ID A0A1S3GPX2_DIPOR Unreviewed; 253 AA.
AC A0A1S3GPX2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Troponin T, slow skeletal muscle {ECO:0000256|ARBA:ARBA00040072};
DE AltName: Full=Slow skeletal muscle troponin T {ECO:0000256|ARBA:ARBA00043016};
GN Name=Tnnt1 {ECO:0000313|RefSeq:XP_012890022.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012890022.1};
RN [1] {ECO:0000313|RefSeq:XP_012890022.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012890022.1};
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 -!- SUBUNIT: Interacts with TPM3. {ECO:0000256|ARBA:ARBA00044035}.
CC -!- SIMILARITY: Belongs to the troponin T family.
CC {ECO:0000256|ARBA:ARBA00008330}.
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DR RefSeq; XP_012890022.1; XM_013034568.1.
DR AlphaFoldDB; A0A1S3GPX2; -.
DR GeneID; 105999532; -.
DR CTD; 7138; -.
DR OrthoDB; 5362548at2759; -.
DR Proteomes; UP000081671; 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:SF6; TROPONIN T, SLOW SKELETAL MUSCLE; 1.
DR Pfam; PF00992; Troponin; 2.
DR SUPFAM; SSF90250; Troponin coil-coiled subunits; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Muscle protein {ECO:0000256|ARBA:ARBA00023179};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671}.
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 191..225
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..18
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 253 AA; 30216 MW; E4C92611FA029DFE CRC64;
MSDLEDQDYE EEQVEAPEVP EPAAEREEER PKPSRPVVPP LIPPKIPEGE RVDFDDIHRK
RMEKDLLELQ TLIDVHFEQR KKEEEELIAL KDRIERRRAE RAEQQRFRTE KERERQAKLA
EEKMRKEEEE AKKRAEDDAK KKKVLSNMGA HFGGYLVKAE QKRGKRQTGR ETKLRILSER
KKPLNIEYLG EDQLREKAQE LLDWIHQLES EKFDLMEKLK QQKYEINVLY NRISHAQKFR
KGAGKGRVGG RWK
//
