P00289 (PLAS_SPIOL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Plastocyanin, chloroplastic

Gene names

Name:

PETE

Organism

Spinacia oleracea (Spinach)

Taxonomic identifier

3562 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Amaranthaceae › Spinacia

Protein attributes

Sequence length	168 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I.
Subcellular location	Plastid › chloroplast thylakoid membrane; Peripheral membrane protein; Lumenal side Ref.3.
Sequence similarities	Contains 1 plastocyanin-like domain.

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Chloroplast Membrane Plastid Thylakoid
Domain	Transit peptide
Ligand	Copper Metal-binding
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast thylakoid membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	copper ion binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 69

69

Chloroplast Ref.2 Ref.3

Chain

70 – 168

99

Plastocyanin, chloroplastic

PRO_0000002897

Regions

Domain

70 – 168

99

Plastocyanin-like

Sites

Metal binding

106

1

Copper

Metal binding

153

1

Copper

Metal binding

156

1

Copper

Metal binding

161

1

Copper

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

168

Helix Strand Turn

Details...

Beta strand

71 – 75

5

Beta strand

83 – 90

8

Beta strand

95 – 100

6

Helix

112 – 114

3

Helix

121 – 124

4

Beta strand

138 – 142

5

Beta strand

147 – 152

6

Helix

154 – 156

3

Turn

157 – 160

4

Beta strand

162 – 167

6

Sequences

	Sequence		Length	Mass (Da)
	P00289 [UniParc]. Last modified April 1, 1990. Version 2. Checksum: F9AAA77D7EFCDBE0	FASTA	168	16,917
	10 20 30 40 50 60 MATVASSAAV AVPSFTGLKA SGSIKPTTAK IIPTTTAVPR LSVKASLKNV GAAVVATAAA 70 80 90 100 110 120 GLLAGNAMAV EVLLGGGDGS LAFLPGDFSV ASGEEIVFKN NAGFPHNVVF DEDEIPSGVD 130 140 150 160 AAKISMSEED LLNAPGETYK VTLTEKGTYK FYCSPHQGAG MVGKVTVN

References

[1]	"Plastocyanin is encoded by an uninterrupted nuclear gene in spinach." Rother C., Jansen T., Tyagi A., Tittgen J., Herrmann R.G. Curr. Genet. 11:171-176(1986) [PubMed: 2834087] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The amino acid sequence of plastocyanin from spinach. (Spinacia oleracea L.)." Scawen M.D., Ramshaw J.A.M., Boulter D. Biochem. J. 147:343-349(1975) [PubMed: 1180895] [Abstract] Cited for: PROTEIN SEQUENCE OF 70-168.
[3]	"Proteome map of the chloroplast lumen of Arabidopsis thaliana." Schubert M., Petersson U.A., Haas B.J., Funk C., Schroeder W.P., Kieselbach T. J. Biol. Chem. 277:8354-8365(2002) [PubMed: 11719511] [Abstract] Cited for: PROTEIN SEQUENCE OF 70-76, SUBCELLULAR LOCATION. Tissue: Leaf.
[4]	"The structure of the complex of plastocyanin and cytochrome f, determined by paramagnetic NMR and restrained rigid-body molecular dynamics." Ubbink M., Ejdebaeck M., Karlsson B.G., Bendall D.S. Structure 6:323-335(1998) [PubMed: 9551554] [Abstract] Cited for: STRUCTURE BY NMR.
[5]	"Crystal structure of spinach plastocyanin at 1.7-A resolution." Xue Y., Okvist M., Hansson O., Young S. Protein Sci. 7:2099-2105(1998) [PubMed: 9792096] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 70-168.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X04693 Genomic DNA. Translation: CAA28398.1.

PIR

CUSP. S00446.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AG6	X-ray	1.60	A	70-168	[»]
1OOW	X-ray	2.00	A	70-168	[»]
1TEF	X-ray	1.90	A/B	70-168	[»]
1TEG	X-ray	1.96	A/B	70-168	[»]
1YLB	NMR	-	B	70-168	[»]
2PCF	NMR	-	A	70-168	[»]

ProteinModelPortal

P00289.

SMR

P00289. Positions 70-168.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-4821.

Family and domain databases

InterPro

IPR000923. BlueCu_1.
IPR001235. Copper_blue.
IPR008972. Cupredoxin.
IPR002387. Plastocyanin.
[Graphical view]

Gene3D

G3DSA:2.60.40.420. Cupredoxin. 1 hit.

Pfam

PF00127. Copper-bind. 1 hit.
[Graphical view]

PRINTS

PR00156. COPPERBLUE.
PR00157. PLASTOCYANIN.

SUPFAM

SSF49503. Cupredoxin. 1 hit.

TIGRFAMs

TIGR02656. Cyanin_plasto. 1 hit.

PROSITE

PS00196. COPPER_BLUE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PLAS_SPIOL

Accession

Primary (citable) accession number: P00289

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	April 1, 1990
Last modified:	May 31, 2011
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program