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Database: UniProt
Entry: A0A401SSA5_CHIPU
LinkDB: A0A401SSA5_CHIPU
Original site: A0A401SSA5_CHIPU 
ID   A0A401SSA5_CHIPU        Unreviewed;       234 AA.
AC   A0A401SSA5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:GCC33287.1};
DE   Flags: Fragment;
GN   ORFNames=chiPu_0011756 {ECO:0000313|EMBL:GCC33287.1};
OS   Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC   Chiloscyllium.
OX   NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC33287.1, ECO:0000313|Proteomes:UP000287033};
RN   [1] {ECO:0000313|EMBL:GCC33287.1, ECO:0000313|Proteomes:UP000287033}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA   Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA   Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA   Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA   Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT   "Shark genomes provide insights into elasmobranch evolution and the origin
RT   of vertebrates.";
RL   Nat. Ecol. Evol. 2:1761-1771(2018).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GCC33287.1}.
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DR   EMBL; BEZZ01000503; GCC33287.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401SSA5; -.
DR   STRING; 137246.A0A401SSA5; -.
DR   OMA; VEEEVQF; -.
DR   Proteomes; UP000287033; Unassembled WGS 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; 2.
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:UP000287033}.
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          72..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          136..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..168
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:GCC33287.1"
SQ   SEQUENCE   234 AA;  28022 MW;  14589E7C542376D1 CRC64;
     QPILEEETKP KPKLFVPSHA PKMPDGEKVD FDDIQRKRME KDLLELQTLI EAHFERRKKE
     EEDLVALKER IEKRRAERSE QQRIRAEKEK ERLNRAAEEK ARKEEEELRK KAEEDMKKKK
     VLSNMALHYG GYLQKTEIRR SGRKQTEREK KKKILADRRK PLNTENLNEQ KLKEKAQELA
     DWLQQLEGEK FDLCEKLKRQ KYEINLLQIR VHEQMGKFST KAARGKGKVG GRWK
//
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