ID CYC_ASPNG Reviewed; 111 AA. AC P56205; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 16-JUN-2009, entry version 63. DE RecName: Full=Cytochrome c; GN Name=cycA; OS Aspergillus niger. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Trichocomaceae; OC mitosporic Trichocomaceae; Aspergillus. OX NCBI_TaxID=5061; RN [1] RP PROTEIN SEQUENCE. RX MEDLINE=89286914; PubMed=2544196; DOI=10.1007/BF01024941; RA Chin C.C.Q., Niehaus W.G., Wold F.; RT "Amino acid sequence of cytochrome c from Aspergillus niger."; RL J. Protein Chem. 8:165-171(1989). 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 -!- 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; A61490; A61490. DR HSSP; P00044; 1CRH. DR SMR; P56205; 6-109. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR InterPro; IPR002327; Cyt_c_1A/1B. DR InterPro; IPR003088; Cyt_c_I. DR InterPro; IPR009056; Cyt_c_monohaem. 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 Direct protein sequencing; Electron transport; Heme; Iron; KW Metal-binding; Methylation; Mitochondrion; Respiratory chain; KW Transport. FT CHAIN 1 111 Cytochrome c. FT /FTId=PRO_0000108317. FT METAL 26 26 Iron (heme axial ligand). FT METAL 88 88 Iron (heme axial ligand) (By similarity). FT BINDING 22 22 Heme (covalent). FT BINDING 25 25 Heme (covalent). FT MOD_RES 80 80 N6,N6,N6-trimethyllysine (By similarity). SQ SEQUENCE 111 AA; 11954 MW; 1F49BA817E205EB1 CRC64; GKDASFAPGD SAKGAKLFQT RCAQCHTVEA GGPHKVGPNL HGLFGRKTGQ SEGYAYTDAN KQAGVTWDEN TLFSYLENPK KFIPGTKMAF GGLKKGKERN DLITYLKEST A //