ID   UMEC_ARMRU              Reviewed;         115 AA.
AC   P42849;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Umecyanin {ECO:0000303|PubMed:5490233};
DE            Short=UMC {ECO:0000303|PubMed:15631465};
OS   Armoracia rusticana (Horseradish) (Armoracia laphatifolia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Cardamineae; Armoracia.
OX   NCBI_TaxID=3704;
RN   [1]
RP   PROTEIN SEQUENCE, VARIANT ILE-48, GLYCOSYLATION AT ASN-76, HYDROXYLATION AT
RP   PRO-113, AND DISULFIDE BOND.
RC   TISSUE=Root;
RX   PubMed=7757010; DOI=10.1002/pro.5560040208;
RA   van Driessche G., Dennison C., Sykes A.G., van Beeumen J.;
RT   "Heterogeneity of the covalent structure of the blue copper protein
RT   umecyanin from horseradish roots.";
RL   Protein Sci. 4:209-227(1995).
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=5490233; DOI=10.1016/0005-2795(70)90265-5;
RA   Paul K.G., Stigbrand T.;
RT   "Umecyanin, a novel intensely blue copper protein from horseradish root.";
RL   Biochim. Biophys. Acta 221:255-263(1970).
RN   [3]
RP   PURIFICATION, FUNCTION, COFACTOR, AND GLYCOSYLATION.
RX   PubMed=5089608; DOI=10.1016/0005-2795(71)90173-5;
RA   Stigbrand T.;
RT   "Structural properties of umecyanin. A copper protein from horseradish
RT   root.";
RL   Biochim. Biophys. Acta 236:246-252(1971).
RN   [4]
RP   FUNCTION.
RX   PubMed=11945593; DOI=10.1016/0014-5793(71)80192-8;
RA   Stigbrand T., Malmstroem B.G., Vaenngaard T.;
RT   "On the state of copper in the blue protein umecyanin.";
RL   FEBS Lett. 12:260-262(1971).
RN   [5]
RP   COFACTOR.
RX   PubMed=4624162; DOI=10.1016/0005-2795(72)90077-3;
RA   Stigbrand T., Sjoeholm I.;
RT   "Circular dichroism studies on the copper protein umecyanin.";
RL   Biochim. Biophys. Acta 263:244-257(1972).
RN   [6]
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=5085267; DOI=10.1016/0014-5793(72)80279-5;
RA   Stigbrand T.;
RT   "Oxidation-reduction potential of umecyanin.";
RL   FEBS Lett. 23:41-43(1972).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH COPPER IONS,
RP   DISULFIDE BOND, COFACTOR, AND COPPER-BINDING SITES.
RC   TISSUE=Root;
RX   PubMed=15631465; DOI=10.1021/ja046184p;
RA   Koch M., Velarde M., Harrison M.D., Echt S., Fischer M., Messerschmidt A.,
RA   Dennison C.;
RT   "Crystal structures of oxidized and reduced stellacyanin from horseradish
RT   roots.";
RL   J. Am. Chem. Soc. 127:158-166(2005).
CC   -!- FUNCTION: Probable electron transfer copper protein that serves as a
CC       direct electron donor (PubMed:5089608, PubMed:11945593). Does not show
CC       any activity towards ascorbic acid, p-phenylenediamine and several
CC       common 'classical' substrates for copper proteins (PubMed:5089608).
CC       {ECO:0000269|PubMed:11945593, ECO:0000269|PubMed:5089608}.
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000269|PubMed:15631465, ECO:0000269|PubMed:4624162,
CC         ECO:0000269|PubMed:5089608};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000269|PubMed:5089608};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Redox potential:
CC         E(0) is +283 mV at pH 7.0. {ECO:0000269|PubMed:5085267};
CC   -!- PTM: Glycosylated at Asn-76 (PubMed:7757010). The carbohydrate content
CC       was determined to be 1.2%, corresponding to one hexose sugar per
CC       molecule (PubMed:5089608). {ECO:0000269|PubMed:5089608,
CC       ECO:0000269|PubMed:7757010}.
