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Database: UniProt
Entry: A0A2K5Z5T1_MANLE
LinkDB: A0A2K5Z5T1_MANLE
Original site: A0A2K5Z5T1_MANLE 
ID   A0A2K5Z5T1_MANLE        Unreviewed;       209 AA.
AC   A0A2K5Z5T1;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Troponin I, cardiac muscle {ECO:0000256|ARBA:ARBA00018910};
DE   AltName: Full=Cardiac troponin I {ECO:0000256|ARBA:ARBA00030764};
GN   Name=TNNI3 {ECO:0000313|Ensembl:ENSMLEP00000023189.1};
OS   Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Mandrillus.
OX   NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000023189.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000023189.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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       {ECO:0000256|ARBA:ARBA00001988}.
CC   -!- SIMILARITY: Belongs to the troponin I family.
CC       {ECO:0000256|ARBA:ARBA00009930}.
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DR   AlphaFoldDB; A0A2K5Z5T1; -.
DR   Ensembl; ENSMLET00000046703.1; ENSMLEP00000023189.1; ENSMLEG00000035806.1.
DR   GeneTree; ENSGT01030000234588; -.
DR   OMA; MLQVAKH; -.
DR   Proteomes; UP000233140; Unplaced.
DR   GO; GO:0005861; C:troponin complex; IEA:InterPro.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.5.350; -; 1.
DR   Gene3D; 6.10.250.180; -; 1.
DR   InterPro; IPR001978; Troponin.
DR   InterPro; IPR021666; Troponin-I_N.
DR   InterPro; IPR038077; Troponin_sf.
DR   PANTHER; PTHR13738; TROPONIN I; 1.
DR   PANTHER; PTHR13738:SF2; TROPONIN I, CARDIAC MUSCLE; 1.
DR   Pfam; PF00992; Troponin; 1.
DR   Pfam; PF11636; Troponin-I_N; 1.
DR   SUPFAM; SSF90250; Troponin coil-coiled subunits; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Muscle protein {ECO:0000256|ARBA:ARBA00023179};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233140}.
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          48..109
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   209 AA;  23851 MW;  1E4963823FBDAA73 CRC64;
     HPDGSSKAGE PRPAPAPIRR RSSNYRAYAT EPHAKKKSKI SASRKLQLKT LLLQIAKQEL
     EREAEERRGE KGRALSTRCQ PLELAGLGFA ELQDLCRQLH ARVDKVDEER YDIQAKVTKN
     ITEIADLTQK IFDLRGKFKR PTLRRVRISA DAMMQALLGA RAKESLDLRA HLKQVKKEDT
     EKENREVGDW RKNIDALSGM EGRKKKFEG
//
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