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Database: UniProt
Entry: M3ZZ30_XIPMA
LinkDB: M3ZZ30_XIPMA
Original site: M3ZZ30_XIPMA 
ID   M3ZZ30_XIPMA            Unreviewed;       278 AA.
AC   M3ZZ30;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Troponin T, fast skeletal muscle isoforms-like {ECO:0000313|Ensembl:ENSXMAP00000007474.2};
OS   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000007474.2, ECO:0000313|Proteomes:UP000002852};
RN   [1] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [3] {ECO:0000313|Ensembl:ENSXMAP00000007474.2}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000007474.2};
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   RefSeq; XP_005814489.1; XM_005814432.1.
DR   AlphaFoldDB; M3ZZ30; -.
DR   STRING; 8083.ENSXMAP00000007474; -.
DR   Ensembl; ENSXMAT00000007482.2; ENSXMAP00000007474.2; ENSXMAG00000007434.2.
DR   GeneID; 102222819; -.
DR   KEGG; xma:102222819; -.
DR   CTD; 58084; -.
DR   eggNOG; KOG3634; Eukaryota.
DR   GeneTree; ENSGT00940000158477; -.
DR   HOGENOM; CLU_076377_2_0_1; -.
DR   InParanoid; M3ZZ30; -.
DR   OMA; ARPPSDW; -.
DR   OrthoDB; 5362548at2759; -.
DR   Proteomes; UP000002852; Unassembled WGS sequence.
DR   GO; GO:0005861; C:troponin complex; IEA:InterPro.
DR   GO; GO:0006937; P:regulation of muscle contraction; IEA:InterPro.
DR   GO; GO:0045214; P:sarcomere organization; IEA:Ensembl.
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:UP000002852}.
FT   REGION          1..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          125..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..57
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..86
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..170
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        171..185
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..202
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   278 AA;  32627 MW;  AC3BB575B403347F CRC64;
     MSDAEEVEQV EAVEVEVVQE VEVAPEAAPE PEAEPEPEPE PEPEPEPVAE PEPEPVIEPE
     EEKPKFKPSA PKIPDGEKVD FDDIQKKRQN KDLMELQALI DAHFECRKKE EEELIALKER
     IEKRRAERAE QQRVRAEKDK ERQARREEER RIREEADAKK KADEEAKKKS ALSSMGSNYS
     SHLQRADQKR GGKKETEREK KKKILAARRK ALNIDHLSED KLKEKINELN DWMRQLESEK
     FDHMERLKLQ KYEVTRLRKR VEELSKFSKK GAAARRRK
//
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