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Database: UniProt
Entry: CYC_ORYSJ
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ID   CYC_ORYSJ               Reviewed;         112 AA.
AC   Q0DI31; B7E4T8; P00055; Q6L4Z1;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 118.
DE   RecName: Full=Cytochrome c;
GN   Name=CC-1; OrderedLocusNames=Os05g0420600, LOC_Os05g34770;
GN   ORFNames=OsJ_017825, OsJ_18585 {ECO:0000312|EMBL:EEE63765.1},
GN   OSJNBb0092E21.3, P0426G01.18;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Yamahoushi;
RA   Nishi R., Uchimiya H., Kato A.;
RT   "cDNA cloning and sequence analysis of rice cytochrome c gene.";
RL   Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA   Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA   Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA   Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT   "A fine physical map of the rice chromosome 5.";
RL   Mol. Genet. Genomics 274:337-345(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [8]
RP   PROTEIN SEQUENCE OF 2-112, ACETYLATION AT ALA-2, AND METHYLATION AT LYS-81
RP   AND LYS-95.
RX   PubMed=6244261; DOI=10.1093/oxfordjournals.jbchem.a132732;
RA   Mori E., Morita Y.;
RT   "Amino acid sequence of cytochrome c from rice.";
RL   J. Biochem. 87:249-266(1980).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   PubMed=6304326; DOI=10.1016/s0022-2836(83)80092-8;
RA   Ochi H., Hata Y., Tanaka N., Kakudo M., Sakurai T., Aihara S., Morita Y.;
RT   "Structure of rice ferricytochrome c at 2.0-A resolution.";
RL   J. Mol. Biol. 166:407-418(1983).
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; D12634; BAA02159.1; -; mRNA.
DR   EMBL; AC124836; AAT44244.1; -; Genomic_DNA.
DR   EMBL; AC137623; AAV25652.1; -; Genomic_DNA.
DR   EMBL; AP008211; BAF17492.1; -; Genomic_DNA.
DR   EMBL; AP014961; BAS94074.1; -; Genomic_DNA.
DR   EMBL; CM000142; EAZ34342.1; -; Genomic_DNA.
DR   EMBL; CM000142; EEE63765.1; -; Genomic_DNA.
DR   EMBL; AK060267; BAG87385.1; -; mRNA.
DR   PIR; JS0709; CCRZ.
DR   RefSeq; XP_015640631.1; XM_015785145.1.
DR   PDB; 1CCR; X-ray; 1.50 A; A=2-112.
DR   PDBsum; 1CCR; -.
DR   AlphaFoldDB; Q0DI31; -.
DR   SMR; Q0DI31; -.
DR   STRING; 39947.Q0DI31; -.
DR   iPTMnet; Q0DI31; -.
DR   PaxDb; 39947-Q0DI31; -.
DR   EnsemblPlants; Os05t0420600-01; Os05t0420600-01; Os05g0420600.
DR   GeneID; 4338825; -.
DR   Gramene; Os05t0420600-01; Os05t0420600-01; Os05g0420600.
DR   KEGG; osa:4338825; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   HOGENOM; CLU_060944_3_0_1; -.
DR   InParanoid; Q0DI31; -.
DR   OMA; WGCPASE; -.
DR   OrthoDB; 4150at2759; -.
DR   EvolutionaryTrace; Q0DI31; -.
DR   Proteomes; UP000000763; Chromosome 5.
DR   Proteomes; UP000007752; Chromosome 5.
DR   Proteomes; UP000059680; Chromosome 5.
DR   Genevisible; Q0DI31; OS.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
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   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
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:SF58; CYTOCHROME C-2; 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; Direct protein sequencing; Electron transport;
KW   Heme; Iron; Metal-binding; Methylation; Mitochondrion; Reference proteome;
KW   Respiratory chain; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:6244261"
FT   CHAIN           2..112
FT                   /note="Cytochrome c"
FT                   /id="PRO_0000108303"
FT   BINDING         23
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         26
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         27
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         89
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-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:6244261"
FT   MOD_RES         81
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000269|PubMed:6244261"
FT   MOD_RES         95
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000269|PubMed:6244261"
FT   HELIX           4..6
FT                   /evidence="ECO:0007829|PDB:1CCR"
FT   HELIX           12..22
FT                   /evidence="ECO:0007829|PDB:1CCR"
FT   TURN            23..26
FT                   /evidence="ECO:0007829|PDB:1CCR"
FT   STRAND          36..38
FT                   /evidence="ECO:0007829|PDB:1CCR"
FT   HELIX           59..64
FT                   /evidence="ECO:0007829|PDB:1CCR"
FT   HELIX           70..78
FT                   /evidence="ECO:0007829|PDB:1CCR"
FT   HELIX           80..83
FT                   /evidence="ECO:0007829|PDB:1CCR"
FT   HELIX           97..110
FT                   /evidence="ECO:0007829|PDB:1CCR"
SQ   SEQUENCE   112 AA;  12271 MW;  C17D2B4628C77146 CRC64;
     MASFSEAPPG NPKAGEKIFK TKCAQCHTVD KGAGHKQGPN LNGLFGRQSG TTPGYSYSTA
     NKNMAVIWEE NTLYDYLLNP KKYIPGTKMV FPGLKKPQER ADLISYLKEA TS
//
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