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Database: UniProt
Entry: A0A3Q2UXE3_HAPBU
LinkDB: A0A3Q2UXE3_HAPBU
Original site: A0A3Q2UXE3_HAPBU 
ID   A0A3Q2UXE3_HAPBU        Unreviewed;       276 AA.
AC   A0A3Q2UXE3;
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 T3, fast skeletal type {ECO:0000313|Ensembl:ENSHBUP00000002657.1};
OS   Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX   NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000002657.1, ECO:0000313|Proteomes:UP000264840};
RN   [1] {ECO:0000313|Ensembl:ENSHBUP00000002657.1}
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; A0A3Q2UXE3; -.
DR   STRING; 8153.ENSHBUP00000002657; -.
DR   Ensembl; ENSHBUT00000011714.1; ENSHBUP00000002657.1; ENSHBUG00000003866.1.
DR   GeneTree; ENSGT00940000158477; -.
DR   OMA; EEXLTAP; -.
DR   Proteomes; UP000264840; Unplaced.
DR   GO; GO:0005861; C:troponin complex; IEA:InterPro.
DR   GO; GO:0006937; P:regulation of muscle contraction; IEA:InterPro.
DR   GO; GO:0045214; P:sarcomere organization; IEA:Ensembl.
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; 1.
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:UP000264840}.
FT   REGION          16..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          125..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..58
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..83
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..169
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..184
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        185..202
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   276 AA;  32480 MW;  BF4B8551D1A8710C CRC64;
     LAACCVAVEE EVVVEVEVAP EAAPEPEPEP QPEPEPEPEP VVEPEPEPEP EPEDPTEEEE
     EKPKFKPTAP KIPDGEKVDF DDIQKKRQNK DLIELQALID AHFEHRKKEE EELIALKERI
     EKRRAERAEQ QRVRAEKEKE RQARREEERR IREEADAKKK ADDDAKKKSA LSSMGSQYSS
     HLQRADQKRG GKKETEREKK KKILAARRKQ LNIDHLNEDK LKEKIKELHD WMTQLESEKF
     DHTERLKRQK YEVTTLRKRI EELSKFSKKG AARRRK
//
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