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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

Manual assertion based on experiment ini

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi44Copper1 Publication1
Metal bindingi85Copper1 Publication1
Metal bindingi90Copper1 Publication1
Metal bindingi95Copper1 Publication1

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000855571 – 115UmecyaninAdd BLAST115

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi57 ↔ 91PROSITE-ProRule annotation2 Publications
Glycosylationi76N-linked (GlcNAc...)1 Publication1
Modified residuei113Hydroxyproline1 Publication1

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

1115
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 4Combined sources3
Helixi7 – 9Combined sources3
Helixi19 – 24Combined sources6
Beta strandi34 – 37Combined sources4
Turni41 – 43Combined sources3
Beta strandi46 – 49Combined sources4
Helixi51 – 55Combined sources5
Beta strandi63 – 66Combined sources4
Beta strandi68 – 74Combined sources7
Beta strandi79 – 84Combined sources6
Turni88 – 94Combined sources7
Beta strandi96 – 102Combined sources7

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP42849.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 103PhytocyaninPROSITE-ProRule annotationAdd BLAST103

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi103 – 110Gly-rich8

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)DescriptionActionsGraphical viewLength
Natural varianti48V → I in 25% of the molecules. 1 Publication1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1X9RX-ray1.90A/B1-115[»]
1X9UX-ray1.80A/B1-115[»]
ProteinModelPortaliP42849.
SMRiP42849.
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...

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: November 2, 2016
This is version 84 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.