ID   TNNI_ASTLP              Reviewed;         201 AA.
AC   P05547;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Troponin I;
DE            Short=TnI;
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, ACETYLATION AT ALA-1, AND METHYLATION AT LYS-142 AND
RP   LYS-146.
RX   PubMed=2912973; DOI=10.1016/s0021-9258(18)94222-5;
RA   Kobayashi T., Takagi T., Konishi K., Cox J.A.;
RT   "Amino acid sequence of crayfish troponin I.";
RL   J. Biol. Chem. 264:1551-1557(1989).
CC   -!- FUNCTION: Troponin I is the actomyosin ATPase inhibitory subunit
CC       present in the thin filament regulatory complex.
CC   -!- MISCELLANEOUS: There is a 30 residue long N-terminal tail that does not
CC       occur in skeletal muscle TnI's, but is present in cardiac muscle TnI's.
CC   -!- SIMILARITY: Belongs to the troponin I family. {ECO:0000305}.
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DR   AlphaFoldDB; P05547; -.
DR   SMR; P05547; -.
DR   Allergome; 6097; Pon l 7.
DR   Allergome; 6098; Pon l 7.0101.
DR   iPTMnet; P05547; -.
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   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   Acetylation; Actin-binding; Direct protein sequencing; Methylation.
FT   CHAIN           1..201
FT                   /note="Troponin I"
FT                   /id="PRO_0000186161"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          108..117
FT                   /note="Troponin T-interaction"
FT   REGION          135..148
FT                   /note="Actin-binding"
FT   REGION          182..201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..39
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000305|PubMed:2912973"
FT   MOD_RES         142
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000269|PubMed:2912973"
FT   MOD_RES         146
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000269|PubMed:2912973"
SQ   SEQUENCE   201 AA;  23490 MW;  47585EB56DB88A65 CRC64;
     ADKAKAAEEA KKKQDDIDRK KAEVRKRLEE QSLKKQKKGF MTPERKKKLR LLLRKKAAEE
     LKKEQERKAG ERRKIIDQRC GQPKNLDGAN EEQLRAIIKE YFDHTAQIES DKYDVELEII
     RKDYEINELN IQVNDLRGKF IKPTLKKVSK YENKFAKLQK KAAEFNFRNQ LKTVKKKEFE
     LEDDKGATEG DGPAAEEVAA E