ID CYC_THUAA Reviewed; 103 AA. AC P81459; DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 27-MAR-2024, entry version 112. DE RecName: Full=Cytochrome c; GN Name=cyc; OS Thunnus alalunga (Albacore) (Scomber alalunga). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Pelagiaria; Scombriformes; Scombridae; Thunnus. OX NCBI_TaxID=8235; RN [1] RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS). RC TISSUE=Heart; RX PubMed=4358609; DOI=10.1016/s0021-9258(19)43594-1; RA Takano T., Kallai O.B., Swanson R., Dickerson R.E.; RT "The structure of ferrocytochrome c at 2.45 A resolution."; RL J. Biol. Chem. 248:5234-5255(1973). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF REDUCED FORM. RC TISSUE=Heart; RX PubMed=6279867; DOI=10.1016/0022-2836(81)90528-3; RA Takano T., Dickerson R.E.; RT "Conformation change of cytochrome c. I. Ferrocytochrome c structure RT refined at 1.5 A resolution."; RL J. Mol. Biol. 153:79-94(1981). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF REDUCED FORM. RC TISSUE=Heart; RX PubMed=6253809; DOI=10.1038/287659a0; RA Northrup S.H., Pear M.R., McCammon J.A., Karplus M., Takano T.; RT "Internal mobility of ferrocytochrome c."; RL Nature 287:659-660(1980). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF OXIDIZED FORM. RC TISSUE=Heart; RX PubMed=13079; DOI=10.1016/s0021-9258(17)32783-7; RA Swanson R., Trus B.L., Mandel N., Mandel G., Kallai O.B., Dickerson R.E.; RT "Tuna cytochrome c at 2.0 A resolution. I. Ferricytochrome structure RT analysis."; RL J. Biol. Chem. 252:759-775(1977). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF REDUCED FORM. RC TISSUE=Heart; RX PubMed=188826; DOI=10.1016/s0021-9258(17)32784-9; RA Takano T., Trus B.L., Mandel N., Mandel G., Kallai O.B., Swanson R., RA Dickerson R.E.; RT "Tuna cytochrome c at 2.0 A resolution. II. Ferrocytochrome structure RT analysis."; RL J. Biol. Chem. 252:776-785(1977). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF OXIDIZED AND REDUCED FORMS. RX PubMed=194885; DOI=10.1016/s0021-9258(17)40207-9; RA Mandel N., Mandel G., Trus B.L., Rosenburg J., Carlson G., Dickerson R.E.; RT "Tuna cytochrome c at 2.0-A resolution. III. Coordinate optimization and RT comparison of structures."; RL J. Biol. Chem. 252:4619-4636(1977). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF OXIDIZED AND REDUCED FORMS. RC TISSUE=Heart; RX PubMed=6256733; DOI=10.1073/pnas.77.11.6371; RA Takano T., Dickerson R.E.; RT "Redox conformation changes in refined tuna cytochrome c."; RL Proc. Natl. Acad. Sci. U.S.A. 77:6371-6375(1980). RN [8] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF ZN-SUBSTITUTED FORMS. RC TISSUE=Heart; RX PubMed=11296248; DOI=10.1073/pnas.081072898; RA Tezcan F.A., Crane B.R., Winkler J.R., Gray H.B.; RT "Electron tunneling in protein crystals."; RL Proc. Natl. Acad. Sci. U.S.A. 98:5002-5006(2001). 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 -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely CC associated with the inner membrane. CC -!- PTM: Binds 1 heme c group covalently per subunit. 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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR PDB; 1I54; X-ray; 1.50 A; A/B=1-103. DR PDB; 1I55; X-ray; 2.00 A; A/B=1-103. DR PDB; 1LFM; X-ray; 1.50 A; A/B=1-103. DR PDB; 3CYT; X-ray; 1.80 A; I/O=1-103. DR PDB; 5CYT; X-ray; 1.50 A; R=1-103. DR PDBsum; 1I54; -. DR PDBsum; 1I55; -. DR PDBsum; 1LFM; -. DR PDBsum; 3CYT; -. DR PDBsum; 5CYT; -. DR AlphaFoldDB; P81459; -. DR SMR; P81459; -. DR EvolutionaryTrace; P81459; -. DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell. 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; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 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; CYTOCHROME C; 1. DR PANTHER; PTHR11961:SF12; CYTOCHROME C; 1. DR Pfam; PF00034; Cytochrom_C; 1. DR PRINTS; PR00604; CYTCHRMECIAB. DR SUPFAM; SSF46626; Cytochrome c; 1. DR PROSITE; PS51007; CYTC; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Electron transport; Heme; Iron; Metal-binding; KW Mitochondrion; Respiratory chain; Transport. FT CHAIN 1..103 FT /note="Cytochrome c" FT /id="PRO_0000108255" FT BINDING 14 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /note="covalent" FT BINDING 17 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 /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT BINDING 80 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 1 FT /note="N-acetylglycine" FT /evidence="ECO:0000250|UniProtKB:P00025" FT HELIX 3..13 FT /evidence="ECO:0007829|PDB:1I54" FT TURN 14..17 FT /evidence="ECO:0007829|PDB:1I54" FT STRAND 27..29 FT /evidence="ECO:0007829|PDB:5CYT" FT HELIX 50..54 FT /evidence="ECO:0007829|PDB:1I54" FT HELIX 61..69 FT /evidence="ECO:0007829|PDB:1I54" FT HELIX 71..74 FT /evidence="ECO:0007829|PDB:1I54" FT HELIX 88..101 FT /evidence="ECO:0007829|PDB:1I54" SQ SEQUENCE 103 AA; 11370 MW; 1CBC776EF34A8677 CRC64; GDVAKGKKTF VQKCAQCHTV ENGGKHKVGP NLWGLFGRKT GQAEGYSYTD ANKSKGIVWN NDTLMEYLEN PKKYIPGTKM IFAGIKKKGE RQDLVAYLKS ATS //