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Cytochrome c

 CYC_HORSE               Reviewed;         105 AA.
P00004;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
23-MAY-2018, entry version 143.
RecName: Full=Cytochrome c;
Name=CYCS; Synonyms=CYC;
Equus caballus (Horse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
NCBI_TaxID=9796;
[1]
PROTEIN SEQUENCE OF 2-105, AND ACETYLATION AT GLY-2.
TISSUE=Heart;
PubMed=14469771; DOI=10.1038/1921125a0;
Margoliash E., Smith E.L., Kreil G., Tuppy H.;
"Amino-acid sequence of horse heart cytochrome c.";
Nature 192:1125-1127(1961).
[2]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
PubMed=5545094;
Dickerson R.E., Takano T., Eisenberg D., Kallai O.B., Samson L.,
Cooper A., Margoliash E.;
"Ferricytochrome c. I. General features of the horse and bonito
proteins at 2.8-A resolution.";
J. Biol. Chem. 246:1511-1535(1971).
[3]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
PubMed=2166170; DOI=10.1016/0022-2836(90)90200-6;
Bushnell G.W., Louie G.V., Brayer G.D.;
"High-resolution three-dimensional structure of horse heart cytochrome
c.";
J. Mol. Biol. 214:585-595(1990).
[4]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
PubMed=8591047; DOI=10.1016/S0969-2126(01)00205-2;
Sanishvili R., Volz K.W., Westbrook E.M., Margoliash E.;
"The low ionic strength crystal structure of horse cytochrome c at
2.1-A resolution and comparison with its high ionic strength
counterpart.";
Structure 3:707-716(1995).
[5]
STRUCTURE BY NMR.
PubMed=2539855; DOI=10.1021/bi00427a027;
Feng Y., Roder H., Englander S.W., Wand A.J., di Stefano D.L.;
"Proton resonance assignments of horse ferricytochrome c.";
Biochemistry 28:195-203(1989).
[6]
STRUCTURE BY NMR.
PubMed=8823161; DOI=10.1021/bi961042w;
Qi P.X., Beckman R.A., Wand A.J.;
"Solution structure of horse heart ferricytochrome c and detection of
redox-related structural changes by high-resolution 1H NMR.";
Biochemistry 35:12275-12286(1996).
[7]
STRUCTURE BY NMR.
TISSUE=Heart;
PubMed=9245419; DOI=10.1021/bi970724w;
Banci L., Bertini I., Gray H.B., Luchinat C., Reddig T., Rosato A.,
Turano P.;
"Solution structure of oxidized horse heart cytochrome c.";
Biochemistry 36:9867-9877(1997).
-!- 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}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-865260, EBI-865260;
-!- 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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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
PIR; A00005; CCHO.
UniGene; Eca.1571; -.
PDB; 1AKK; NMR; -; A=2-105.
PDB; 1CRC; X-ray; 2.08 A; A/B=2-105.
PDB; 1FI7; NMR; -; A=2-105.
PDB; 1FI9; NMR; -; A=2-105.
PDB; 1GIW; NMR; -; A=2-105.
PDB; 1HRC; X-ray; 1.90 A; A=2-105.
PDB; 1I5T; NMR; -; A=2-105.
PDB; 1LC1; NMR; -; A=2-105.
PDB; 1LC2; NMR; -; A=2-105.
PDB; 1M60; NMR; -; A=2-105.
PDB; 1OCD; NMR; -; A=2-105.
PDB; 1U75; X-ray; 2.55 A; B=2-105.
PDB; 1WEJ; X-ray; 1.80 A; F=2-105.
PDB; 2FRC; NMR; -; A=2-105.
PDB; 2GIW; NMR; -; A=2-105.
PDB; 2N3B; NMR; -; A=2-105.
PDB; 2PCB; X-ray; 2.80 A; B=2-105.
PDB; 3JBT; EM; 3.80 A; B/D/F/H/J/L/N=1-105.
PDB; 3NBS; X-ray; 2.20 A; A/B/C/D=2-105.
PDB; 3NBT; X-ray; 2.10 A; A/B/C/D/E/F=2-105.
PDB; 3O1Y; X-ray; 1.75 A; A/B/C=2-105.
PDB; 3O20; X-ray; 1.90 A; A/B/C=2-105.
PDB; 3WC8; X-ray; 1.80 A; A=2-105.
PDB; 3WUI; X-ray; 1.80 A; A=2-105.
PDB; 4NFG; X-ray; 2.11 A; B=2-105.
