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Cytochrome c

 CYC_EQUAS               Reviewed;         105 AA.
P68097; P00005;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
20-DEC-2017, entry version 74.
RecName: Full=Cytochrome c;
Name=CYCS; Synonyms=CYC;
Equus asinus (Donkey) (Equus africanus asinus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
NCBI_TaxID=9793;
[1]
PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 48-49.
PubMed=190219;
Walasek O.F., Margoliash E.;
"Transmission of the cytochrome c structural gene in horse-donkey
crosses.";
J. Biol. Chem. 252:830-834(1977).
-!- FUNCTION: Electron carrier protein. The oxidized form of the
cytochrome c heme group can accept an electron from the heme group
of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
then transfers this electron to the cytochrome oxidase complex,
the final protein carrier in the mitochondrial electron-transport
chain.
-!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
apoptotic members or activation of the pro-apoptotic members of
the Bcl-2 family leads to altered mitochondrial membrane
permeability resulting in release of cytochrome c into the
cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
of caspase-9, which then accelerates apoptosis by activating other
caspases (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
Note=Loosely associated with the inner membrane.
-!- PTM: Binds 1 heme group per subunit.
-!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
turnover in the reaction with cytochrome c oxidase, down-
regulating mitochondrial respiration. {ECO:0000250}.
-!- MISCELLANEOUS: Mules and hinnies are heterozygous, having equal
amount of horse and donkey cytochromes c.
-!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
of November 2006;
URL="https://web.expasy.org/spotlight/back_issues/076";
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PIR; A00006; CCHOD.
RefSeq; XP_014694486.1; XM_014839000.1.
RefSeq; XP_014694487.1; XM_014839001.1.
ProteinModelPortal; P68097; -.
SMR; P68097; -.
PeptideAtlas; P68097; -.
GeneID; 106829744; -.
KEGG; eai:106829744; -.
HOVERGEN; HBG003023; -.
KO; K08738; -.
GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
Gene3D; 1.10.760.10; -; 1.
InterPro; IPR009056; Cyt_c-like_dom.
InterPro; IPR036909; Cyt_c-like_dom_sf.
InterPro; IPR002327; Cyt_c_1A/1B.
PANTHER; PTHR11961; PTHR11961; 1.
Pfam; PF00034; Cytochrom_C; 1.
PRINTS; PR00604; CYTCHRMECIAB.
SUPFAM; SSF46626; SSF46626; 1.
PROSITE; PS51007; CYTC; 1.
1: Evidence at protein level;
Acetylation; Apoptosis; Direct protein sequencing; Electron transport;
Heme; Iron; Metal-binding; Mitochondrion; Phosphoprotein;
Respiratory chain; Transport.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P00003,
ECO:0000250|UniProtKB:P62894}.
CHAIN 2 105 Cytochrome c.
/FTId=PRO_0000108212.
METAL 19 19 Iron (heme axial ligand).
METAL 81 81 Iron (heme axial ligand).
BINDING 15 15 Heme (covalent).
BINDING 18 18 Heme (covalent).
MOD_RES 2 2 N-acetylglycine.
{ECO:0000250|UniProtKB:P62894}.
MOD_RES 49 49 Phosphotyrosine.
{ECO:0000250|UniProtKB:P62894}.
MOD_RES 56 56 N6-succinyllysine.
{ECO:0000250|UniProtKB:P62897}.
MOD_RES 73 73 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P62897}.
MOD_RES 73 73 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P62897}.
MOD_RES 98 98 Phosphotyrosine.
{ECO:0000250|UniProtKB:P62894}.
MOD_RES 100 100 N6-acetyllysine.
{ECO:0000250|UniProtKB:P62897}.
SEQUENCE 105 AA; 11819 MW; 659CA628E23B3868 CRC64;
MGDVEKGKKI FVQKCAQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGFSYT DANKNKGITW
KEETLMEYLE NPKKYIPGTK MIFAGIKKKT EREDLIAYLK KATNE


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