ID   TNNC3_BLAGE             Reviewed;         154 AA.
AC   Q1A7B1;
DT   03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Troponin C, isoallergen Bla g 6.0301 {ECO:0000303|PubMed:16751002};
DE   AltName: Allergen=Bla g 6.0301 {ECO:0000303|PubMed:16751002};
OS   Blattella germanica (German cockroach) (Blatta germanica).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blaberoidea; Ectobiidae;
OC   Blattellinae; Blattella.
OX   NCBI_TaxID=6973 {ECO:0000312|EMBL:ABB89298.1};
RN   [1] {ECO:0000312|EMBL:ABB89298.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], 3D-STRUCTURE MODELING, AND ALLERGEN.
RX   PubMed=16751002; DOI=10.1016/j.jaci.2006.02.017;
RA   Hindley J., Wunschmann S., Satinover S.M., Woodfolk J.A., Chew F.T.,
RA   Chapman M.D., Pomes A.;
RT   "Bla g 6: a troponin C allergen from Blattella germanica with IgE binding
RT   calcium dependence.";
RL   J. Allergy Clin. Immunol. 117:1389-1395(2006).
CC   -!- FUNCTION: Troponin is the central regulatory protein of striated muscle
CC       contraction. It consists of three components: Troponin-I (Tn-I) which
CC       is the inhibitor of actomyosin ATPase, Troponin-T (Tn-T) which contains
CC       the binding site for tropomyosin and Troponin-C (Tn-C). The binding of
CC       calcium to Tn-C abolishes the inhibitory action of Tn on actin
CC       filaments. {ECO:0000305}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE in 14% of
CC       the 104 patients tested allergic to cockroach. Calcium depletion by 10
CC       mM ethylene glycol bis(2-aminoethyl)tetraacetic acid (EGTA) does not
CC       significantly affect IgE-binding, but addition of 10 mM CaCl(2) after
CC       calcium depletion increases IgE-binding by approximately 2-fold.
CC       {ECO:0000269|PubMed:16751002}.
CC   -!- SIMILARITY: Belongs to the troponin C family. {ECO:0000305}.
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DR   EMBL; DQ279094; ABB89298.1; -; mRNA.
DR   AlphaFoldDB; Q1A7B1; -.
DR   SMR; Q1A7B1; -.
DR   Allergome; 145; Bla g 6.
DR   Allergome; 2867; Bla g 6.0301.
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..154
FT                   /note="Troponin C, isoallergen Bla g 6.0301"
FT                   /id="PRO_0000447468"
FT   DOMAIN          11..46
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          47..82
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          87..122
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          123..154
FT                   /note="EF-hand 4"
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         66
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         71
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
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         142
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         147
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ   SEQUENCE   154 AA;  17750 MW;  859037F4B0C23449 CRC64;
     MADEQLQLPP EQISVLRKAF DAFDREKSGS ISTNMVEEIL RLMGQPFNRR TLEELIDEVD
     ADKSGRLEFD EFVTLAAKFI IEEDSEAMEK ELREAFRLYD KEGNGYIPTS CLREILRELD
     EQLTSDELDM MIEEIDADGS GTVDFDEFME MMTG