BABL_ARATH
ID BABL_ARATH Reviewed; 129 AA.
AC Q8LG89; O64499; Q8S8T5;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Basic blue protein;
DE AltName: Full=Plantacyanin;
DE Flags: Precursor;
GN Name=ARPN; OrderedLocusNames=At2g02850; ORFNames=T17M13.2;
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].
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 [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 [3]
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 [4]
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 [5]
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 [6]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=15908590; DOI=10.1104/pp.105.063388;
RA Dong J., Kim S.T., Lord E.M.;
RT "Plantacyanin plays a role in reproduction in Arabidopsis.";
RL Plant Physiol. 138:778-789(2005).
RN [7]
RP INDUCTION BY COPPER.
RX PubMed=18408011; DOI=10.1074/jbc.m801406200;
RA Abdel-Ghany S.E., Pilon M.;
RT "MicroRNA-mediated systemic down-regulation of copper protein expression in
RT response to low copper availability in Arabidopsis.";
RL J. Biol. Chem. 283:15932-15945(2008).
RN [8]
RP INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=22174881; DOI=10.1371/journal.pone.0028729;
RA Maunoury N., Vaucheret H.;
RT "AGO1 and AGO2 act redundantly in miR408-mediated Plantacyanin
RT regulation.";
RL PLoS ONE 6:E28729-E28729(2011).
CC -!- FUNCTION: Forms a concentration gradient along the pollen tube growth
CC path, with a lower level in the stigma papilla cell wall and a higher
CC level in the transmitting tract extracellular matix of the style.
CC {ECO:0000269|PubMed:15908590}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:15908590}.
CC -!- TISSUE SPECIFICITY: Expressed in the inflorescence and in the
CC transmitting tract of the pistil. Detected in roots, stems, cauline
CC leaves, cotyledons, hypocotyls, guard cells, pistils, sepals, stamen
CC filaments and vascular bundles of roots but not of leaves. Not
CC expressed in petals, anthers or pollen. {ECO:0000269|PubMed:15908590}.
CC -!- DEVELOPMENTAL STAGE: Expressed in style and papilla cells when
CC pollination occurs. Detected in the mature embryo sacs of ovules before
CC and after fertilization. {ECO:0000269|PubMed:15908590}.
CC -!- INDUCTION: Down-regulated by microRNA 408 (miR408) via AGO1 and AGO2 in
CC response to low copper availability. {ECO:0000269|PubMed:18408011,
CC ECO:0000269|PubMed:22174881}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:15908590}.
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DR EMBL; U76297; AAC32449.1; -; Genomic_DNA.
DR EMBL; AC002521; AAM14843.1; -; Genomic_DNA.
DR EMBL; AC004138; AAC32906.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05633.1; -; Genomic_DNA.
DR EMBL; AF325063; AAK17131.1; -; mRNA.
DR EMBL; AY064141; AAL36048.1; -; mRNA.
DR EMBL; AY097407; AAM19923.1; -; mRNA.
DR EMBL; AY084407; AAM60981.1; -; mRNA.
DR PIR; F84441; F84441.
DR PIR; T00843; T00843.
DR RefSeq; NP_178388.1; NM_126340.3.
DR AlphaFoldDB; Q8LG89; -.
DR SMR; Q8LG89; -.
DR STRING; 3702.AT2G02850.1; -.
DR PaxDb; Q8LG89; -.
DR PRIDE; Q8LG89; -.
DR ProteomicsDB; 241119; -.
DR EnsemblPlants; AT2G02850.1; AT2G02850.1; AT2G02850.
DR GeneID; 814816; -.
DR Gramene; AT2G02850.1; AT2G02850.1; AT2G02850.
DR KEGG; ath:AT2G02850; -.
DR Araport; AT2G02850; -.
DR TAIR; locus:2056700; AT2G02850.
DR eggNOG; ENOG502S11U; Eukaryota.
DR HOGENOM; CLU_058719_4_1_1; -.
DR InParanoid; Q8LG89; -.
DR OMA; GHCESGT; -.
DR OrthoDB; 1514321at2759; -.
DR PhylomeDB; Q8LG89; -.
DR PRO; PR:Q8LG89; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8LG89; baseline and differential.
DR Genevisible; Q8LG89; AT.
DR GO; GO:0046658; C:anchored component of plasma membrane; IBA:GO_Central.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0031012; C:extracellular matrix; IDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; 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:0048653; P:anther development; IMP:TAIR.
DR GO; GO:0009856; P:pollination; IMP:TAIR.
DR CDD; cd11013; Plantacyanin; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR039391; Phytocyanin.
DR InterPro; IPR003245; Phytocyanin_dom.
DR InterPro; IPR041844; Plantacyanin.
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 Copper; Disulfide bond; Electron transport; Extracellular matrix;
KW Metal-binding; Reference proteome; Secreted; Signal; Transport.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..129
FT /note="Basic blue protein"
FT /id="PRO_0000002864"
FT DOMAIN 34..129
FT /note="Phytocyanin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT BINDING 72
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 BINDING 122
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT DISULFID 85..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
SQ SEQUENCE 129 AA; 14038 MW; 87536E196BBD65C3 CRC64;
MAKGRGSASW SARAIVTLMA VSVLLLQADY VQAATYTVGD SGIWTFNAVG WPKGKHFRAG
DVLVFNYNPR MHNVVKVDSG SYNNCKTPTG AKPYTSGKDR ITLSKGQNFF ICNFPNHCES
DMKIAVTAV