CC   -!- PTM: Strongly heterogeneous at the C-terminus with the majority of the
CC       chains ending at position 106. {ECO:0000269|PubMed:7757010}.
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DR   PIR; A55827; A55827.
DR   PDB; 1X9R; X-ray; 1.90 A; A/B=1-115.
DR   PDB; 1X9U; X-ray; 1.80 A; A/B=1-115.
DR   PDBsum; 1X9R; -.
DR   PDBsum; 1X9U; -.
DR   AlphaFoldDB; P42849; -.
DR   SMR; P42849; -.
DR   iPTMnet; P42849; -.
DR   EvolutionaryTrace; P42849; -.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.420; -; 1.
DR   InterPro; IPR028871; BlueCu_1_BS.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR039391; Phytocyanin.
DR   InterPro; IPR003245; Phytocyanin_dom.
DR   PANTHER; PTHR33021; PTHR33021; 1.
DR   Pfam; PF02298; Cu_bind_like; 1.
DR   SUPFAM; SSF49503; SSF49503; 1.
DR   PROSITE; PS00196; COPPER_BLUE; 1.
DR   PROSITE; PS51485; PHYTOCYANIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Copper; Direct protein sequencing; Disulfide bond;
KW   Electron transport; Glycoprotein; Hydroxylation; Metal-binding; Transport.
FT   CHAIN           1..115
FT                   /note="Umecyanin"
FT                   /id="PRO_0000085557"
FT   DOMAIN          1..103
FT                   /note="Phytocyanin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT   BINDING         44
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000269|PubMed:15631465"
FT   BINDING         85
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000269|PubMed:15631465"
FT   BINDING         90
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000269|PubMed:15631465"
FT   BINDING         95
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000269|PubMed:15631465"
FT   MOD_RES         113
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:7757010"
FT   CARBOHYD        76
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:7757010"
FT   DISULFID        57..91
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00818,
FT                   ECO:0000269|PubMed:15631465, ECO:0000269|PubMed:7757010"
FT   VARIANT         48
FT                   /note="V -> I (in 25% of the molecules)"
FT                   /evidence="ECO:0000269|PubMed:7757010"
FT   STRAND          2..4
FT                   /evidence="ECO:0007829|PDB:1X9U"
FT   HELIX           7..9
FT                   /evidence="ECO:0007829|PDB:1X9U"
FT   HELIX           19..24
FT                   /evidence="ECO:0007829|PDB:1X9U"
FT   STRAND          34..37
FT                   /evidence="ECO:0007829|PDB:1X9U"
FT   TURN            41..43
FT                   /evidence="ECO:0007829|PDB:1X9U"
FT   STRAND          46..49
FT                   /evidence="ECO:0007829|PDB:1X9U"
FT   HELIX           51..55
FT                   /evidence="ECO:0007829|PDB:1X9U"
FT   STRAND          63..66
FT                   /evidence="ECO:0007829|PDB:1X9U"
FT   STRAND          68..74
FT                   /evidence="ECO:0007829|PDB:1X9U"
FT   STRAND          79..84
FT                   /evidence="ECO:0007829|PDB:1X9U"
FT   TURN            88..94
FT                   /evidence="ECO:0007829|PDB:1X9U"
FT   STRAND          96..102
FT                   /evidence="ECO:0007829|PDB:1X9U"
SQ   SEQUENCE   115 AA;  12372 MW;  72B52EBDECAF1C6B CRC64;
     EDYDVGGDME WKRPSDPKFY ITWATGKTFR VGDELEFDFA AGMHDVAVVT KDAFDNCKKE
     NPISHMTTPP VKIMLNTTGP QYYICTVGDH CRVGQKLSIN VVGAGGAGGG ATPGA