PDB; 4RSZ; X-ray; 2.19 A; A/B/C/D/E/F=2-105.
PDB; 5IY5; X-ray; 2.00 A; 1/2=2-105.
PDB; 5WVE; EM; 4.40 A; B/D/F/H/J/L/N=1-105.
PDBsum; 1AKK; -.
PDBsum; 1CRC; -.
PDBsum; 1FI7; -.
PDBsum; 1FI9; -.
PDBsum; 1GIW; -.
PDBsum; 1HRC; -.
PDBsum; 1I5T; -.
PDBsum; 1LC1; -.
PDBsum; 1LC2; -.
PDBsum; 1M60; -.
PDBsum; 1OCD; -.
PDBsum; 1U75; -.
PDBsum; 1WEJ; -.
PDBsum; 2FRC; -.
PDBsum; 2GIW; -.
PDBsum; 2N3B; -.
PDBsum; 2PCB; -.
PDBsum; 3JBT; -.
PDBsum; 3NBS; -.
PDBsum; 3NBT; -.
PDBsum; 3O1Y; -.
PDBsum; 3O20; -.
PDBsum; 3WC8; -.
PDBsum; 3WUI; -.
PDBsum; 4NFG; -.
PDBsum; 4RSZ; -.
PDBsum; 5IY5; -.
PDBsum; 5WVE; -.
DisProt; DP00006; -.
ProteinModelPortal; P00004; -.
SMR; P00004; -.
DIP; DIP-36774N; -.
IntAct; P00004; 2.
STRING; 9796.ENSECAP00000012031; -.
MoonProt; P00004; -.
CarbonylDB; P00004; -.
iPTMnet; P00004; -.
PaxDb; P00004; -.
PeptideAtlas; P00004; -.
PRIDE; P00004; -.
eggNOG; KOG3453; Eukaryota.
eggNOG; COG3474; LUCA.
HOGENOM; HOG000009762; -.
HOVERGEN; HBG003023; -.
InParanoid; P00004; -.
SABIO-RK; P00004; -.
EvolutionaryTrace; P00004; -.
PMAP-CutDB; P00004; -.
Proteomes; UP000002281; Unplaced.
GO; GO:0070069; C:cytochrome complex; IDA:CAFA.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; ISS:UniProtKB.
GO; GO:0020037; F:heme binding; IDA:CAFA.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0018063; P:cytochrome c-heme linkage; IDA:CAFA.
GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
GO; GO:2001056; P:positive regulation of cysteine-type endopeptidase activity; IDA:CAFA.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
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;
3D-structure; Acetylation; Apoptosis; Complete proteome;
Direct protein sequencing; Electron transport; Heme; Iron;
Metal-binding; Mitochondrion; Phosphoprotein; Reference proteome;
Respiratory chain; Transport.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:14469771}.
CHAIN 2 105 Cytochrome c.
/FTId=PRO_0000108217.
METAL 19 19 Iron (heme axial ligand).
{ECO:0000255|PROSITE-ProRule:PRU00433,
ECO:0000269|PubMed:5545094}.
METAL 81 81 Iron (heme axial ligand).
BINDING 15 15 Heme (covalent).
BINDING 18 18 Heme (covalent).
MOD_RES 2 2 N-acetylglycine.
{ECO:0000269|PubMed:14469771}.
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}.
HELIX 4 14 {ECO:0000244|PDB:3O1Y}.
TURN 15 18 {ECO:0000244|PDB:3O1Y}.
STRAND 22 24 {ECO:0000244|PDB:5IY5}.
STRAND 28 30 {ECO:0000244|PDB:1U75}.
TURN 34 37 {ECO:0000244|PDB:1OCD}.
STRAND 39 42 {ECO:0000244|PDB:5IY5}.
STRAND 44 47 {ECO:0000244|PDB:1I5T}.
HELIX 51 54 {ECO:0000244|PDB:3O1Y}.
HELIX 62 70 {ECO:0000244|PDB:3O1Y}.
HELIX 72 75 {ECO:0000244|PDB:3O1Y}.
STRAND 76 78 {ECO:0000244|PDB:2PCB}.
STRAND 86 88 {ECO:0000244|PDB:1FI7}.
HELIX 89 102 {ECO:0000244|PDB:3O1Y}.
SEQUENCE 105 AA; 11833 MW; 659BA128E53C3868 CRC64;
MGDVEKGKKI FVQKCAQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGFTYT DANKNKGITW
KEETLMEYLE NPKKYIPGTK MIFAGIKKKT EREDLIAYLK KATNE


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