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P00299 (PLAS1_POPNI) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Plastocyanin A, chloroplastic
Gene names
Name:PETE
OrganismPopulus nigra (Lombardy poplar)
Taxonomic identifier3691 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesSalicaceaeSaliceaePopulus

Protein attributes

Sequence length168 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I.

Subcellular location

Plastidchloroplast 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 processElectron transport
Transport
   Cellular componentChloroplast
Membrane
Plastid
Thylakoid
   DomainTransit peptide
   LigandCopper
Metal-binding
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processoxidation-reduction process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchloroplast thylakoid membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncopper ion binding

Inferred from electronic annotation. Source: InterPro

electron carrier activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6969Chloroplast Ref.2
Chain70 – 16899Plastocyanin A, chloroplastic
PRO_0000002893

Regions

Domain70 – 16899Plastocyanin-like

Sites

Metal binding1061Copper
Metal binding1531Copper
Metal binding1561Copper
Metal binding1611Copper

Secondary structure

.................... 168
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00299 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 901B21A7573DBF82

FASTA16817,020
        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 

« Hide

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.
PIRCUPX. S58209.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JXGX-ray1.60A/B70-168[»]
1PLCX-ray1.33A70-168[»]
1PNCX-ray1.60A70-168[»]
1PNDX-ray1.60A70-168[»]
1TKWNMR-A70-168[»]
2PCYX-ray1.80A70-168[»]
3PCYX-ray1.90A70-168[»]
4DP7X-ray1.08X70-168[»]
4DP8X-ray1.07X70-168[»]
4DP9X-ray1.00X70-168[»]
4DPAX-ray1.05X70-168[»]
4DPBX-ray1.00X70-168[»]
4DPCX-ray1.06X70-168[»]
4PCYX-ray2.15A70-168[»]
5PCYX-ray1.80A70-168[»]
6PCYX-ray1.90A70-168[»]
ProteinModelPortalP00299.
SMRP00299. Positions 70-168.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.40.420. 1 hit.
InterProIPR000923. BlueCu_1.
IPR028871. BlueCu_1_BS.
IPR001235. Copper_blue_Plastocyanin.
IPR008972. Cupredoxin.
IPR002387. Plastocyanin.
[Graphical view]
PfamPF00127. Copper-bind. 1 hit.
[Graphical view]
PRINTSPR00156. COPPERBLUE.
PR00157. PLASTOCYANIN.
SUPFAMSSF49503. SSF49503. 1 hit.
TIGRFAMsTIGR02656. cyanin_plasto. 1 hit.
PROSITEPS00196. COPPER_BLUE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00299.

Entry information

Entry namePLAS1_POPNI
AccessionPrimary (citable) accession number: P00299
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1996
Last modified: March 19, 2014
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references