ID A0A0M4FAR5_DROBS Unreviewed; 374 AA.
AC A0A0M4FAR5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Up {ECO:0000313|EMBL:ALC49545.1};
GN ORFNames=Dbus_chrXg1401 {ECO:0000313|EMBL:ALC49545.1};
OS Drosophila busckii (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC49545.1, ECO:0000313|Proteomes:UP000494163};
RN [1] {ECO:0000313|EMBL:ALC49545.1, ECO:0000313|Proteomes:UP000494163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole larvae {ECO:0000313|EMBL:ALC49545.1};
RA Zhou Q., Bachtrog D.;
RT "Ancestral chromatin configuration constrains chromatin evolution on
RT differentiating sex chromosomes in Drosophila.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the troponin T family.
CC {ECO:0000256|ARBA:ARBA00008330}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP012528; ALC49545.1; -; Genomic_DNA.
DR RefSeq; XP_017851586.1; XM_017996097.1.
DR AlphaFoldDB; A0A0M4FAR5; -.
DR SMR; A0A0M4FAR5; -.
DR STRING; 30019.A0A0M4FAR5; -.
DR GeneID; 108606211; -.
DR OMA; WGRRENE; -.
DR OrthoDB; 2968211at2759; -.
DR Proteomes; UP000494163; Chromosome x sequence.
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:SF1; TROPONIN T, SKELETAL MUSCLE; 1.
DR Pfam; PF00992; Troponin; 1.
DR SUPFAM; SSF90250; Troponin coil-coiled subunits; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000494163}.
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 40..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..374
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 374 AA; 44901 MW; 5252B265150A54C0 CRC64;
MSDDEEYTGE GDPEFIKRQD QKRSDLDEQL KEYISEWRKQ RAKEEDELKK LKEKQAKRKV
TRAEEEQKMA QRKKEEEERR VREAEEKKQR EIEEKRMRLE EAEKKRQAML QAMKDKDKKG
PNFTIAKKET GVLGLSSAAM ERNKTKEQLE EEKKISLSFR IKPLAIEGFG EQKLREKAQE
LWELIVKLET EKYDLEERQK RQDYDLKELK ERQKQQLRHK ALKKGLDPEA LTGKYPPKIQ
VASKYERRVD TRSYDDKKKL FEGGYNTVYA ETLEKAWQER QERFTTRTKS KLPKWFGERP
GKKAGEPETP EGEEDAKADE DIVEDEDEVE EEVAEEEDEE AEEDEEEEEE EEEEEEEEEE
EEEEEEEEEE EEEE
//
