CYC_HORSE
ID CYC_HORSE Reviewed; 105 AA.
AC P00004;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Cytochrome c;
GN Name=CYCS; Synonyms=CYC;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP PROTEIN SEQUENCE OF 2-105, AND ACETYLATION AT GLY-2.
RC TISSUE=Heart;
RX PubMed=14469771; DOI=10.1038/1921125a0;
RA Margoliash E., Smith E.L., Kreil G., Tuppy H.;
RT "Amino-acid sequence of horse heart cytochrome c.";
RL Nature 192:1125-1127(1961).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=5545094; DOI=10.1016/s0021-9258(19)77002-1;
RA Dickerson R.E., Takano T., Eisenberg D., Kallai O.B., Samson L., Cooper A.,
RA Margoliash E.;
RT "Ferricytochrome c. I. General features of the horse and bonito proteins at
RT 2.8-A resolution.";
RL J. Biol. Chem. 246:1511-1535(1971).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=2166170; DOI=10.1016/0022-2836(90)90200-6;
RA Bushnell G.W., Louie G.V., Brayer G.D.;
RT "High-resolution three-dimensional structure of horse heart cytochrome c.";
RL J. Mol. Biol. 214:585-595(1990).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=8591047; DOI=10.1016/s0969-2126(01)00205-2;
RA Sanishvili R., Volz K.W., Westbrook E.M., Margoliash E.;
RT "The low ionic strength crystal structure of horse cytochrome c at 2.1-A
RT resolution and comparison with its high ionic strength counterpart.";
RL Structure 3:707-716(1995).
RN [5]
RP STRUCTURE BY NMR.
RX PubMed=2539855; DOI=10.1021/bi00427a027;
RA Feng Y., Roder H., Englander S.W., Wand A.J., di Stefano D.L.;
RT "Proton resonance assignments of horse ferricytochrome c.";
RL Biochemistry 28:195-203(1989).
RN [6]
RP STRUCTURE BY NMR.
RX PubMed=8823161; DOI=10.1021/bi961042w;
RA Qi P.X., Beckman R.A., Wand A.J.;
RT "Solution structure of horse heart ferricytochrome c and detection of
RT redox-related structural changes by high-resolution 1H NMR.";
RL Biochemistry 35:12275-12286(1996).
RN [7]
RP STRUCTURE BY NMR.
RC TISSUE=Heart;
RX PubMed=9245419; DOI=10.1021/bi970724w;
RA Banci L., Bertini I., Gray H.B., Luchinat C., Reddig T., Rosato A.,
RA Turano P.;
RT "Solution structure of oxidized horse heart cytochrome c.";
RL Biochemistry 36:9867-9877(1997).
CC -!- FUNCTION: Electron carrier protein. The oxidized form of the cytochrome
CC c heme group can accept an electron from the heme group of the
CC cytochrome c1 subunit of cytochrome reductase. Cytochrome c then
CC transfers this electron to the cytochrome oxidase complex, the final
CC protein carrier in the mitochondrial electron-transport chain.
CC -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic
CC members or activation of the pro-apoptotic members of the Bcl-2 family
CC leads to altered mitochondrial membrane permeability resulting in
CC release of cytochrome c into the cytosol. Binding of cytochrome c to
CC Apaf-1 triggers the activation of caspase-9, which then accelerates
CC apoptosis by activating other caspases (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P00004; P00004: CYCS; NbExp=3; IntAct=EBI-865260, EBI-865260;
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely
CC associated with the inner membrane.
CC -!- PTM: Binds 1 heme c group covalently per subunit.
CC -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC turnover in the reaction with cytochrome c oxidase, down-regulating
CC mitochondrial respiration. {ECO:0000250}.
CC -!- MISCELLANEOUS: Mules and hinnies are heterozygous, having equal amount
CC of horse and donkey cytochromes c.
CC -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 of
CC November 2006;
CC URL="https://web.expasy.org/spotlight/back_issues/076";
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DR PIR; A00005; CCHO.
DR PDB; 1AKK; NMR; -; A=2-105.
DR PDB; 1CRC; X-ray; 2.08 A; A/B=2-105.
DR PDB; 1FI7; NMR; -; A=2-105.
DR PDB; 1FI9; NMR; -; A=2-105.
DR PDB; 1GIW; NMR; -; A=2-105.
DR PDB; 1HRC; X-ray; 1.90 A; A=2-105.
DR PDB; 1I5T; NMR; -; A=2-105.
DR PDB; 1LC1; NMR; -; A=2-105.
DR PDB; 1LC2; NMR; -; A=2-105.
DR PDB; 1M60; NMR; -; A=2-105.
DR PDB; 1OCD; NMR; -; A=2-105.
DR PDB; 1U75; X-ray; 2.55 A; B=2-105.
DR PDB; 1WEJ; X-ray; 1.80 A; F=2-105.
DR PDB; 2FRC; NMR; -; A=2-105.
DR PDB; 2GIW; NMR; -; A=2-105.
DR PDB; 2N3B; NMR; -; A=2-105.
DR PDB; 2PCB; X-ray; 2.80 A; B=2-105.
DR PDB; 3JBT; EM; 3.80 A; B/D/F/H/J/L/N=1-105.
DR PDB; 3NBS; X-ray; 2.20 A; A/B/C/D=2-105.
DR PDB; 3NBT; X-ray; 2.10 A; A/B/C/D/E/F=2-105.
