TNNI2_COTJA
ID TNNI2_COTJA Reviewed; 183 AA.
AC P68247; P02644;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Troponin I, fast skeletal muscle;
DE AltName: Full=Troponin I, fast-twitch isoform;
GN Name=TNNI2;
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 [GENOMIC DNA].
RX PubMed=3865218; DOI=10.1073/pnas.82.23.8080;
RA Baldwin A.S. Jr., Kittler E.L.W., Emerson C.P. Jr.;
RT "Structure, evolution, and regulation of a fast skeletal muscle troponin I
RT gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:8080-8084(1985).
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 -!- PTM: The N-terminus is blocked.
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; M12132; AAB00122.1; -; Genomic_DNA.
DR PIR; A23569; A23569.
DR AlphaFoldDB; P68247; -.
DR BMRB; P68247; -.
DR SMR; P68247; -.
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; IPR038077; Troponin_sf.
DR Pfam; PF00992; Troponin; 1.
DR SUPFAM; SSF90250; SSF90250; 1.
PE 3: Inferred from homology;
KW Acetylation; Actin-binding; Muscle protein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..183
FT /note="Troponin I, fast skeletal muscle"
FT /id="PRO_0000186148"
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-acetylserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 183 AA; 21234 MW; E33F7517E84BB09E CRC64;
MSDEEKKRRA ATARRQHLKS AMLQLAVTEI EKEAAAKEVE KQNYLAEHCP PLSLPGSMQE
LQELCKKLHA KIDSVDEERY DTEVKLQKTN KELEDLSQKL FDLRGKFKRP PLRRVRMSAD
AMLRALLGSK HKVNMDLRAN LKQVKKEDTE KEKDLRDVGD WRKNIEEKSG MEGRKKMFEA
GES