BCB3_ARATH
ID BCB3_ARATH Reviewed; 222 AA.
AC Q96316;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Uclacyanin-3;
DE Short=Uclacyanin-III;
DE AltName: Full=Blue copper-binding protein III;
DE Short=BCB III;
DE AltName: Full=Phytocyanin 3;
DE Flags: Precursor;
GN Name=UCC3; OrderedLocusNames=At3g60280; ORFNames=F27H5.70;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, AND NOMENCLATURE.
RX PubMed=9761472; DOI=10.1002/pro.5560070907;
RA Nersissian A.M., Immoos C., Hill M.G., Hart P.J., Williams G.,
RA Herrmann R.G., Valentine J.S.;
RT "Uclacyanins, stellacyanins, and plantacyanins are distinct subfamilies of
RT phytocyanins: plant-specific mononuclear blue copper proteins.";
RL Protein Sci. 7:1915-1929(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.H., Cho Y.H., Hong Y.-N.;
RT "Isolation of blue copper-binding protein III cDNA in Arabidopsis
RT thaliana.";
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probably acts as an electron carrier involved in oxygen
CC activation and/or lignin formation. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC like-anchor {ECO:0000250}.
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DR EMBL; AF039404; AAC32461.1; -; mRNA.
DR EMBL; U65650; AAB07009.1; -; mRNA.
DR EMBL; AL163852; CAB87865.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80037.1; -; Genomic_DNA.
DR EMBL; BT025287; ABF19040.1; -; mRNA.
DR PIR; T49223; T49223.
DR RefSeq; NP_191587.1; NM_115892.4.
DR AlphaFoldDB; Q96316; -.
DR SMR; Q96316; -.
DR STRING; 3702.AT3G60280.1; -.
DR iPTMnet; Q96316; -.
DR MetOSite; Q96316; -.
DR PaxDb; Q96316; -.
DR ProteomicsDB; 240748; -.
DR EnsemblPlants; AT3G60280.1; AT3G60280.1; AT3G60280.
DR GeneID; 825199; -.
DR Gramene; AT3G60280.1; AT3G60280.1; AT3G60280.
DR KEGG; ath:AT3G60280; -.
DR Araport; AT3G60280; -.
DR TAIR; locus:2081957; AT3G60280.
DR eggNOG; ENOG502S1ER; Eukaryota.
DR HOGENOM; CLU_058719_2_1_1; -.
DR InParanoid; Q96316; -.
DR OMA; AFAKEHI; -.
DR OrthoDB; 1537588at2759; -.
DR PRO; PR:Q96316; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q96316; baseline and differential.
DR Genevisible; Q96316; AT.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0046658; C:anchored component of plasma membrane; IBA:GO_Central.
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; 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; PS51485; PHYTOCYANIN; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Copper; Disulfide bond; Electron transport; Glycoprotein;
KW GPI-anchor; Lipoprotein; Membrane; Metal-binding; Reference proteome;
KW Signal; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..198
FT /note="Uclacyanin-3"
FT /id="PRO_0000430148"
FT PROPEP 199..222
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000430149"
FT DOMAIN 22..120
FT /note="Phytocyanin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT REGION 121..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..195
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 61
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 102
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 107
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 112
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT LIPID 198
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 74..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
SQ SEQUENCE 222 AA; 22521 MW; 5C483A3A00584539 CRC64;
MGSTVAAALL LFLAAVPAVF AATFKVGDIS GWTSNLDYTV WLTGKTFRVG DTLEFVYGLS
HSVSVVDKAG YDNCDSSGAT QNFADGDTKI DLTTVGTMHF LCPTFGHCKN GMKLAVPVLA
AAPSPSTPSS PPSTPSTPSS PPSTPSTPSS PPSPPSPPSP SLPPSSLPPS ASPPTNGTPD
SETLTPPPAP LPPSLSPNAA SKGVMSYGII GVTMILMYAV MT
