BCB1_ARATH
ID BCB1_ARATH Reviewed; 196 AA.
AC Q07488; O82664;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Blue copper protein;
DE AltName: Full=Blue copper-binding protein;
DE Short=AtBCB;
DE AltName: Full=Phytocyanin 1;
DE AltName: Full=Stellacyanin;
DE Flags: Precursor;
GN Name=BCB; Synonyms=AWI 32; OrderedLocusNames=At5g20230; ORFNames=F5O24.120;
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia, and cv. Columbia K85;
RX PubMed=8294044; DOI=10.1016/0378-1119(93)90450-h;
RA van Gysel A., van Montagu M., Inze D.;
RT "A negatively light-regulated gene from Arabidopsis thaliana encodes a
RT protein showing high similarity to blue copper-binding proteins.";
RL Gene 136:79-85(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Wassilewskija;
RA Yang K.Y., Kim C.S., Cho B.H.;
RT "Characterization of a wound-inducible Arabidopsis gene encoding a protein
RT homologous to blue copper binding proteins.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=10769227; DOI=10.1242/dev.127.10.2021;
RA Honma T., Goto K.;
RT "The Arabidopsis floral homeotic gene PISTILLATA is regulated by discrete
RT cis-elements responsive to induction and maintenance signals.";
RL Development 127:2021-2030(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [5]
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 [6]
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 [7]
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 [8]
RP 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).
CC -!- FUNCTION: Probably acts as an electron carrier.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- DEVELOPMENTAL STAGE: Maximum levels are found in 35 day old plantlets
CC when the rosette is mature, consisting of 8-10 fully expanded leaves,
CC and as the floral stem starts to form. This level remains constant
CC during the further life span of the plant.
CC -!- INDUCTION: By dark adaptation. This gives a 20-fold increase in
CC expression.
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DR EMBL; Z15058; CAA78771.1; -; Genomic_DNA.
DR EMBL; Y18227; CAA77089.1; -; mRNA.
DR EMBL; AB035137; BAA86999.1; -; Genomic_DNA.
DR EMBL; AF296825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92816.1; -; Genomic_DNA.
DR EMBL; AY052681; AAK96585.1; -; mRNA.
DR EMBL; AY034986; AAK59491.1; -; mRNA.
DR EMBL; AY142577; AAN13146.1; -; mRNA.
DR EMBL; AY088549; AAM66081.1; -; mRNA.
DR PIR; I39698; I39698.
DR PIR; T51838; T51838.
DR RefSeq; NP_197523.1; NM_122030.4.
DR AlphaFoldDB; Q07488; -.
DR SMR; Q07488; -.
DR BioGRID; 17421; 63.
DR IntAct; Q07488; 62.
DR STRING; 3702.AT5G20230.1; -.
DR PaxDb; Q07488; -.
DR PRIDE; Q07488; -.
DR ProteomicsDB; 241131; -.
DR EnsemblPlants; AT5G20230.1; AT5G20230.1; AT5G20230.
DR GeneID; 832145; -.
DR Gramene; AT5G20230.1; AT5G20230.1; AT5G20230.
DR KEGG; ath:AT5G20230; -.
DR Araport; AT5G20230; -.
DR TAIR; locus:2149249; AT5G20230.
DR eggNOG; ENOG502S4BK; Eukaryota.
DR HOGENOM; CLU_058719_2_7_1; -.
DR InParanoid; Q07488; -.
DR OMA; NFESGSH; -.
DR OrthoDB; 1557663at2759; -.
DR PhylomeDB; Q07488; -.
DR PRO; PR:Q07488; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q07488; baseline and differential.
DR Genevisible; Q07488; 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:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015690; P:aluminum cation transport; IMP:TAIR.
DR GO; GO:0070417; P:cellular response to cold; IMP:TAIR.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:1901141; P:regulation of lignin biosynthetic process; IMP:TAIR.
DR GO; GO:0009646; P:response to absence of light; IEP:TAIR.
DR GO; GO:0002239; P:response to oomycetes; IEP:TAIR.
DR GO; GO:0006979; P:response to oxidative stress; TAS:TAIR.
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 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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..174
FT /note="Blue copper protein"
FT /id="PRO_0000002866"
FT PROPEP 175..196
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000002867"
FT DOMAIN 23..125
FT /note="Phytocyanin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT REGION 133..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 66
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT BINDING 107
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT BINDING 112
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT BINDING 117
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT LIPID 174
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 79..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT CONFLICT 44
FT /note="T -> S (in Ref. 1; CAA78771)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="P -> L (in Ref. 1; CAA78771)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="P -> L (in Ref. 1; CAA78771)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 196 AA; 20054 MW; 05100B50518F0A56 CRC64;
MAGVFKTVTF LVLVFAAVVV FAEDYDVGDD TEWTRPMDPE FYTTWATGKT FRVGDELEFD
FAAGRHDVAV VSEAAFENCE KEKPISHMTV PPVKIMLNTT GPQYFICTVG DHCRFGQKLS
ITVVAAGATG GATPGAGATP APGSTPSTGG TTPPTAGGTT TPSGSSGTTT PAGNAASSLG
GATFLVAFVS AVVALF
