BCB2_ARATH
ID BCB2_ARATH Reviewed; 202 AA.
AC O80517; O03987; O82082; Q39252; Q42071; Q8LDL7;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Uclacyanin-2;
DE AltName: Full=Blue copper-binding protein II;
DE Short=BCB II;
DE AltName: Full=Phytocyanin 2;
DE AltName: Full=Uclacyanin-II;
DE Flags: Precursor;
GN OrderedLocusNames=At2g44790; ORFNames=F16B22.32;
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, and cv. Landsberg erecta;
RA Kim C.H., Cho Y.H., Hong Y.-N.;
RT "Isolation of blue copper-binding protein II cDNA in Arabidopsis
RT thaliana.";
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-108.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT a set of 5000 non-redundant ESTs.";
RL Plant J. 9:101-124(1996).
CC -!- FUNCTION: Probably acts as an electron carrier involved in oxygen
CC activation and/or lignin formation.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC32039.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA81189.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U76299; AAC32039.1; ALT_FRAME; mRNA.
DR EMBL; U90428; AAB50232.1; -; Genomic_DNA.
DR EMBL; U57320; AAB47973.1; -; mRNA.
DR EMBL; AC003672; AAC27480.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10467.1; -; Genomic_DNA.
DR EMBL; AY049292; AAK83634.1; -; mRNA.
DR EMBL; AY093758; AAM10382.1; -; mRNA.
DR EMBL; AY085929; AAM63141.1; -; mRNA.
DR EMBL; Z26202; CAA81189.1; ALT_FRAME; mRNA.
DR PIR; T01605; T01605.
DR PIR; T52408; T52408.
DR PIR; T52409; T52409.
DR PIR; T52410; T52410.
DR RefSeq; NP_182006.1; NM_130043.3.
DR AlphaFoldDB; O80517; -.
DR SMR; O80517; -.
DR BioGRID; 4424; 3.
DR IntAct; O80517; 1.
DR STRING; 3702.AT2G44790.1; -.
DR PaxDb; O80517; -.
DR PRIDE; O80517; -.
DR ProteomicsDB; 240747; -.
DR EnsemblPlants; AT2G44790.1; AT2G44790.1; AT2G44790.
DR GeneID; 819088; -.
DR Gramene; AT2G44790.1; AT2G44790.1; AT2G44790.
DR KEGG; ath:AT2G44790; -.
DR Araport; AT2G44790; -.
DR TAIR; locus:2042426; AT2G44790.
DR eggNOG; ENOG502S1ER; Eukaryota.
DR HOGENOM; CLU_058719_2_5_1; -.
DR InParanoid; O80517; -.
DR OMA; TGDYSTW; -.
DR OrthoDB; 1514321at2759; -.
DR PhylomeDB; O80517; -.
DR PRO; PR:O80517; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80517; baseline and differential.
DR Genevisible; O80517; AT.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
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; Electron transport; Glycoprotein; GPI-anchor;
KW Lipoprotein; Membrane; Metal-binding; Reference proteome; Signal;
KW Transport.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..178
FT /note="Uclacyanin-2"
FT /id="PRO_0000002868"
FT PROPEP 179..202
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000002869"
FT DOMAIN 30..126
FT /note="Phytocyanin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT REGION 129..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..178
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 65
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT BINDING 106
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT BINDING 111
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT BINDING 118
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT LIPID 178
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 113..114
FT /note="RT -> SL (in strain: cv. Landsberg erecta)"
FT CONFLICT 80
FT /note="A -> G (in Ref. 2; AAB47973)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="P -> T (in Ref. 2; AAB47973)"
FT /evidence="ECO:0000305"
FT CONFLICT 113..115
FT /note="RTN -> S (in Ref. 1; AAC32039 and 2; AAB47973)"
FT /evidence="ECO:0000305"
FT CONFLICT 130..133
FT /note="GPPA -> DLR (in Ref. 2; AAB50232/AAB47973)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 202 AA; 20354 MW; 571122127BDEBAF6 CRC64;
MAMNGLSKMA VAAATALLLV LTIVPGAVAV TYTIEWTTGV DYSGWATGKT FRVGDILEFK
YGSSHTVDVV DKAGYDGCDA SSSTENHSDG DTKIDLKTVG INYFICSTPG HCRTNGGMKL
AVNVVAGSAG PPATPTPPSS TPGTPTTPES PPSGGSPTPT TPTPGAGSTS PPPPPKASGA
SKGVMSYVLV GVSMVLGYGL WM
