TNNC2_ASTLP
ID TNNC2_ASTLP Reviewed; 150 AA.
AC P06708;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Troponin C, isotype gamma;
OS Astacus leptodactylus (Turkish narrow-clawed crayfish) (Pontastacus
OS leptodactylus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Astacidea;
OC Astacoidea; Astacidae; Astacus.
OX NCBI_TaxID=6717;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RX PubMed=2681191; DOI=10.1016/s0021-9258(19)84704-x;
RA Kobayashi T., Takagi T., Konishi K., Wnuk W.;
RT "Amino acid sequences of the two major isoforms of troponin C from
RT crayfish.";
RL J. Biol. Chem. 264:18247-18259(1989).
RN [2]
RP PROTEIN SEQUENCE.
RA Wnuk W., Schoechlin M., Kobayashi T., Takagi T., Konishi K., Hoar P.E.,
RA Kerrick W.G.L.;
RT "Two isoforms of troponin C from crayfish. Their characterization and a
RT comparison of their primary structure with the tertiary structure of
RT troponin C.";
RL J. Muscle Res. Cell Motil. 7:67-68(1986).
RN [3]
RP CALCIUM-BINDING.
RX PubMed=2808376; DOI=10.1016/s0021-9258(19)84703-8;
RA Wnuk W.;
RT "Resolution and calcium-binding properties of the two major isoforms of
RT troponin C from crayfish.";
RL J. Biol. Chem. 264:18240-18246(1989).
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: There are two different troponin C in crayfish.
CC -!- MISCELLANEOUS: This protein binds two calcium ions.
CC -!- SIMILARITY: Belongs to the troponin C family. {ECO:0000305}.
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DR PIR; B34380; B34380.
DR AlphaFoldDB; P06708; -.
DR SMR; P06708; -.
DR iPTMnet; P06708; -.
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 Acetylation; Calcium; Direct protein sequencing; Metal-binding;
KW Muscle protein; Repeat.
FT CHAIN 1..150
FT /note="Troponin C, isotype gamma"
FT /id="PRO_0000073681"
FT DOMAIN 7..42
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 43..78
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 83..118
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 119..150
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 56
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:2681191"
SQ SEQUENCE 150 AA; 16924 MW; 3826C6B166A10836 CRC64;
MDTLDEEQLS ALKKAFDSFD TDSKGFITPE TVGVILRMMG VKISEKNLQQ VIAETDEDGS
GELEFEEFVE LAAKFLIEED EEALKAELKE AFRIYDKGGD GYITTDVLRE ILRELDNRLT
EDDLDGIIEE VDEDGSGTLD FDEFMEMMSG