DR PDB; 3O1Y; X-ray; 1.75 A; A/B/C=2-105.
DR PDB; 3O20; X-ray; 1.90 A; A/B/C=2-105.
DR PDB; 3WC8; X-ray; 1.80 A; A=2-105.
DR PDB; 3WUI; X-ray; 1.80 A; A=2-105.
DR PDB; 4NFG; X-ray; 2.11 A; B=2-105.
DR PDB; 4RSZ; X-ray; 2.19 A; A/B/C/D/E/F=2-105.
DR PDB; 5IY5; X-ray; 2.00 A; 1/2=2-105.
DR PDB; 5WVE; EM; 4.40 A; B/D/F/H/J/L/N=1-105.
DR PDB; 5ZKV; NMR; -; A=2-105.
DR PDB; 6K9I; X-ray; 1.80 A; A=2-105.
DR PDB; 6K9J; X-ray; 0.98 A; A=2-105.
DR PDB; 6SUV; X-ray; 2.50 A; AaA/BaB/CaC/DaD/EaE/FaF/GaG/HaH=2-105.
DR PDBsum; 1AKK; -.
DR PDBsum; 1CRC; -.
DR PDBsum; 1FI7; -.
DR PDBsum; 1FI9; -.
DR PDBsum; 1GIW; -.
DR PDBsum; 1HRC; -.
DR PDBsum; 1I5T; -.
DR PDBsum; 1LC1; -.
DR PDBsum; 1LC2; -.
DR PDBsum; 1M60; -.
DR PDBsum; 1OCD; -.
DR PDBsum; 1U75; -.
DR PDBsum; 1WEJ; -.
DR PDBsum; 2FRC; -.
DR PDBsum; 2GIW; -.
DR PDBsum; 2N3B; -.
DR PDBsum; 2PCB; -.
DR PDBsum; 3JBT; -.
DR PDBsum; 3NBS; -.
DR PDBsum; 3NBT; -.
DR PDBsum; 3O1Y; -.
DR PDBsum; 3O20; -.
DR PDBsum; 3WC8; -.
DR PDBsum; 3WUI; -.
DR PDBsum; 4NFG; -.
DR PDBsum; 4RSZ; -.
DR PDBsum; 5IY5; -.
DR PDBsum; 5WVE; -.
DR PDBsum; 5ZKV; -.
DR PDBsum; 6K9I; -.
DR PDBsum; 6K9J; -.
DR PDBsum; 6SUV; -.
DR AlphaFoldDB; P00004; -.
DR BMRB; P00004; -.
DR PCDDB; P00004; -.
DR SASBDB; P00004; -.
DR SMR; P00004; -.
DR DIP; DIP-36774N; -.
DR IntAct; P00004; 2.
DR STRING; 9796.ENSECAP00000012031; -.
DR MoonProt; P00004; -.
DR CarbonylDB; P00004; -.
DR iPTMnet; P00004; -.
DR MetOSite; P00004; -.
DR PaxDb; P00004; -.
DR PeptideAtlas; P00004; -.
DR PRIDE; P00004; -.
DR ABCD; P00004; 5 sequenced antibodies.
DR InParanoid; P00004; -.
DR SABIO-RK; P00004; -.
DR EvolutionaryTrace; P00004; -.
DR Proteomes; UP000002281; Unplaced.
DR GO; GO:0070069; C:cytochrome complex; IDA:CAFA.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IDA:CAFA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0018063; P:cytochrome c-heme linkage; IDA:CAFA.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:ARUK-UCL.
DR GO; GO:2001056; P:positive regulation of cysteine-type endopeptidase activity; IDA:CAFA.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:ARUK-UCL.
DR Gene3D; 1.10.760.10; -; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR002327; Cyt_c_1A/1B.
DR PANTHER; PTHR11961; PTHR11961; 1.
DR Pfam; PF00034; Cytochrom_C; 1.
DR PRINTS; PR00604; CYTCHRMECIAB.
DR SUPFAM; SSF46626; SSF46626; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Apoptosis; Direct protein sequencing;
KW Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:14469771"
FT CHAIN 2..105
FT /note="Cytochrome c"
FT /id="PRO_0000108217"
FT BINDING 15
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 18
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 19
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT ECO:0000269|PubMed:5545094"
FT BINDING 81
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000269|PubMed:14469771"
FT MOD_RES 49
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P62894"
FT MOD_RES 56
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62897"
FT MOD_RES 73
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62897"
FT MOD_RES 73
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62897"
FT MOD_RES 98
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P62894"
FT MOD_RES 100
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62897"
FT HELIX 4..14
FT /evidence="ECO:0007829|PDB:6K9J"
FT TURN 15..18
FT /evidence="ECO:0007829|PDB:6K9J"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:5IY5"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:1U75"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:1OCD"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:5IY5"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:1I5T"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:6K9J"
FT HELIX 62..70
FT /evidence="ECO:0007829|PDB:6K9J"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:6K9J"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:2PCB"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:1FI7"
FT HELIX 89..102
FT /evidence="ECO:0007829|PDB:6K9J"
SQ SEQUENCE 105 AA; 11833 MW; 659BA128E53C3868 CRC64;
MGDVEKGKKI FVQKCAQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGFTYT DANKNKGITW
KEETLMEYLE NPKKYIPGTK MIFAGIKKKT EREDLIAYLK KATNE
