ID S4RQ63_PETMA Unreviewed; 254 AA.
AC S4RQ63;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Troponin T type 3a (skeletal, fast) {ECO:0000313|Ensembl:ENSPMAP00000007349.1};
OS Petromyzon marinus (Sea lamprey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX NCBI_TaxID=7757 {ECO:0000313|Ensembl:ENSPMAP00000007349.1, ECO:0000313|Proteomes:UP000245300};
RN [1] {ECO:0000313|Ensembl:ENSPMAP00000007349.1}
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; S4RQ63; -.
DR STRING; 7757.ENSPMAP00000007349; -.
DR Ensembl; ENSPMAT00000007381.1; ENSPMAP00000007349.1; ENSPMAG00000006639.1.
DR GeneTree; ENSGT00940000158477; -.
DR HOGENOM; CLU_076377_1_0_1; -.
DR OMA; SRINEQQ; -.
DR Proteomes; UP000245300; 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:SF20; TROPONIN T2E, CARDIAC ISOFORM X1; 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:UP000245300}.
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..192
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..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 254 AA; 30332 MW; 121F6C0B96C7BB9C CRC64;
MSDTEDVAVE EEEVHEEEAE PETETEPEPE VKAEIVAEEP EEQGEFKTEK PKHKIHVPQP
AAPEGPPELV FDDMHRKRME KDLSELQTLI DAHFETRKKE EEELLLLKER IEKRRQERDE
NIRQRAEKEK ERQLRIAEEK ARREEEDQRK RAEEDSKKRR LLTDASATYG STLSKAERGR
KGKKVTEREK KRKILGERRK ALNIDHLSED KLKEKATELW EWLHGLESEK FDLLERIKRQ
KYDIQSLNRR VDEL
//
