ID   TNNI3_COTJA             Reviewed;         208 AA.
AC   P27672;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Troponin I, cardiac muscle;
DE   AltName: Full=Cardiac troponin I;
GN   Name=TNNI3;
OS   Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Perdicinae; Coturnix.
OX   NCBI_TaxID=93934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1918073; DOI=10.1016/s0021-9258(18)55043-2;
RA   Hastings K.E., Koppe R.I., Marmur E., Bader D., Shimada Y., Toyota N.;
RT   "Structure and developmental expression of troponin I isoforms. cDNA clone
RT   analysis of avian cardiac troponin I mRNA.";
RL   J. Biol. Chem. 266:19659-19665(1991).
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.
CC   -!- SIMILARITY: Belongs to the troponin I family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M73702; AAA49513.1; -; mRNA.
DR   AlphaFoldDB; P27672; -.
DR   SMR; P27672; -.
DR   Proteomes; UP000694412; 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   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; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..208
FT                   /note="Troponin I, cardiac muscle"
FT                   /id="PRO_0000186157"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          28..73
FT                   /note="Involved in binding TNC"
FT   REGION          54..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          168..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..73
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        168..201
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   208 AA;  23601 MW;  51AEB9567F220C03 CRC64;
     MAEEEEPKPP PLRRKSSANY RGYAVEPHAK RQSKISASRK LQLKTLLLQR AKRDLEREEQ
     ERAGEKQRHL GELCPPPELD GLGVAQLQEL CRELHARIGR VDEERYDMGT RVSKNMAEME
     ELRLRVAGGR FVRPALRRVR LSADAMMAAL LGSKHRVGTD LRAGLRQVRK DEAEKESREV
     GDWRKNVDAL SGMEGRKKKF EAPGGGQS