ID PLAS2_ARATH Reviewed; 167 AA.
AC P42699; Q6UB15; Q8LD06; Q9LN26;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 24-JAN-2024, entry version 163.
DE RecName: Full=Plastocyanin major isoform, chloroplastic;
DE AltName: Full=DNA-damage-repair/toleration protein DRT112;
DE Flags: Precursor;
GN Name=DRT112; OrderedLocusNames=At1g20340;
GN ORFNames=F14O10.6, F14O10_4, K3F10TP;
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].
RC STRAIN=cv. Columbia;
RX PubMed=8479917; DOI=10.1093/nar/21.7.1647;
RA Pang Q., Hays J.B., Rajagopal I.;
RT "Two cDNAs from the plant Arabidopsis thaliana that partially restore
RT recombination proficiency and DNA-damage resistance to E. coli mutants
RT lacking recombination-intermediate-resolution activities.";
RL Nucleic Acids Res. 21:1647-1653(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 69-88,
RP CHARACTERIZATION, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=11034343; DOI=10.1016/s0014-5793(00)01890-1;
RA Kieselbach T., Bystedt M., Hynds P., Robinson C., Schroeder W.P.;
RT "A peroxidase homologue and novel plastocyanin located by proteomics to the
RT Arabidopsis chloroplast thylakoid lumen.";
RL FEBS Lett. 480:271-276(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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;
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 [GENOMIC DNA] OF 107-167.
RC STRAIN=cv. Columbia;
RA Strzalka W.K.;
RT "Plant/T-DNA junction of SALK_135199.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP PROTEIN SEQUENCE OF 69-97, AND SUBCELLULAR LOCATION.
RX PubMed=11719511; DOI=10.1074/jbc.m108575200;
RA Schubert M., Petersson U.A., Haas B.J., Funk C., Schroeder W.P.,
RA Kieselbach T.;
RT "Proteome map of the chloroplast lumen of Arabidopsis thaliana.";
RL J. Biol. Chem. 277:8354-8365(2002).
RN [9]
RP PROTEIN SEQUENCE OF N-TERMINUS, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11826309; DOI=10.1105/tpc.010304;
RA Peltier J.-B., Emanuelsson O., Kalume D.E., Ytterberg J., Friso G.,
RA Rudella A., Liberles D.A., Soederberg L., Roepstorff P., von Heijne G.,
RA van Wijk K.J.;
RT "Central functions of the lumenal and peripheral thylakoid proteome of
RT Arabidopsis determined by experimentation and genome-wide prediction.";
RL Plant Cell 14:211-236(2002).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
CC -!- FUNCTION: Participates in electron transfer between P700 and the
CC cytochrome b6-f complex in photosystem I. Seems to be the major
CC plastocyanin in Arabidopsis. {ECO:0000269|PubMed:11034343}.
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000250|UniProtKB:P18068};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:11034343, ECO:0000269|PubMed:11719511,
CC ECO:0000269|PubMed:18431481}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11034343}; Lumenal side
CC {ECO:0000269|PubMed:11034343}. Note=Loosely bound to the chloroplast
CC thylakoid inner membrane surface (PubMed:11034343).
CC -!- SIMILARITY: Belongs to the plastocyanin family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be involved in the resistance to UV
CC light and chemical DNA-damaging agents. {ECO:0000305|PubMed:8479917}.
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DR EMBL; M98456; AAA32787.1; -; mRNA.
DR EMBL; AJ271355; CAB66894.1; -; Genomic_DNA.
DR EMBL; AC026234; AAF88155.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29963.1; -; Genomic_DNA.
DR EMBL; AF324702; AAG40053.1; -; mRNA.
DR EMBL; AF326879; AAG41461.1; -; mRNA.
DR EMBL; AF334383; AAG50089.1; -; mRNA.
DR EMBL; AF361853; AAK32865.1; -; mRNA.
DR EMBL; BT001030; AAN46784.1; -; mRNA.
DR EMBL; AY086284; AAM64356.1; -; mRNA.
DR EMBL; AY374308; AAR15395.1; -; Genomic_DNA.
DR PIR; B86337; B86337.
