ID   A0A3Q3GZY8_KRYMA        Unreviewed;       290 AA.
AC   A0A3Q3GZY8;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Troponin T, fast skeletal muscle isoforms-like {ECO:0000313|Ensembl:ENSKMAP00000028652.1};
GN   Name=TNNT3 {ECO:0000313|Ensembl:ENSKMAP00000028652.1};
OS   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000028652.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000028652.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Troponin T is the tropomyosin-binding subunit of troponin,
CC       the thin filament regulatory complex which confers calcium-sensitivity
CC       to striated muscle actomyosin ATPase activity.
CC       {ECO:0000256|ARBA:ARBA00003363}.
CC   -!- SIMILARITY: Belongs to the troponin T family.
CC       {ECO:0000256|ARBA:ARBA00008330}.
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DR   AlphaFoldDB; A0A3Q3GZY8; -.
DR   STRING; 37003.ENSKMAP00000028652; -.
DR   Ensembl; ENSKMAT00000029012.1; ENSKMAP00000028652.1; ENSKMAG00000021246.1.
DR   GeneTree; ENSGT00940000158477; -.
DR   OMA; IMTERCK; -.
DR   Proteomes; UP000264800; Unplaced.
DR   GO; GO:0005861; C:troponin complex; IEA:InterPro.
DR   GO; GO:0006937; P:regulation of muscle contraction; IEA:InterPro.
DR   Gene3D; 1.20.5.350; -; 1.
DR   InterPro; IPR027707; TNNT.
DR   InterPro; IPR001978; Troponin.
DR   InterPro; IPR038077; Troponin_sf.
DR   PANTHER; PTHR11521; TROPONIN T; 1.
DR   PANTHER; PTHR11521:SF4; TROPONIN T, FAST SKELETAL MUSCLE; 1.
DR   Pfam; PF00992; Troponin; 2.
DR   SUPFAM; SSF90250; Troponin coil-coiled subunits; 1.
PE   3: Inferred from homology;
KW   Muscle protein {ECO:0000256|ARBA:ARBA00023179};
KW   Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..290
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018668339"
FT   REGION          21..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          138..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..72
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..97
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..183
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..217
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   290 AA;  34459 MW;  0385C0D26B64C352 CRC64;
     FCVVIVPLFF IFCKTEEEEA QEEVVEVEVA PEAEAQVEAE PEVEPEPEPE PEPEPEPEPQ
     EVVHEEEEAY EEEEEKPKFK PSAPKIPDGE KVDFDDIQKK RQNKDLIELQ SLIDAHFECR
     KKEEEELIAL KERIEKRRAE RAEQQRIRAE KDKERQARRE AERMRKEEAD LLRRHDDEAK
     KKIALTNMGS GFTSHLQRID QKRGKKQTER EKKKKVLAER LKPLNVDSLS DDQLREKAKE
     LWEWLQNLEA IKYDHAEKLN RQRYEVISLR NRIDELQKHS KKGAASRRRK
//