ID A0A091P2Q4_9PASS Unreviewed; 158 AA.
AC A0A091P2Q4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Troponin C, slow skeletal and cardiac muscles {ECO:0000256|ARBA:ARBA00044185};
DE Flags: Fragment;
GN ORFNames=N310_12784 {ECO:0000313|EMBL:KFP85840.1};
OS Acanthisitta chloris (rifleman).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Acanthisittidae;
OC Acanthisitta.
OX NCBI_TaxID=57068 {ECO:0000313|EMBL:KFP85840.1, ECO:0000313|Proteomes:UP000053537};
RN [1] {ECO:0000313|EMBL:KFP85840.1, ECO:0000313|Proteomes:UP000053537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP85840.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Troponin is the central regulatory protein of striated muscle
CC contraction. Tn consists of three components: Tn-I which is the
CC inhibitor of actomyosin ATPase, Tn-T which contains the binding site
CC for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the
CC inhibitory action of Tn on actin filaments.
CC {ECO:0000256|ARBA:ARBA00037722}.
CC -!- SIMILARITY: Belongs to the troponin C family.
CC {ECO:0000256|ARBA:ARBA00038202}.
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DR EMBL; KK843918; KFP85840.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091P2Q4; -.
DR Proteomes; UP000053537; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; ISS:AgBase.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:UniProt.
DR CDD; cd00051; EFh; 2.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR23048; MYOSIN LIGHT CHAIN 1, 3; 1.
DR PANTHER; PTHR23048:SF48; TROPONIN C1, SLOW SKELETAL AND CARDIAC TYPE; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR PRINTS; PR00450; RECOVERIN.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF47473; EF-hand; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Muscle protein {ECO:0000256|ARBA:ARBA00023179};
KW Reference proteome {ECO:0000313|Proteomes:UP000053537}.
FT DOMAIN 49..84
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 89..124
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 125..158
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP85840.1"
FT NON_TER 158
FT /evidence="ECO:0000313|EMBL:KFP85840.1"
SQ SEQUENCE 158 AA; 18097 MW; FE92E98E66C19DF8 CRC64;
VFSLQVEQLT EEQKNEFKAA FDIFVLGAED GCISTKELGK VMRMLGQNPT PEELQEMIDE
VDEDGSGTVD FDEFLVMMVR CMKDDSKGKT EEELSDLFRM FDKNADGYID LEELKIMLQA
TGETITEDDI EELMKDGDKN NDGRIDYDEF LEFMKGVE
//