ID   CYC_MANSE               Reviewed;         108 AA.
AC   P00039;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Cytochrome c;
OS   Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Sphingidae; Sphinginae; Sphingini; Manduca.
OX   NCBI_TaxID=7130;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Thoracic muscle;
RX   PubMed=2984675; DOI=10.1073/pnas.82.7.1964;
RA   Swanson M.S., Zieminn S.M., Miller D.D., Garber E.A.E., Margoliash E.;
RT   "Developmental expression of nuclear genes that encode mitochondrial
RT   proteins: insect cytochromes c.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:1964-1968(1985).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-108.
RC   TISSUE=Thoracic muscle;
RX   PubMed=5499433; DOI=10.1016/0005-2795(70)90220-5;
RA   Chan S.K.;
RT   "Biochemical studies in the developing thoracic muscles of the tobacco horn
RT   worm. IV. Primary structure of cytochrome c.";
RL   Biochim. Biophys. Acta 221:497-501(1970).
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   EMBL; M11382; AAA29308.1; -; mRNA.
DR   PIR; A90578; CCWOT.
DR   PDB; 3QIB; X-ray; 2.70 A; P=97-108.
DR   PDB; 3QIU; X-ray; 2.70 A; E=97-108.
DR   PDB; 3QIW; X-ray; 3.30 A; E=97-108.
DR   PDBsum; 3QIB; -.
DR   PDBsum; 3QIU; -.
DR   PDBsum; 3QIW; -.
DR   AlphaFoldDB; P00039; -.
DR   SMR; P00039; -.
DR   EvolutionaryTrace; P00039; -.
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; 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:5499433"
FT   CHAIN           2..108
FT                   /note="Cytochrome c"
FT                   /id="PRO_0000108264"
FT   BINDING         19
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         22
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
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"
FT   CONFLICT        7..10
FT                   /note="DVEK -> NADN (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        14
FT                   /note="L -> I (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        33
FT                   /note="I -> V (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        55
FT                   /note="D -> N (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        65..66
FT                   /note="NE -> QD (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        105
FT                   /note="Q -> E (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   108 AA;  11860 MW;  5748FCB9F9F0D3C3 CRC64;
     MGVPAGDVEK GKKLFVQRCA QCHTVEAGGK HKIGPNLHGF FGRKTGQAPG FSYSDANKAK
     GITWNEDTLF EYLENPKKYI PGTKMVFAGL KKANERADLI AYLKQATK