ID   CYC_APIME               Reviewed;         108 AA.
AC   P00038; Q6J4P9;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Cytochrome c;
GN   Name=cytC;
OS   Apis mellifera (Honeybee).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; Apidae;
OC   Apis.
OX   NCBI_TaxID=7460;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Corona M., Hughes K.A., Weaver D.B., Robinson G.E.;
RT   "Molecular mechanisms of honey bee queen longevity.";
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 2-108.
RX   PubMed=2991212; DOI=10.1093/oxfordjournals.jbchem.a135136;
RA   Inoue S., Matsubara H., Yamanaka T.;
RT   "Complete amino acid sequence of cytochrome c from the honeybee, Apis
RT   mellifera, and evolutionary relationship of the honeybee to other insects
RT   on the basis of the amino acid sequence.";
RL   J. Biochem. 97:947-954(1985).
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   EMBL; AY601642; AAT12410.1; -; mRNA.
DR   PIR; A00031; CCHB.
DR   RefSeq; NP_001170961.1; NM_001177490.1.
DR   AlphaFoldDB; P00038; -.
DR   SMR; P00038; -.
DR   STRING; 7460.GB48784-PA; -.
DR   PaxDb; P00038; -.
DR   PRIDE; P00038; -.
DR   EnsemblMetazoa; NM_001177490; NP_001170961; GeneID_408270.
DR   GeneID; 408270; -.
DR   KEGG; ame:408270; -.
DR   CTD; 408270; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   HOGENOM; CLU_060944_3_0_1; -.
DR   InParanoid; P00038; -.
DR   OMA; AQCHTIN; -.
DR   OrthoDB; 1533604at2759; -.
DR   PhylomeDB; P00038; -.
DR   Proteomes; UP000005203; Unplaced.
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   Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding;
KW   Mitochondrion; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2991212"
FT   CHAIN           2..108
FT                   /note="Cytochrome c"
FT                   /id="PRO_0000108258"
FT   BINDING         19
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT                   ECO:0000269|PubMed:2991212"
FT   BINDING         22
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT                   ECO:0000269|PubMed:2991212"
FT   BINDING         23
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         85
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"
SQ   SEQUENCE   108 AA;  11910 MW;  17C298A8B7092AB1 CRC64;
     MGIPAGDPEK GKKIFVQKCA QCHTIESGGK HKVGPNLYGV YGRKTGQAPG YSYTDANKGK
     GITWNKETLF EYLENPKKYI PGTKMVFAGL KKPQERADLI AYIEQASK