ID A0A2K5H8E2_COLAP Unreviewed; 161 AA.
AC A0A2K5H8E2;
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 C, slow skeletal and cardiac muscles {ECO:0000256|ARBA:ARBA00044185};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000000611.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000000611.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Troponin is the central regulatory protein of striated muscle
CC contraction. Tn consists of three components: Tn-I which is the
CC inhibitor of actomyosin ATPase, Tn-T which contains the binding site
CC for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the
CC inhibitory action of Tn on actin filaments.
CC {ECO:0000256|ARBA:ARBA00037722}.
CC -!- SIMILARITY: Belongs to the troponin C family.
CC {ECO:0000256|ARBA:ARBA00038202}.
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 RefSeq; XP_011814244.1; XM_011958854.1.
DR AlphaFoldDB; A0A2K5H8E2; -.
DR SMR; A0A2K5H8E2; -.
DR STRING; 336983.ENSCANP00000000611; -.
DR Ensembl; ENSCANT00000002576.1; ENSCANP00000000611.1; ENSCANG00000001867.1.
DR GeneID; 105523834; -.
DR KEGG; cang:105523834; -.
DR CTD; 7134; -.
DR OMA; QKSEFRA; -.
DR OrthoDB; 4239664at2759; -.
DR Proteomes; UP000233080; Unplaced.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:UniProt.
DR GO; GO:0006936; P:muscle contraction; IEA:UniProt.
DR CDD; cd00051; EFh; 2.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR23048; MYOSIN LIGHT CHAIN 1, 3; 1.
DR PANTHER; PTHR23048:SF48; TROPONIN C1, SLOW SKELETAL AND CARDIAC TYPE; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR PRINTS; PR00450; RECOVERIN.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF47473; EF-hand; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233080}.
FT DOMAIN 52..87
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 92..127
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 128..161
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
SQ SEQUENCE 161 AA; 18421 MW; 34DCC903C157A312 CRC64;
MDDIYKAAVE QLTEEQKNEF KAAFDIFVLG AEDGCISTKE LGKVMRMLGQ NPTPEELQEM
IDEVDEDGSG TVDFDEFLVM MVRCMKDDSK GKSEEELSDL FRMFDKNADG YIDLDELKMM
LQATGETITE DDIEELMKDG DKNNDGRIDY DEFLEFMKGV E
//
