TNNI3_HORSE
ID TNNI3_HORSE Reviewed; 205 AA.
AC Q5PYI0;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Troponin I, cardiac muscle;
DE AltName: Full=Cardiac troponin I;
GN Name=TNNI3;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=16475519; DOI=10.1177/104063870501700611;
RA Rishniw M., Simpson K.W.;
RT "Cloning and sequencing of equine cardiac troponin I and confirmation of
RT its usefulness as a target analyte for commercial troponin I analyzers.";
RL J. Vet. Diagn. Invest. 17:582-584(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. {ECO:0000250}.
CC -!- SUBUNIT: Binds to actin and tropomyosin. Interacts with TRIM63.
CC Interacts with STK4/MST1 (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated at Ser-17 and Ser-18 by PRKD1; phosphorylation
CC reduces myofilament calcium sensitivity. Phosphorylated preferentially
CC at Thr-26. Phosphorylation by STK4/MST1 alters its binding affinity to
CC TNNC1 (cardiac Tn-C) and TNNT2 (cardiac Tn-T). Phosphorylated at Ser-37
CC and Ser-39 by PRKCE; phosphorylation increases myocardium contractile
CC dysfunction (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the troponin I family. {ECO:0000305}.
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DR EMBL; AY819020; AAV68047.1; -; mRNA.
DR RefSeq; NP_001075373.1; NM_001081904.1.
DR AlphaFoldDB; Q5PYI0; -.
DR SMR; Q5PYI0; -.
DR STRING; 9796.ENSECAP00000045110; -.
DR PaxDb; Q5PYI0; -.
DR GeneID; 100034065; -.
DR KEGG; ecb:100034065; -.
DR CTD; 7137; -.
DR InParanoid; Q5PYI0; -.
DR OrthoDB; 1566919at2759; -.
DR Proteomes; UP000002281; 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:0060048; P:cardiac muscle contraction; IBA:GO_Central.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0003009; P:skeletal muscle contraction; IBA:GO_Central.
DR Gene3D; 1.20.5.350; -; 1.
DR InterPro; IPR001978; Troponin.
DR InterPro; IPR021666; Troponin-I_N.
DR InterPro; IPR038077; Troponin_sf.
DR Pfam; PF00992; Troponin; 1.
DR Pfam; PF11636; Troponin-I_N; 1.
DR SUPFAM; SSF90250; SSF90250; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Actin-binding; Muscle protein; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P08057"
FT CHAIN 2..205
FT /note="Troponin I, cardiac muscle"
FT /id="PRO_0000186152"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 27..74
FT /note="Involved in binding TNC"
FT REGION 124..145
FT /note="Involved in binding TNC and actin"
FT SITE 75
FT /note="Involved in TNI-TNT interactions"
FT /evidence="ECO:0000250"
FT SITE 92
FT /note="Involved in TNI-TNT interactions"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P08057"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 17
FT /note="Phosphoserine; by PKA and PKD/PRKD1"
FT /evidence="ECO:0000250|UniProtKB:P02646"
FT MOD_RES 18
FT /note="Phosphoserine; by PKA and PKD/PRKD1"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 21
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 26
FT /note="Phosphothreonine; by STK4/MST1"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 37
FT /note="Phosphoserine; by PKC/PRKCE"
FT /evidence="ECO:0000250|UniProtKB:P48787"
FT MOD_RES 39
FT /note="Phosphoserine; by PKC/PRKCE"
FT /evidence="ECO:0000250|UniProtKB:P48787"
FT MOD_RES 46
FT /note="Phosphothreonine; by STK4/MST1"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 73
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 138
FT /note="Phosphothreonine; by STK4/MST1"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 145
FT /note="Phosphoserine; by PAK3"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 176
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19429"
SQ SEQUENCE 205 AA; 23483 MW; AF6598E660FE6414 CRC64;
MADQSGNAAP PPVRRRSSAN YRAYATEPHA KKKSKISASR KLQLKTLMLQ IAKQELEREA
VERRGEKGRA LSTRCQPLEL AGLGFEELQD LCRQLHARVD KVDEERYDVE AKVTKNITEI
ADLNQKIFDL RGKFKRPTLR RVRISADAMM QALLGTRAKE TLDLRAHLKQ VKKEDTEKEN
REVGDWRKNI DALSGMEGRK KKFEG
