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Database: UniProt
Entry: A0A3B4DD52_PYGNA
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ID   A0A3B4DD52_PYGNA        Unreviewed;       178 AA.
AC   A0A3B4DD52;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Troponin I, fast skeletal muscle {ECO:0000256|ARBA:ARBA00039349};
DE   AltName: Full=Troponin I, fast-twitch isoform {ECO:0000256|ARBA:ARBA00042462};
OS   Pygocentrus nattereri (Red-bellied piranha).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Pygocentrus.
OX   NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000021378.1, ECO:0000313|Proteomes:UP000261440};
RN   [1] {ECO:0000313|Ensembl:ENSPNAP00000021378.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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       {ECO:0000256|ARBA:ARBA00001988}.
CC   -!- SUBUNIT: Binds to actin and tropomyosin.
CC       {ECO:0000256|ARBA:ARBA00038767}.
CC   -!- SIMILARITY: Belongs to the troponin I family.
CC       {ECO:0000256|ARBA:ARBA00009930}.
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DR   RefSeq; XP_017555501.1; XM_017700012.1.
DR   AlphaFoldDB; A0A3B4DD52; -.
DR   STRING; 42514.ENSPNAP00000021378; -.
DR   Ensembl; ENSPNAT00000032627.1; ENSPNAP00000021378.1; ENSPNAG00000006788.1.
DR   GeneID; 108428757; -.
DR   GeneTree; ENSGT01030000234588; -.
DR   OMA; RRCESHA; -.
DR   OrthoDB; 2882372at2759; -.
DR   Proteomes; UP000261440; Unplaced.
DR   GO; GO:0005861; C:troponin complex; IEA:InterPro.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.5.350; -; 1.
DR   Gene3D; 6.10.250.180; -; 1.
DR   InterPro; IPR001978; Troponin.
DR   InterPro; IPR038077; Troponin_sf.
DR   PANTHER; PTHR13738; TROPONIN I; 1.
DR   PANTHER; PTHR13738:SF15; TROPONIN I, FAST SKELETAL MUSCLE; 1.
DR   Pfam; PF00992; Troponin; 1.
DR   SUPFAM; SSF90250; Troponin coil-coiled subunits; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Muscle protein {ECO:0000256|ARBA:ARBA00023179}.
FT   COILED          54..102
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   178 AA;  20427 MW;  ABC497ED0EB640FC CRC64;
     MSEKKMSSSR KHHLKSLMLS IAKGLLEVEA KEKESERTRY MADICPPLSL PGGVQALQEL
     CRELHHKIDV TDEERYDLAS KVDKSSKEIE DLKIKVQDLK GKFKKPALRK VRLSADQMLQ
     ALLGSKHKVS LDLRANLKQV KKEVKEEDKE LRDVGDWRKN IEDKAGMDGR KKMFESEA
//
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