ID   A0A3Q1BTK9_AMPOC        Unreviewed;       187 AA.
AC   A0A3Q1BTK9;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Troponin I, slow skeletal muscle-like {ECO:0000313|Ensembl:ENSAOCP00000018062.1};
OS   Amphiprion ocellaris (Clown anemonefish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000018062.1, ECO:0000313|Proteomes:UP000257160};
RN   [1] {ECO:0000313|Ensembl:ENSAOCP00000018062.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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   -!- SIMILARITY: Belongs to the troponin I family.
CC       {ECO:0000256|ARBA:ARBA00009930}.
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DR   AlphaFoldDB; A0A3Q1BTK9; -.
DR   STRING; 80972.ENSAOCP00000018062; -.
DR   Ensembl; ENSAOCT00000032961.1; ENSAOCP00000018062.1; ENSAOCG00000023215.1.
DR   GeneTree; ENSGT01030000234588; -.
DR   OMA; CIHNTRE; -.
DR   Proteomes; UP000257160; 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:SF41; TROPONIN I, SLOW 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   Muscle protein {ECO:0000256|ARBA:ARBA00023179};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257160}.
FT   REGION          146..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..180
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   187 AA;  21489 MW;  20D0B9DF9DA5E183 CRC64;
     IILSKQRKPK ISASRKLMLK SLMVAKAKEE LEQEILVKEE EKHRYLAERA PPLNTSGLSL
     GQLQDLCREL HAKIDVVDEE RYDIEAKVML NTREIKDLNI KVLDLRGKFK RPNLRRVRVS
     ADAILRSLLG SKHKVSMDLR ANLKSVKKED TEKKRPVEDS DWRKNVEAMS GMEGRKKMFD
     AAKGSAQ
//