ID A0A2K5WPF7_MACFA Unreviewed; 406 AA.
AC A0A2K5WPF7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Troponin T, fast skeletal muscle {ECO:0000256|ARBA:ARBA00014961};
GN Name=TNNT3 {ECO:0000313|Ensembl:ENSMFAP00000039015.2};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000039015.2, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000039015.2, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000039015.2}
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; A0A2K5WPF7; -.
DR Ensembl; ENSMFAT00000013275.2; ENSMFAP00000039015.2; ENSMFAG00000038686.2.
DR VEuPathDB; HostDB:ENSMFAG00000038686; -.
DR GeneTree; ENSGT00940000158477; -.
DR OrthoDB; 5362548at2759; -.
DR Proteomes; UP000233100; Chromosome 14.
DR Bgee; ENSMFAG00000038686; Expressed in skeletal muscle tissue and 6 other cell types or tissues.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000233100}.
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..284
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 406 AA; 45989 MW; C040A2F5962FA1A1 CRC64;
MSDEEVEQVE EQYEEEEEAQ EEEEKPRPKL TAPKIPEGEK VDFDDIQKKR QNKDLMELQA
LIDSHFEARK KEEEELVALK ERIEKRRAER AEQQRIRAEK ERERQNRLAE EKARREEEDA
KRRAEDDLKK KKALSSMGAN YSSYLAKADQ KRGKKQTARE MKKKILAERR KPLNIDHLSE
DKLRDKAKEL WETLHQLETD KFEFGEKLKR QKYDIMNVRA RVQMLAKLSP RSEAASTRPR
STARRLGPQP RAKSAGAGSR EDRKAPRGRD PPPSCPPGPP VGLHILRPPQ SCQGLPDNPG
GEEAIPGHPP HLCPCCLYPL GPVNKAADPL PQCVLASAWG ALGDTGGMWV GASQGHSILA
IRGASSGGHW PARTTCYYGQ GGAWMPIRCC PWLFPLKRGP HPRPSL
//