DR PIR; PA0004; PA0004.
DR PIR; S33707; S33707.
DR RefSeq; NP_173459.1; NM_101885.3.
DR AlphaFoldDB; P42699; -.
DR SMR; P42699; -.
DR BioGRID; 23861; 2.
DR STRING; 3702.P42699; -.
DR PaxDb; 3702-AT1G20340-1; -.
DR ProteomicsDB; 235035; -.
DR EnsemblPlants; AT1G20340.1; AT1G20340.1; AT1G20340.
DR GeneID; 838622; -.
DR Gramene; AT1G20340.1; AT1G20340.1; AT1G20340.
DR KEGG; ath:AT1G20340; -.
DR Araport; AT1G20340; -.
DR TAIR; AT1G20340; DRT112.
DR eggNOG; ENOG502RXIY; Eukaryota.
DR HOGENOM; CLU_084115_0_0_1; -.
DR InParanoid; P42699; -.
DR OMA; YDYYCEP; -.
DR OrthoDB; 471748at2759; -.
DR PhylomeDB; P42699; -.
DR PRO; PR:P42699; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P42699; baseline and differential.
DR Genevisible; P42699; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0055035; C:plastid thylakoid membrane; IDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0031977; C:thylakoid lumen; HDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0046028; F:electron transporter, transferring electrons from cytochrome b6/f complex of photosystem II activity; IGI:CACAO.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0055070; P:copper ion homeostasis; IMP:TAIR.
DR GO; GO:0017148; P:negative regulation of translation; IMP:TAIR.
DR GO; GO:0046688; P:response to copper ion; IEP:TAIR.
DR CDD; cd04219; Plastocyanin; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 1.
DR InterPro; IPR000923; BlueCu_1.
DR InterPro; IPR028871; BlueCu_1_BS.
DR InterPro; IPR001235; Copper_blue_Plastocyanin.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR002387; Plastocyanin.
DR NCBIfam; TIGR02656; cyanin_plasto; 1.
DR PANTHER; PTHR34192; PLASTOCYANIN MAJOR ISOFORM, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR34192:SF10; PLASTOCYANIN MAJOR ISOFORM, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00127; Copper-bind; 1.
DR PRINTS; PR00156; COPPERBLUE.
DR PRINTS; PR00157; PLASTOCYANIN.
DR SUPFAM; SSF49503; Cupredoxins; 1.
DR PROSITE; PS00196; COPPER_BLUE; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Copper; Direct protein sequencing; Electron transport;
KW Membrane; Metal-binding; Plastid; Reference proteome; Thylakoid;
KW Transit peptide; Transport.
FT TRANSIT 1..52
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT 53..68
FT /note="Thylakoid"
FT /evidence="ECO:0000269|PubMed:11034343,
FT ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:11826309"
FT CHAIN 69..167
FT /note="Plastocyanin major isoform, chloroplastic"
FT /id="PRO_0000002885"
FT DOMAIN 69..167
FT /note="Plastocyanin-like"
FT BINDING 105
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P18068"
FT BINDING 152
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P18068"
FT BINDING 155
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P18068"
FT BINDING 160
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P18068"
FT CONFLICT 7
FT /note="A -> T (in Ref. 1; AAA32787)"
FT /evidence="ECO:0000305"
FT CONFLICT 10
FT /note="A -> P (in Ref. 1; AAA32787)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="I -> T (in Ref. 1; AAA32787)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="I -> T (in Ref. 1; AAA32787)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="A -> P (in Ref. 1; AAA32787)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="V -> I (in Ref. 6; AAM64356)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="V -> G (in Ref. 2; CAB66894)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 167 AA; 16984 MW; 00BE1D33D47E35D6 CRC64;
MASVTSATVA IPSFTGLKAS TIKSSATVRI QTAAVASPKL TVKSSLKNFG VAAVAAAASI
ALAGNAMAIE VLLGGGDGSL AFIPNDFSIA KGEKIVFKNN AGYPHNVVFD EDEIPSGVDV
AKISMDEQDL LNGAGETYEV ALTEPGTYSF YCAPHQGAGM VGKVTVN
//
