TNNI1_RABIT
ID TNNI1_RABIT Reviewed; 184 AA.
AC P02645;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Troponin I, slow skeletal muscle;
DE AltName: Full=Troponin I, slow-twitch isoform;
GN Name=TNNI1;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT PRO-1.
RX PubMed=588250; DOI=10.1042/bj1670183;
RA Grand R.J.A., Wilkinson J.M.;
RT "The amino acid sequence of rabbit slow-muscle troponin I.";
RL Biochem. J. 167:183-192(1977).
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 -!- SUBUNIT: Binds to actin and tropomyosin.
CC -!- PTM: In the muscle sample, approximately 25% of the chains were
CC blocked. Pro-1 is probably acetylated.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the troponin I family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; A03089; TPRBIW.
DR AlphaFoldDB; P02645; -.
DR SMR; P02645; -.
DR STRING; 9986.ENSOCUP00000008977; -.
DR iPTMnet; P02645; -.
DR eggNOG; KOG3977; Eukaryota.
DR InParanoid; P02645; -.
DR Proteomes; UP000001811; Unplaced.
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; Muscle protein;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..184
FT /note="Troponin I, slow skeletal muscle"
FT /id="PRO_0000186141"
FT REGION 1..45
FT /note="Involved in binding TNC"
FT REGION 94..115
FT /note="Involved in binding TNC and actin"
FT MOD_RES 1
FT /note="N-acetylproline; partial"
FT /evidence="ECO:0000269|PubMed:588250"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUZ5"
FT VARIANT 183..184
FT /note="Missing (in some molecules)"
SQ SEQUENCE 184 AA; 21144 MW; 4CC73E38AC6FD3E9 CRC64;
PEVERKSKIT ASRKLLKSLM LAKAKECQQE HEAREAEKVR YLAERIPALQ TRGLSLSALQ
DLCRQLHAKV EVVDEERYDI EAKCLHNTRE IKDLKLKVLD LRGKFKRPPL RRVRVSADAM
LRALLGSKHK VSMDLRANLK SVKKEDTEKE RPVEVGDWRK NVEAMSGMEG RKKMFDAAKS
PTSQ