ID A0A3B3SZC2_9TELE Unreviewed; 294 AA.
AC A0A3B3SZC2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Troponin T type 3b (skeletal, fast) {ECO:0000313|Ensembl:ENSPKIP00000035598.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000035598.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000035598.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A3B3SZC2; -.
DR Ensembl; ENSPKIT00000016530.1; ENSPKIP00000035598.1; ENSPKIG00000014475.1.
DR GeneTree; ENSGT00940000158477; -.
DR Proteomes; UP000261540; 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; 1.
DR SUPFAM; SSF90250; Troponin coil-coiled subunits; 1.
PE 3: Inferred from homology;
KW Muscle protein {ECO:0000256|ARBA:ARBA00023179}.
FT REGION 33..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..52
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..68
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 294 AA; 34377 MW; AF86575FF55B404F CRC64;
LFLSPLTYLS DPPTLRSLGA CRIAVAEEVV EVEVAPEVAP EPEPEPEVAP EPEPEPVQEV
APEPEPEPQP VEEVQEEEKP KFKPSAPRIP EGDKVDFDDI QKKRQNKDLI ELQALIDAHF
EHRKKEEEEI IALKERIEKR RAERSEQQRI RAEKDKERQA RREEERLKRE EADAKKRADE
DAKKKSALAN MGSQYSSYLQ KADSKRGGKK QTEREKKKKI LADRRKALNV DHLNEDKLRE
KAKELWDWMH SLESEKFDHL EKLKKQKYEV TTLRNRIDEL QKHSKKGAAA RRRK
//