CYC_THUAA
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 03-AUG-2022, entry version 109.
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";
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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; -; 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; 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
