P00299 (PLAS1_POPNI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Plastocyanin A, chloroplastic

Gene names

Name:

PETE

Organism

Populus nigra (Lombardy poplar)

Taxonomic identifier

3691 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Malpighiales › Salicaceae › Saliceae › Populus

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. Note: Loosely bound to the inner thylakoid membrane surface in chloroplasts.
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
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

Chain

70 – 168

99

Plastocyanin A, chloroplastic

PRO_0000002893

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

.

.

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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 – 123

3

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)
	P00299 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 901B21A7573DBF82	FASTA	168	17,020
	10 20 30 40 50 60 MATVTSAAVS IPSFTGLKAG SASNAKVSAS AKVSASPLPR LSIKASMKDV GAAVVATAAS 70 80 90 100 110 120 AMIASNAMAI DVLLGADDGS LAFVPSEFSI SPGEKIVFKN NAGFPHNIVF DEDSIPSGVD 130 140 150 160 ASKISMSEED LLNAKGETFE VALSNKGEYS FYCSPHQGAG MVGKVTVN

References

[1]	Reichert J., Jenzelewski V., Haehnel W. Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Italica. Tissue: Leaf.
[2]	"Elegance in molecular design: the copper site of photosynthetic electron-transfer protein." Freeman H.C. J. Proc. Royal Soc. N.S. Wales 112:45-62(1979) Cited for: PROTEIN SEQUENCE OF 70-168. Strain: cv. Italica.
[3]	"The crystal structure of poplar apoplastocyanin at 1.8-A resolution. The geometry of the copper-binding site is created by the polypeptide." Garrett T.P.J., Clingeleffer D.J., Guss J.M., Rogers S.J., Freeman H.C. J. Biol. Chem. 259:2822-2825(1984) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[4]	"Structure of oxidized poplar plastocyanin at 1.6-A resolution." Guss J.M., Freeman H.C. J. Mol. Biol. 169:521-563(1983) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
[5]	"X-ray crystal structure analysis of plastocyanin at 2.7-A resolution." Colman P.M., Freeman H.C., Guss J.M., Murata M., Norris V.A., Ramshaw J.A.M., Venkatappa M.P. Nature 272:319-324(1978) Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z50185 mRNA. Translation: CAA90564.1.

PIR

CUPX. S58209.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JXG	X-ray	1.60	A/B	70-168	[»]
1PLC	X-ray	1.33	A	70-168	[»]
1PNC	X-ray	1.60	A	70-168	[»]
1PND	X-ray	1.60	A	70-168	[»]
1TKW	NMR	-	A	70-168	[»]
2PCY	X-ray	1.80	A	70-168	[»]
3PCY	X-ray	1.90	A	70-168	[»]
4DP7	X-ray	1.08	X	70-168	[»]
4DP8	X-ray	1.07	X	70-168	[»]
4DP9	X-ray	1.00	X	70-168	[»]
4DPA	X-ray	1.05	X	70-168	[»]
4DPB	X-ray	1.00	X	70-168	[»]
4DPC	X-ray	1.06	X	70-168	[»]
4PCY	X-ray	2.15	A	70-168	[»]
5PCY	X-ray	1.80	A	70-168	[»]
6PCY	X-ray	1.90	A	70-168	[»]

ProteinModelPortal

P00299.

SMR

P00299. Positions 70-168.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

2.60.40.420. 1 hit.

InterPro

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

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...

Other

EvolutionaryTrace

P00299.

Entry information

Entry name

PLAS1_POPNI

Accession

Primary (citable) accession number: P00299

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program