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TNNC1_COTJA
ID   TNNC1_COTJA             Reviewed;         161 AA.
AC   P05936;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Troponin C, slow skeletal and cardiac muscles;
DE            Short=TN-C;
GN   Name=TNNC1;
OS   Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Perdicinae; Coturnix.
OX   NCBI_TaxID=93934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pectoralis muscle;
RX   PubMed=3587028; DOI=10.1016/0076-6879(87)39096-2;
RA   Maisonpierre P.C., Hastings K.E.M., Emerson C.P. Jr.;
RT   "The cloning and the codon and amino acid sequence of the quail
RT   slow/cardiac troponin C cDNA.";
RL   Methods Enzymol. 139:326-337(1987).
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   -!- MISCELLANEOUS: Cardiac muscle Tn-C can bind 3 calcium ions per
CC       molecule. Domain I does not bind calcium.
CC   -!- SIMILARITY: Belongs to the troponin C family. {ECO:0000305}.
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DR   EMBL; M29722; AAA49502.1; -; mRNA.
DR   AlphaFoldDB; P05936; -.
DR   BMRB; P05936; -.
DR   SMR; P05936; -.
DR   Proteomes; UP000694412; Unplaced.
DR   GO; GO:0005509; F:calcium ion binding; ISS:AgBase.
DR   CDD; cd00051; EFh; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   Pfam; PF13833; EF-hand_8; 1.
DR   SMART; SM00054; EFh; 4.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 4.
PE   2: Evidence at transcript level;
KW   Acetylation; Calcium; Metal-binding; Muscle protein; Reference proteome;
KW   Repeat.
FT   CHAIN           1..161
FT                   /note="Troponin C, slow skeletal and cardiac muscles"
FT                   /id="PRO_0000073702"
FT   DOMAIN          16..51
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          52..87
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          92..127
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          128..161
FT                   /note="EF-hand 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         65
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         67
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         69
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         71
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         105
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         107
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         109
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         111
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         116
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         143
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000305"
FT   BINDING         145
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000305"
FT   BINDING         147
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000305"
FT   BINDING         152
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        56
FT                   /note="Missing (in Ref. 1; AAA49502)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   161 AA;  18428 MW;  E33FA912DC600F9D CRC64;
     MDDIYKAAVE QLTEEQKNEF KAAFDIFVLG AEDGCISTKE LGKVMRMLGQ NPTPEELQEM
     IDEVDEDGSG TVDFDQFLVM MVRCMKDDSK GKTEEELSDL FRMFDKNADG YIDLEELKIM
     LQATGETITE DDIEELMKDG NKNNDGRIDY DEFLQFMKGV E
 
 
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