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Umecyanin (UMC)

 UMEC_ARMRU              Reviewed;         115 AA.
P42849;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
12-SEP-2018, entry version 89.
RecName: Full=Umecyanin {ECO:0000303|PubMed:5490233};
Short=UMC {ECO:0000303|PubMed:15631465};
Armoracia rusticana (Horseradish) (Armoracia laphatifolia).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Cardamineae;
Armoracia.
NCBI_TaxID=3704;
[1]
PROTEIN SEQUENCE, VARIANT ILE-48, GLYCOSYLATION AT ASN-76,
HYDROXYLATION AT PRO-113, AND DISULFIDE BOND.
TISSUE=Root;
PubMed=7757010; DOI=10.1002/pro.5560040208;
van Driessche G., Dennison C., Sykes A.G., van Beeumen J.;
"Heterogeneity of the covalent structure of the blue copper protein
umecyanin from horseradish roots.";
Protein Sci. 4:209-227(1995).
[2]
IDENTIFICATION.
PubMed=5490233;
Paul K.G., Stigbrand T.;
"Umecyanin, a novel intensely blue copper protein from horseradish
root.";
Biochim. Biophys. Acta 221:255-263(1970).
[3]
PURIFICATION, FUNCTION, COFACTOR, AND GLYCOSYLATION.
PubMed=5089608;
Stigbrand T.;
"Structural properties of umecyanin. A copper protein from horseradish
root.";
Biochim. Biophys. Acta 236:246-252(1971).
[4]
FUNCTION.
PubMed=11945593; DOI=10.1016/0014-5793(71)80192-8;
Stigbrand T., Malmstroem B.G., Vaenngaard T.;
"On the state of copper in the blue protein umecyanin.";
FEBS Lett. 12:260-262(1971).
[5]
COFACTOR.
PubMed=4624162;
Stigbrand T., Sjoeholm I.;
"Circular dichroism studies on the copper protein umecyanin.";
Biochim. Biophys. Acta 263:244-257(1972).
[6]
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=5085267; DOI=10.1016/0014-5793(72)80279-5;
Stigbrand T.;
"Oxidation-reduction potential of umecyanin.";
FEBS Lett. 23:41-43(1972).
[7]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH COPPER IONS,
DISULFIDE BOND, COFACTOR, AND COPPER-BINDING SITES.
TISSUE=Root;
PubMed=15631465; DOI=10.1021/ja046184p;
Koch M., Velarde M., Harrison M.D., Echt S., Fischer M.,
Messerschmidt A., Dennison C.;
"Crystal structures of oxidized and reduced stellacyanin from
horseradish roots.";
J. Am. Chem. Soc. 127:158-166(2005).
-!- FUNCTION: 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). {ECO:0000269|PubMed:11945593,
ECO:0000269|PubMed:5089608}.
-!- COFACTOR:
Name=Cu cation; Xref=ChEBI:CHEBI:23378;
Evidence={ECO:0000269|PubMed:15631465,
ECO:0000269|PubMed:4624162, ECO:0000269|PubMed:5089608};
Note=Binds 1 copper ion per subunit. {ECO:0000269|PubMed:5089608};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Redox potential:
E(0) is +283 mV at pH 7.0. {ECO:0000269|PubMed:5085267};
-!- PTM: Glycosylated at Asn-76 (PubMed:7757010). The carbohydrate
content was determined to be 1.2%, corresponding to one hexose
sugar per molecule (PubMed:5089608). {ECO:0000269|PubMed:5089608,
ECO:0000269|PubMed:7757010}.
-!- PTM: Strongly heterogeneous at the C-terminus with the majority of
the chains ending at position 106. {ECO:0000269|PubMed:7757010}.
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PIR; A55827; A55827.
PDB; 1X9R; X-ray; 1.90 A; A/B=1-115.
PDB; 1X9U; X-ray; 1.80 A; A/B=1-115.
PDBsum; 1X9R; -.
PDBsum; 1X9U; -.
ProteinModelPortal; P42849; -.
SMR; P42849; -.
iPTMnet; P42849; -.
EvolutionaryTrace; P42849; -.
GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
Gene3D; 2.60.40.420; -; 1.
InterPro; IPR028871; BlueCu_1_BS.
InterPro; IPR008972; Cupredoxin.
InterPro; IPR039391; Phytocyanin.
InterPro; IPR003245; Phytocyanin_dom.
PANTHER; PTHR33021; PTHR33021; 1.
Pfam; PF02298; Cu_bind_like; 1.
ProDom; PD003122; Plcyanin-like; 1.
SUPFAM; SSF49503; SSF49503; 1.
PROSITE; PS00196; COPPER_BLUE; 1.
PROSITE; PS51485; PHYTOCYANIN; 1.
1: Evidence at protein level;
3D-structure; Copper; Direct protein sequencing; Disulfide bond;
Electron transport; Glycoprotein; Hydroxylation; Metal-binding;
Polymorphism; Transport.
CHAIN 1 115 Umecyanin.
/FTId=PRO_0000085557.
DOMAIN 1 103 Phytocyanin. {ECO:0000255|PROSITE-
ProRule:PRU00818}.
COMPBIAS 103 110 Gly-rich.
METAL 44 44 Copper. {ECO:0000269|PubMed:15631465}.
METAL 85 85 Copper. {ECO:0000269|PubMed:15631465}.
METAL 90 90 Copper. {ECO:0000269|PubMed:15631465}.
METAL 95 95 Copper. {ECO:0000269|PubMed:15631465}.
MOD_RES 113 113 Hydroxyproline.
{ECO:0000269|PubMed:7757010}.
CARBOHYD 76 76 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:7757010}.
DISULFID 57 91 {ECO:0000255|PROSITE-ProRule:PRU00818,
ECO:0000269|PubMed:15631465,
ECO:0000269|PubMed:7757010}.
VARIANT 48 48 V -> I (in 25% of the molecules).
{ECO:0000269|PubMed:7757010}.
STRAND 2 4 {ECO:0000244|PDB:1X9U}.
HELIX 7 9 {ECO:0000244|PDB:1X9U}.
HELIX 19 24 {ECO:0000244|PDB:1X9U}.
STRAND 34 37 {ECO:0000244|PDB:1X9U}.
TURN 41 43 {ECO:0000244|PDB:1X9U}.
STRAND 46 49 {ECO:0000244|PDB:1X9U}.
HELIX 51 55 {ECO:0000244|PDB:1X9U}.
STRAND 63 66 {ECO:0000244|PDB:1X9U}.
STRAND 68 74 {ECO:0000244|PDB:1X9U}.
STRAND 79 84 {ECO:0000244|PDB:1X9U}.
TURN 88 94 {ECO:0000244|PDB:1X9U}.
STRAND 96 102 {ECO:0000244|PDB:1X9U}.
SEQUENCE 115 AA; 12372 MW; 72B52EBDECAF1C6B CRC64;
EDYDVGGDME WKRPSDPKFY ITWATGKTFR VGDELEFDFA AGMHDVAVVT KDAFDNCKKE
NPISHMTTPP VKIMLNTTGP QYYICTVGDH CRVGQKLSIN VVGAGGAGGG ATPGA


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