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Database: UniProt
Entry: A0A3Q7TWI3_VULVU
LinkDB: A0A3Q7TWI3_VULVU
Original site: A0A3Q7TWI3_VULVU 
ID   A0A3Q7TWI3_VULVU        Unreviewed;       250 AA.
AC   A0A3Q7TWI3;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Troponin T, fast skeletal muscle {ECO:0000256|ARBA:ARBA00014961};
GN   Name=TNNT3 {ECO:0000313|RefSeq:XP_025859675.1};
OS   Vulpes vulpes (Red fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX   NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025859675.1};
RN   [1]
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (JAN-2019) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_025859675.1}
RP   IDENTIFICATION.
RC   STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025859675.1};
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_025859675.1};
RG   RefSeq;
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   RefSeq; XP_025859675.1; XM_026003890.1.
DR   AlphaFoldDB; A0A3Q7TWI3; -.
DR   Proteomes; UP000286640; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000286640}.
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          92..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          226..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..53
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..138
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..173
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   250 AA;  29776 MW;  C9B9992DC1844A5F CRC64;
     MSDEEVEQVE EQYEEEEEAQ EEEEVQEEEK PRPRLTAPKI PEGEKVDFDD IQKKRQNKDL
     MELQALIDSH FEARKKEEEE LIALKERIEK RRAERAEQQR IRAEKERERQ NRLAEEKARR
     EEEDAKRRAE DDLKKKKALS SMGANYSSYL AKADQKRGKK QTAREMKKKV LAERRKPLNI
     DHLSEDKLRD KAKELWDTLY QLETDKFEFG EKLKRQKYDI TNLRSRIDQA QKHSKKAGAP
     AKGKVGGRWK
//
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