[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=3036842 [NCBI, ExPASy, EBI, Israel, Japan] Merchant S., Bogorad L.; "The Cu(II)-repressible plastidic cytochrome c. Cloning and sequence of a complementary DNA for the pre-apoprotein."; J. Biol. Chem. 262:9062-9067(1987).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=1714451 [NCBI, ExPASy, EBI, Israel, Japan] Hill K.L., Li H.H., Singer J., Merchant S.; "Isolation and structural characterization of the Chlamydomonas reinhardtii gene for cytochrome c6. Analysis of the kinetics and metal specificity of its copper-responsive expression."; J. Biol. Chem. 266:15060-15067(1991).
[3]	X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). DOI=10.1006/jmbi.1995.0404; PubMed=7623381 [NCBI, ExPASy, EBI, Israel, Japan] Kerfeld C.A., Anwar H.P., Interrante R., Merchant S., Yeates T.O.; "The structure of chloroplast cytochrome c6 at 1.9-A resolution: evidence for functional oligomerization."; J. Mol. Biol. 250:627-647(1995).

Comments

FUNCTION: Functions as an electron carrier between membrane-bound cytochrome b6-f and photosystem I in oxygenic photosynthesis.
SUBUNIT: Monomer.
SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen.
PTM: Binds 1 heme group per subunit.
SIMILARITY: Belongs to the cytochrome c family. PetJ subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M67448; AAB00729.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J02774; AAA33081.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A27113; CCKM6R.

XP_001698242.1; -.

3D structure databases

PDB

1CYI; X-ray; 1.90 A; A=59-148.	[ExPASy / RCSB / EBI]
1CYJ; X-ray; 1.90 A; A=59-148.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1CYI; -.
1CYJ; -.

ModBase

P08197.

Ontologies

GO:0009507;	Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
GO:0009579;	Cellular component: thylakoid (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0022900;	Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0015979;	Biological process: photosynthesis (inferred from electronic annotation from UniProtKB-KW).
GO:0006810;	Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR009056; Cyt_c_monohaem.
IPR003088; Cyt_CI.
IPR008168; Cyt_CIC.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.760.10; Cytochrome_c_R; 1.

Pfam

PF00034; Cytochrom_C; 1.
Pfam graphical view of domain structure.

PRINTS

PR00605; CYTCHROMECIC.

PROSITE

PS51007; CYTC; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

5723799; -.

KEGG

cre:CHLREDRAFT_193170; -.

Other

P08197; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Chloroplast; Electron transport; Heme; Iron; Metal-binding; Photosynthesis; Plastid; Thylakoid; Transit peptide; Transport.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 58`	`58`	`Chloroplast.`
`CHAIN`	`59 148`	`90`	`Cytochrome c6, chloroplastic.`	`PRO_0000023850`
`METAL`	`76 76`		`Iron (heme axial ligand).`
`METAL`	`118 118`		`Iron (heme axial ligand).`
`BINDING`	`72 72`		`Heme (covalent).`
`BINDING`	`75 75`		`Heme (covalent).`
`CONFLICT`	`107 107`		`I -> S (in Ref. 1; AAA33081).`
`HELIX`	`61 71`	`11`
`HELIX`	`73 76`	`4`
`HELIX`	`77 79`	`3`
`STRAND`	`82 84`	`3`
`HELIX`	`91 97`	`7`
`HELIX`	`104 113`	`10`
`TURN`	`122 124`	`3`
`HELIX`	`127 143`	`17`

Sequence information

Length: 148 AA [This is the length of the unprocessed precursor]

Molecular weight: 15427 Da [This is the MW of the unprocessed precursor]

CRC64: 091567E642F457E8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLQLANRSVR AKAARASQSA RSVSCAAAKR GADVAPLTSA LAVTASILLT TGAASASAAD 

        70         80         90        100        110        120 
LALGAQVFNG NCAACHMGGR NSVMPEKTLD KAALEQYLDG GFKVESIIYQ VENGKGAMPA 

       130        140 
WADRLSEEEI QAVAEYVFKQ ATDAAWKY

P08197 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools