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Protein

Plastocyanin, chloroplastic

Gene

PETE

Organism
Spinacia oleracea (Spinach)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I.1 Publication

Cofactori

Cu2+1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi106 – 1061Copper; via pros nitrogen1 Publication
Metal bindingi153 – 1531Copper1 Publication
Metal bindingi156 – 1561Copper; via pros nitrogen1 Publication
Metal bindingi161 – 1611Copper1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

Copper, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-4821.

Names & Taxonomyi

Protein namesi
Recommended name:
Plastocyanin, chloroplastic
Gene namesi
Name:PETE
OrganismiSpinacia oleracea (Spinach)
Taxonomic identifieri3562 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Membrane, Plastid, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei? – 69Thylakoid
Transit peptidei1 – ?Chloroplast
Chaini70 – 16899Plastocyanin, chloroplasticPRO_0000002897Add
BLAST

Interactioni

Protein-protein interaction databases

IntActiP00289. 1 interaction.
MINTiMINT-1534146.

Structurei

Secondary structure

1
168
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi71 – 755Combined sources
Turni76 – 794Combined sources
Beta strandi83 – 908Combined sources
Beta strandi95 – 1006Combined sources
Beta strandi102 – 1043Combined sources
Beta strandi108 – 1103Combined sources
Helixi112 – 1143Combined sources
Helixi121 – 1244Combined sources
Beta strandi128 – 1303Combined sources
Beta strandi138 – 1425Combined sources
Beta strandi147 – 1526Combined sources
Helixi154 – 1563Combined sources
Turni157 – 1604Combined sources
Beta strandi162 – 1676Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AG6X-ray1.60A70-168[»]
1OOWX-ray2.00A70-168[»]
1TEFX-ray1.90A/B70-168[»]
1TEGX-ray1.96A/B70-168[»]
1YLBNMR-B70-168[»]
2PCFNMR-A70-168[»]
ProteinModelPortaliP00289.
SMRiP00289. Positions 70-168.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00289.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini70 – 16899Plastocyanin-likeAdd
BLAST

Sequence similaritiesi

Belongs to the plastocyanin family.Curated
Contains 1 plastocyanin-like domain.Curated

Keywords - Domaini

Transit peptide

Family and domain databases

Gene3Di2.60.40.420. 1 hit.
InterProiIPR000923. BlueCu_1.
IPR028871. BlueCu_1_BS.
IPR001235. Copper_blue_Plastocyanin.
IPR008972. Cupredoxin.
IPR002387. Plastocyanin.
[Graphical view]
PfamiPF00127. Copper-bind. 1 hit.
[Graphical view]
PRINTSiPR00156. COPPERBLUE.
PR00157. PLASTOCYANIN.
SUPFAMiSSF49503. SSF49503. 1 hit.
TIGRFAMsiTIGR02656. cyanin_plasto. 1 hit.
PROSITEiPS00196. COPPER_BLUE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00289-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATVASSAAV AVPSFTGLKA SGSIKPTTAK IIPTTTAVPR LSVKASLKNV
60 70 80 90 100
GAAVVATAAA GLLAGNAMAV EVLLGGGDGS LAFLPGDFSV ASGEEIVFKN
110 120 130 140 150
NAGFPHNVVF DEDEIPSGVD AAKISMSEED LLNAPGETYK VTLTEKGTYK
160
FYCSPHQGAG MVGKVTVN
Length:168
Mass (Da):16,917
Last modified:April 1, 1990 - v2
Checksum:iF9AAA77D7EFCDBE0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04693 Genomic DNA. Translation: CAA28398.1.
PIRiS00446. CUSP.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04693 Genomic DNA. Translation: CAA28398.1.
PIRiS00446. CUSP.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AG6X-ray1.60A70-168[»]
1OOWX-ray2.00A70-168[»]
1TEFX-ray1.90A/B70-168[»]
1TEGX-ray1.96A/B70-168[»]
1YLBNMR-B70-168[»]
2PCFNMR-A70-168[»]
ProteinModelPortaliP00289.
SMRiP00289. Positions 70-168.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP00289. 1 interaction.
MINTiMINT-1534146.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-4821.

Miscellaneous databases

EvolutionaryTraceiP00289.

Family and domain databases

Gene3Di2.60.40.420. 1 hit.
InterProiIPR000923. BlueCu_1.
IPR028871. BlueCu_1_BS.
IPR001235. Copper_blue_Plastocyanin.
IPR008972. Cupredoxin.
IPR002387. Plastocyanin.
[Graphical view]
PfamiPF00127. Copper-bind. 1 hit.
[Graphical view]
PRINTSiPR00156. COPPERBLUE.
PR00157. PLASTOCYANIN.
SUPFAMiSSF49503. SSF49503. 1 hit.
TIGRFAMsiTIGR02656. cyanin_plasto. 1 hit.
PROSITEiPS00196. COPPER_BLUE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 70-168, SUBCELLULAR LOCATION.
  3. 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] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, SUBCELLULAR LOCATION.
  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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 70-168 IN COMPLEX WITH COPPER, FUNCTION, COFACTOR, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiPLAS_SPIOL
AccessioniPrimary (citable) accession number: P00289
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1990
Last modified: May 11, 2016
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.