ID CYC_ALLMI Reviewed; 105 AA.
AC P81280;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=Cytochrome c;
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496;
RN [1]
RP PROTEIN SEQUENCE OF 2-105, AND ACETYLATION AT GLY-2.
RC TISSUE=Liver;
RX PubMed=8384830; DOI=10.1006/abbi.1993.1146;
RA Barber M.J., Trimboli A.J., Clark M., Young C., Neame P.J.;
RT "Purification and properties of Alligator mississipiensis cytochrome c.";
RL Arch. Biochem. Biophys. 301:294-298(1993).
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 PIR; S30377; S30377.
DR AlphaFoldDB; P81280; -.
DR SMR; P81280; -.
DR iPTMnet; P81280; -.
DR eggNOG; KOG3453; Eukaryota.
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 Acetylation; Direct protein sequencing; Electron transport; Heme; Iron;
KW Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8384830"
FT CHAIN 2..105
FT /note="Cytochrome c"
FT /id="PRO_0000108244"
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 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:8384830"
SQ SEQUENCE 105 AA; 11624 MW; 18EF5728E959955E CRC64;
MGDVEKGKKI FVQKCAQCHT VEKGGKHKTG PNLHGLIGRK TGQAPGFSYT EANKNKGITW
GEETLMEYLE NPKKYIPGTK MIFAGIKKKP ERADLIAYLK EATSN
//
