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Protein

Umecyanin

Gene
N/A
Organism
Armoracia rusticana (Horseradish) (Armoracia laphatifolia)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probable electron transfer copper protein that serves as a direct electron donor (PubMed:5089608, PubMed:11945593). Does not show any activity towards ascorbic acid, p-phenylenediamine and several common "classical" substrates for copper proteins (PubMed:5089608).2 Publications

Cofactori

Cu cation3 PublicationsNote: Binds 1 copper ion per subunit.1 Publication

Redox potential

E0 is +283 mV at pH 7.0.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi44 – 441Copper1 Publication
Metal bindingi85 – 851Copper1 Publication
Metal bindingi90 – 901Copper1 Publication
Metal bindingi95 – 951Copper1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Umecyanin1 Publication
Short name:
UMC1 Publication
OrganismiArmoracia rusticana (Horseradish) (Armoracia laphatifolia)
Taxonomic identifieri3704 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCardamineaeArmoracia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 115115UmecyaninPRO_0000085557Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi57 ↔ 91PROSITE-ProRule annotation2 Publications
Glycosylationi76 – 761N-linked (GlcNAc...)1 Publication
Modified residuei113 – 1131Hydroxyproline1 Publication

Post-translational modificationi

Glycosylated at Asn-76 (PubMed:7757010). The carbohydrate content was determined to be 1.2%, corresponding to one hexose sugar per molecule (PubMed:5089608).2 Publications
Strongly heterogeneous at the C-terminus with the majority of the chains ending at position 106.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Structurei

Secondary structure

1
115
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 43Combined sources
Helixi7 – 93Combined sources
Helixi19 – 246Combined sources
Beta strandi34 – 374Combined sources
Turni41 – 433Combined sources
Beta strandi46 – 494Combined sources
Helixi51 – 555Combined sources
Beta strandi63 – 664Combined sources
Beta strandi68 – 747Combined sources
Beta strandi79 – 846Combined sources
Turni88 – 947Combined sources
Beta strandi96 – 1027Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X9RX-ray1.90A/B1-115[»]
1X9UX-ray1.80A/B1-115[»]
ProteinModelPortaliP42849.
SMRiP42849. Positions 1-104.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42849.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 103103PhytocyaninPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi103 – 1108Gly-rich

Sequence similaritiesi

Contains 1 phytocyanin domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di2.60.40.420. 1 hit.
InterProiIPR028871. BlueCu_1_BS.
IPR008972. Cupredoxin.
IPR003245. Phytocyanin_dom.
[Graphical view]
PfamiPF02298. Cu_bind_like. 1 hit.
[Graphical view]
ProDomiPD003122. Plcyanin-like. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF49503. SSF49503. 1 hit.
PROSITEiPS00196. COPPER_BLUE. 1 hit.
PS51485. PHYTOCYANIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P42849-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
EDYDVGGDME WKRPSDPKFY ITWATGKTFR VGDELEFDFA AGMHDVAVVT
60 70 80 90 100
KDAFDNCKKE NPISHMTTPP VKIMLNTTGP QYYICTVGDH CRVGQKLSIN
110
VVGAGGAGGG ATPGA
Length:115
Mass (Da):12,372
Last modified:November 1, 1995 - v1
Checksum:i72B52EBDECAF1C6B
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti48 – 481V → I in 25% of the molecules. 1 Publication

Sequence databases

PIRiA55827.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

PIRiA55827.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X9RX-ray1.90A/B1-115[»]
1X9UX-ray1.80A/B1-115[»]
ProteinModelPortaliP42849.
SMRiP42849. Positions 1-104.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP42849.

Family and domain databases

Gene3Di2.60.40.420. 1 hit.
InterProiIPR028871. BlueCu_1_BS.
IPR008972. Cupredoxin.
IPR003245. Phytocyanin_dom.
[Graphical view]
PfamiPF02298. Cu_bind_like. 1 hit.
[Graphical view]
ProDomiPD003122. Plcyanin-like. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF49503. SSF49503. 1 hit.
PROSITEiPS00196. COPPER_BLUE. 1 hit.
PS51485. PHYTOCYANIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Heterogeneity of the covalent structure of the blue copper protein umecyanin from horseradish roots."
    van Driessche G., Dennison C., Sykes A.G., van Beeumen J.
    Protein Sci. 4:209-227(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, VARIANT ILE-48, GLYCOSYLATION AT ASN-76, HYDROXYLATION AT PRO-113, DISULFIDE BOND.
    Tissue: Root.
  2. "Umecyanin, a novel intensely blue copper protein from horseradish root."
    Paul K.G., Stigbrand T.
    Biochim. Biophys. Acta 221:255-263(1970) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  3. "Structural properties of umecyanin. A copper protein from horseradish root."
    Stigbrand T.
    Biochim. Biophys. Acta 236:246-252(1971) [PubMed] [Europe PMC] [Abstract]
    Cited for: PURIFICATION, FUNCTION, COFACTOR, GLYCOSYLATION.
  4. "On the state of copper in the blue protein umecyanin."
    Stigbrand T., Malmstroem B.G., Vaenngaard T.
    FEBS Lett. 12:260-262(1971) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Circular dichroism studies on the copper protein umecyanin."
    Stigbrand T., Sjoeholm I.
    Biochim. Biophys. Acta 263:244-257(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: COFACTOR.
  6. "Oxidation-reduction potential of umecyanin."
    Stigbrand T.
    FEBS Lett. 23:41-43(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
  7. "Crystal structures of oxidized and reduced stellacyanin from horseradish roots."
    Koch M., Velarde M., Harrison M.D., Echt S., Fischer M., Messerschmidt A., Dennison C.
    J. Am. Chem. Soc. 127:158-166(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH COPPER IONS, DISULFIDE BOND, COFACTOR, COPPER-BINDING SITES.
    Tissue: Root.

Entry informationi

Entry nameiUMEC_ARMRU
AccessioniPrimary (citable) accession number: P42849
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 11, 2016
This is version 82 of the entry and version 1 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.