ID   A0A3B4T4F8_SERDU        Unreviewed;       185 AA.
AC   A0A3B4T4F8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Troponin I1, slow skeletal type {ECO:0000313|Ensembl:ENSSDUP00000000919.1};
OS   Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000000919.1, ECO:0000313|Proteomes:UP000261420};
RN   [1] {ECO:0000313|Ensembl:ENSSDUP00000000919.1}
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   -!- SIMILARITY: Belongs to the troponin I family.
CC       {ECO:0000256|ARBA:ARBA00009930}.
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DR   AlphaFoldDB; A0A3B4T4F8; -.
DR   STRING; 41447.ENSSDUP00000000919; -.
DR   Ensembl; ENSSDUT00000000964.1; ENSSDUP00000000919.1; ENSSDUG00000000673.1.
DR   GeneTree; ENSGT01030000234588; -.
DR   OMA; KQDFRAN; -.
DR   Proteomes; UP000261420; 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:SF9; 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}.
FT   REGION          28..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   185 AA;  21409 MW;  7D31D201367B9C4A CRC64;
     MPEKRKSKIS ASRKLMLKSL MVAKAKEELE QEMEEKEEEK TKYLEEKSPP IQTRSMSLAE
     LRTLCEELHA KIDVVDEERY DIEAKVLHNT REIKDLNIKV LDLRGKFKRP SLRRVRVSAD
     AILRSLLGSK HKVSLDLRAN LKSVKKEDTE KEKTVEVSDW RKNVEAMSGM EGRKKMFDAA
     KGPSQ
//