TNNI3_CANLF
ID TNNI3_CANLF Reviewed; 211 AA.
AC Q8MKD5;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Troponin I, cardiac muscle;
DE AltName: Full=Cardiac troponin I;
GN Name=TNNI3;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=14719702; DOI=10.2460/ajvr.2004.65.53;
RA Rishniw M., Barr S.C., Simpson K.W., Winand N.J., Wootton J.A.;
RT "Cloning and sequencing of the canine and feline cardiac troponin I
RT genes.";
RL Am. J. Vet. Res. 65:53-58(2004).
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-23 and Ser-24 by PRKD1; phosphorylation
CC reduces myofilament calcium sensitivity. Phosphorylated preferentially
CC at Thr-32. Phosphorylation by STK4/MST1 alters its binding affinity to
CC TNNC1 (cardiac Tn-C) and TNNT2 (cardiac Tn-T). Phosphorylated at Ser-43
CC and Ser-45 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; AF506750; AAM33343.1; -; mRNA.
DR RefSeq; NP_001003041.1; NM_001003041.1.
DR AlphaFoldDB; Q8MKD5; -.
DR SMR; Q8MKD5; -.
DR STRING; 9612.ENSCAFP00000003805; -.
DR iPTMnet; Q8MKD5; -.
DR PaxDb; Q8MKD5; -.
DR Ensembl; ENSCAFT00030000840; ENSCAFP00030000723; ENSCAFG00030000501.
DR Ensembl; ENSCAFT00040014508; ENSCAFP00040012545; ENSCAFG00040007766.
DR GeneID; 403566; -.
DR KEGG; cfa:403566; -.
DR CTD; 7137; -.
DR eggNOG; KOG3977; Eukaryota.
DR HOGENOM; CLU_098686_1_0_1; -.
DR InParanoid; Q8MKD5; -.
DR OMA; CKEIHQK; -.
DR OrthoDB; 1566919at2759; -.
DR TreeFam; TF313374; -.
DR Reactome; R-CFA-390522; Striated Muscle Contraction.
DR Reactome; R-CFA-5578775; Ion homeostasis.
DR Proteomes; UP000002254; Unplaced.
DR Bgee; ENSCAFG00000002618; Expressed in mitral valve and 50 other tissues.
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:0006874; P:cellular calcium ion homeostasis; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0006937; P:regulation of muscle contraction; IEA:Ensembl.
DR GO; GO:0001980; P:regulation of systemic arterial blood pressure by ischemic conditions; IEA:Ensembl.
DR GO; GO:0003009; P:skeletal muscle contraction; IBA:GO_Central.
DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
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..211
FT /note="Troponin I, cardiac muscle"
FT /id="PRO_0000186150"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 33..80
FT /note="Involved in binding TNC"
FT REGION 130..150
FT /note="Involved in binding TNC and actin"
FT SITE 81
FT /note="Involved in TNI-TNT interactions"
FT /evidence="ECO:0000250"
FT SITE 98
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 23
FT /note="Phosphoserine; by PKA and PKD/PRKD1"
FT /evidence="ECO:0000250|UniProtKB:P02646"
FT MOD_RES 24
FT /note="Phosphoserine; by PKA and PKD/PRKD1"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 27
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 32
FT /note="Phosphothreonine; by STK4/MST1"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 43
FT /note="Phosphoserine; by PKC/PRKCE"
FT /evidence="ECO:0000250|UniProtKB:P48787"
FT MOD_RES 45
FT /note="Phosphoserine; by PKC/PRKCE"
FT /evidence="ECO:0000250|UniProtKB:P48787"
FT MOD_RES 52
FT /note="Phosphothreonine; by STK4/MST1"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 79
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 130
FT /note="Phosphothreonine; by STK4/MST1"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 144
FT /note="Phosphothreonine; by STK4/MST1"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 151
FT /note="Phosphoserine; by PAK3"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 182
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19429"
SQ SEQUENCE 211 AA; 23912 MW; E26D1FB56C89F9F3 CRC64;
MADESGDAAG CPPPAPAPIR RQSSANYRAY ATEPHAKKKS KISASRKLQL KTLMLQIAKQ
ELEREAEERR GEKGRALSTR CQPLELAGLG FAELQDLCRQ LHARVDKVDE ERYDVEAKVT
KNITEIADLT QKIFDLRGKF KRPTLRRVRI SADAMMQALL GTRAKESLDL RAHLKQVKKE
DTEKENREVG DWRKNIDALS GMEGRKKKFE G
