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 04-NOV-2008, entry version 80. DE RecName: Full=Cytochrome c; GN Name=CYCS; Synonyms=CYC; OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; 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 MEDLINE=62071232; PubMed=14469771; 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 MEDLINE=71116428; PubMed=5545094; RA Dickerson R.E., Takano T., Eisenberg D., Kallai O.B., Samson L., RA Cooper A., Margoliash E.; RT "Ferricytochrome c. I. General features of the horse and bonito RT proteins at 2.8-A resolution."; RL J. Biol. Chem. 246:1511-1533(1971). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). RX MEDLINE=90339495; 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 RT c."; RL J. Mol. Biol. 214:585-595(1990). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). RX MEDLINE=96000860; 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 RT 2.1-A resolution and comparison with its high ionic strength RT counterpart."; RL Structure 3:707-716(1995). RN [5] RP STRUCTURE BY NMR. RX MEDLINE=89207529; 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 MEDLINE=96420462; 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 MEDLINE=97392653; 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 CC cytochrome c heme group can accept an electron from the heme group CC of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c CC then transfers this electron to the cytochrome oxidase complex, CC the final protein carrier in the mitochondrial electron-transport CC chain. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. CC -!- PTM: Binds 1 heme group per subunit. CC -!- MISCELLANEOUS: Mules and hinnies are heterozygous, having equal CC amount of horse and donkey cytochromes c. CC -!- SIMILARITY: Belongs to the cytochrome c family. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 CC of November 2006; CC URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; A00005; CCHO. DR PDB; 1AKK; NMR; -; A=1-105. DR PDB; 1CRC; X-ray; 2.08 A; A/B=1-105. DR PDB; 1FI7; NMR; -; A=1-105. DR PDB; 1FI9; NMR; -; A=1-105. DR PDB; 1GIW; NMR; -; A=1-105. DR PDB; 1HRC; X-ray; 1.90 A; A=1-105. DR PDB; 1I5T; NMR; -; A=1-105. DR PDB; 1LC1; NMR; -; A=1-105. DR PDB; 1LC2; NMR; -; A=1-105. DR PDB; 1M60; NMR; -; A=1-105. DR PDB; 1OCD; NMR; -; A=1-105. DR PDB; 1U75; X-ray; 2.55 A; B=1-105. DR PDB; 1WEJ; X-ray; 1.80 A; F=1-105. DR PDB; 2FRC; NMR; -; A=1-105. DR PDB; 2GIW; NMR; -; A=1-105. DR PDB; 2PCB; X-ray; 2.80 A; B=1-105. 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; 2PCB; -. DR DisProt; DP00006; -. DR HOVERGEN; P00004; -. DR LinkHub; P00004; -. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB. DR GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS:UniProtKB. DR InterPro; IPR009056; Cyt_c_monohaem. DR InterPro; IPR003088; Cyt_CI. DR InterPro; IPR002327; Cyt_CIAB. DR Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1. DR PANTHER; PTHR11961; Cyt_CIAB; 1. DR Pfam; PF00034; Cytochrom_C; 1. DR PRINTS; PR00604; CYTCHRMECIAB. DR ProDom; PD000375; Cyt_CIAB; 1. DR PROSITE; PS51007; CYTC; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Direct protein sequencing; KW Electron transport; Heme; Iron; Metal-binding; Mitochondrion; KW Respiratory chain; Transport. FT INIT_MET 1 1 Removed. FT CHAIN 2 105 Cytochrome c. FT /FTId=PRO_0000108217. FT METAL 19 19 Iron (heme axial ligand). FT METAL 81 81 Iron (heme axial ligand). FT BINDING 15 15 Heme (covalent). FT BINDING 18 18 Heme (covalent). FT MOD_RES 2 2 N-acetylglycine. FT HELIX 4 14 FT TURN 15 18 FT HELIX 51 55 FT HELIX 62 70 FT HELIX 72 75 FT HELIX 89 102 SQ SEQUENCE 105 AA; 11833 MW; 659BA128E53C3868 CRC64; MGDVEKGKKI FVQKCAQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGFTYT DANKNKGITW KEETLMEYLE NPKKYIPGTK MIFAGIKKKT EREDLIAYLK KATNE //