ID   TNNC_TYRPU              Reviewed;         153 AA.
AC   D2DGW3;
DT   05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Troponin C {ECO:0000303|PubMed:19786801, ECO:0000312|EMBL:ACL36923.1};
DE   AltName: Full=Allergen Tyr p 24 {ECO:0000303|PubMed:19786801};
DE   AltName: Allergen=Tyr p 24.0101 {ECO:0000305};
OS   Tyrophagus putrescentiae (Mold mite) (Acarus putrescentiae).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Sarcoptiformes; Astigmata; Acaroidea; Acaridae; Tyrophaginae;
OC   Tyrophagus.
OX   NCBI_TaxID=59818 {ECO:0000312|EMBL:ACL36923.1};
RN   [1] {ECO:0000312|EMBL:ACL36923.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGEN.
RX   PubMed=19786801; DOI=10.1159/000242358;
RA   Jeong K.Y., Kim C.R., Un S., Yi M.H., Lee I.Y., Park J.W., Hong C.S.,
RA   Yong T.S.;
RT   "Allergenicity of recombinant troponin C from Tyrophagus putrescentiae.";
RL   Int. Arch. Allergy Immunol. 151:207-213(2010).
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. {ECO:0000305}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE in 11% of
CC       the 46 patients tested allergic to storage mite T.putrescentiae. IgE
CC       reactivity is calcium-dependent. Addition of 10 mM CaCl(2) increases
CC       the intensity of IgE-binding approximately 2-fold in 4 sera out of 5
CC       tested. {ECO:0000269|PubMed:19786801}.
CC   -!- SIMILARITY: Belongs to the troponin C family. {ECO:0000305}.
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DR   EMBL; FJ534553; ACL36923.1; -; mRNA.
DR   AlphaFoldDB; D2DGW3; -.
DR   SMR; D2DGW3; -.
DR   Allergome; 6136; Tyr p 24.
DR   Allergome; 6137; Tyr p 24.0101.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; 2.
DR   SMART; SM00054; EFh; 4.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 4.
PE   1: Evidence at protein level;
KW   Allergen; Calcium; Metal-binding; Muscle protein; Repeat.
FT   CHAIN           1..153
FT                   /note="Troponin C"
FT                   /id="PRO_0000447338"
FT   DOMAIN          9..44
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          45..80
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          85..120
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          121..153
FT                   /note="EF-hand 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         58
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         60
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         62
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         64
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         69
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         134
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         136
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         138
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         140
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         145
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ   SEQUENCE   153 AA;  17692 MW;  BA416935C8E913C6 CRC64;
     MSVEELSKEQ VQMLRKAFDM FDRDKKGYIH TNMVSTILRT LGQTFEENDL QQLIIEIDAD
     GSGELEFDEF LTLTARFLVE EDTEAMQEEL REAFRMYDKE GNGYIPTSAL REILRALDDK
     LTEDELDEMI AEIDTDGSGT VDFDEFMEMM TGD