ID   TNNI_CHLNI              Reviewed;         292 AA.
AC   Q7M3Y3; O44077; Q9TXE2;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Troponin I;
DE            Short=TnI;
OS   Chlamys nipponensis akazara (Akazara scallop) (Japanese scallop).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Pectinida; Pectinoidea; Pectinidae; Chlamys.
OX   NCBI_TaxID=6571;
RN   [1]
RP   PROTEIN SEQUENCE, AND ACETYLATION AT SER-1.
RX   PubMed=9685719; DOI=10.1093/oxfordjournals.jbchem.a022112;
RA   Tanaka H., Ojima T., Nishita K.;
RT   "Amino acid sequence of troponin-I from Akazara scallop striated adductor
RT   muscle.";
RL   J. Biochem. 124:304-310(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 22-292.
RA   Nishita K., Ojima T., Soejima T.;
RT   "cDNA for Akazara scallop troponin I.";
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 158-292.
RX   PubMed=7775383; DOI=10.1093/oxfordjournals.jbchem.a124703;
RA   Ojima T., Tanaka H., Nishita K.;
RT   "Amino acid sequence of C-terminal 17 kDa CNBr-fragment of Akazara scallop
RT   troponin-I.";
RL   J. Biochem. 117:158-162(1995).
CC   -!- FUNCTION: Troponin I is the inhibitory subunit of troponin, the thin
CC       filament regulatory complex which confers calcium-sensitivity to
CC       striated muscle actomyosin ATPase activity.
CC   -!- SIMILARITY: Belongs to the troponin I family. {ECO:0000305}.
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DR   EMBL; AB009368; BAA23775.1; -; mRNA.
DR   PIR; JE0233; JE0233.
DR   PDB; 3TZ1; X-ray; 1.80 A; B=143-166.
DR   PDBsum; 3TZ1; -.
DR   AlphaFoldDB; Q7M3Y3; -.
DR   SMR; Q7M3Y3; -.
DR   iPTMnet; Q7M3Y3; -.
DR   PRIDE; Q7M3Y3; -.
DR   GO; GO:0005861; C:troponin complex; IEA:InterPro.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   DisProt; DP01367; -.
DR   Gene3D; 1.20.5.350; -; 1.
DR   InterPro; IPR001978; Troponin.
DR   InterPro; IPR038077; Troponin_sf.
DR   Pfam; PF00992; Troponin; 1.
DR   SUPFAM; SSF90250; SSF90250; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Actin-binding; Direct protein sequencing;
KW   Muscle protein.
FT   CHAIN           1..292
FT                   /note="Troponin I"
FT                   /id="PRO_0000186160"
FT   REGION          1..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          237..250
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          255..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..44
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..149
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000305|PubMed:9685719"
FT   CONFLICT        279
FT                   /note="E -> I (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        291
FT                   /note="N -> G (in Ref. 2; BAA23775)"
FT                   /evidence="ECO:0000305"
FT   HELIX           146..164
FT                   /evidence="ECO:0007829|PDB:3TZ1"
SQ   SEQUENCE   292 AA;  34636 MW;  9C869796019A5620 CRC64;
     SSLEERRAAR AARRRKQDEN EGGEEQEETT SRRSRRRQQE DEEDSYSAPA EPAYDAEAEN
     RRRQQQEEEE AAARAAEEEY NRQQEELRRQ RQEEERQRRE EEQRRQQEEE ERLRLEREEQ
     EREEEARRMA EEQKKKKKKG LGGLSPEKKK MLKKLIMQKA AEDLANEAKA KAEAKEKYIN
     DLVPKFSTDG KDVAALQALC KDFHKRLASL EEDVYDWEAK IRKQDFEINE LTLKVNDTKG
     KFVKPVLRKV NKTESKLDKI QRKEAKKSDF RDNLKSSREH EADKEGGEGE NE