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TNNI3_XENLA
ID   TNNI3_XENLA             Reviewed;         244 AA.
AC   P50754;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Troponin I, cardiac muscle;
DE            Short=Troponin IC;
GN   Name=tnni3;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Heart muscle;
RX   PubMed=7958411; DOI=10.1006/dbio.1994.1265;
RA   Drysdale T.A., Tonissen K.F., Patterson K.D., Crawford M.J., Krieg P.A.;
RT   "Cardiac troponin I is a heart-specific marker in the Xenopus embryo:
RT   expression during abnormal heart morphogenesis.";
RL   Dev. Biol. 165:432-441(1994).
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   -!- TISSUE SPECIFICITY: Heart.
CC   -!- DEVELOPMENTAL STAGE: Expressed at all stages of development.
CC   -!- SIMILARITY: Belongs to the troponin I family. {ECO:0000305}.
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DR   EMBL; L25721; AAA65727.1; -; mRNA.
DR   PIR; I51408; I51408.
DR   RefSeq; NP_001081378.1; NM_001087909.2.
DR   AlphaFoldDB; P50754; -.
DR   SMR; P50754; -.
DR   PRIDE; P50754; -.
DR   GeneID; 397803; -.
DR   KEGG; xla:397803; -.
DR   CTD; 397803; -.
DR   Xenbase; XB-GENE-17334604; tnni3.S.
DR   OrthoDB; 1566919at2759; -.
DR   Proteomes; UP000186698; Chromosome 7S.
DR   Bgee; 397803; Expressed in heart and 10 other tissues.
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   2: Evidence at transcript level;
KW   Acetylation; Actin-binding; Muscle protein; Phosphoprotein;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..244
FT                   /note="Troponin I, cardiac muscle"
FT                   /id="PRO_0000186158"
FT   REGION          1..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..42
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   244 AA;  28198 MW;  57CC019518202F65 CRC64;
     MSDEEEVTYE EEEEEYVEEE EEEVVAPEPP KPAPPPAAPP PLIRRRSSAN YRSYATEPQV
     KRKPKISASR KLQLNTMMLQ IAKAEMEREE EERAREKERY LAEHCQPLQL SGLSRSELQD
     LCQELHARID VVDEERYDME AKVNKNITEL EDLNQKIFDL RGKFKKPNLR RVRLSADAMM
     MALLGTKHKV SMDLRANLKQ VKQTKKDDAD KDIREVGDWR KNVDALSGME GRKKKFESTG
     AAAV
 
 
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