB26824.1; -; mRNA.
DR EMBL; V00897; CAA24262.1; -; mRNA.
DR EMBL; V00898; CAA24263.1; -; mRNA.
DR PIR; A45060; TPRBIS.
DR PIR; I46513; I46513.
DR RefSeq; NP_001076252.1; NM_001082783.1.
DR PDB; 1A2X; X-ray; 2.30 A; B=2-48.
DR PDB; 1NPQ; NMR; -; B=116-132.
DR PDBsum; 1A2X; -.
DR PDBsum; 1NPQ; -.
DR AlphaFoldDB; P02643; -.
DR BMRB; P02643; -.
DR SMR; P02643; -.
DR BioGRID; 1172600; 5.
DR CORUM; P02643; -.
DR IntAct; P02643; 2.
DR iPTMnet; P02643; -.
DR GeneID; 100009581; -.
DR KEGG; ocu:100009581; -.
DR CTD; 7136; -.
DR InParanoid; P02643; -.
DR EvolutionaryTrace; P02643; -.
DR Proteomes; UP000001811; 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 GO; GO:0031014; F:troponin T binding; IPI:UniProtKB.
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; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1180911"
FT CHAIN 2..182
FT /note="Troponin I, fast skeletal muscle"
FT /id="PRO_0000186145"
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-acetylglycine"
FT /evidence="ECO:0000269|PubMed:1180911"
FT MOD_RES 12
FT /note="Phosphothreonine; by PHK"
FT /evidence="ECO:0000269|PubMed:4369265,
FT ECO:0000269|PubMed:4369337"
FT MOD_RES 118
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:4369265,
FT ECO:0000269|PubMed:4369337"
FT CONFLICT 154..156
FT /note="Missing (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 6..32
FT /evidence="ECO:0007829|PDB:1A2X"
FT HELIX 120..126
FT /evidence="ECO:0007829|PDB:1NPQ"
SQ SEQUENCE 182 AA; 21214 MW; 5BE12DBB6C90FFCF CRC64;
MGDEEKRNRA ITARRQHLKS VMLQIAATEL EKEEGRREAE KQNYLAEHCP PLSLPGSMAE
VQELCKQLHA KIDAAEEEKY DMEIKVQKSS KELEDMNQKL FDLRGKFKRP PLRRVRMSAD
AMLKALLGSK HKVCMDLRAN LKQVKKEDTE KERDLRDVGD WRKNIEEKSG MEGRKKMFES
ES
