LPR2_ARATH
ID LPR2_ARATH Reviewed; 581 AA.
AC Q949X9; Q8W4N2; Q9C9A4;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Multicopper oxidase LPR2;
DE EC=1.-.-.-;
DE AltName: Full=Protein LOW PHOSPHATE ROOT 2;
DE Flags: Precursor;
GN Name=LPR2; OrderedLocusNames=At1g71040; ORFNames=F23N20.3;
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 [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 [2]
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 [3]
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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Sha;
RX PubMed=17496893; DOI=10.1038/ng2041;
RA Svistoonoff S., Creff A., Reymond M., Sigoillot-Claude C., Ricaud L.,
RA Blanchet A., Nussaume L., Desnos T.;
RT "Root tip contact with low-phosphate media reprograms plant root
RT architecture.";
RL Nat. Genet. 39:792-796(2007).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=19666499; DOI=10.1073/pnas.0901778106;
RA Ticconi C.A., Lucero R.D., Sakhonwasee S., Adamson A.W., Creff A.,
RA Nussaume L., Desnos T., Abel S.;
RT "ER-resident proteins PDR2 and LPR1 mediate the developmental response of
RT root meristems to phosphate availability.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:14174-14179(2009).
CC -!- FUNCTION: Multicopper oxidase that may be involved in copper
CC homeostasis and oxidative stress response, and that is necessary for
CC root growth inhibition by low phosphate conditions. Functions together
CC with LPR1 and PDR2 in a common pathway that adjusts root meristem
CC activity to phosphate availability. {ECO:0000269|PubMed:17496893,
CC ECO:0000269|PubMed:19666499}.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:P37064};
CC Note=Binds 4 Cu cations per monomer. The Cu cations are bound as 3
CC distinct Cu centers known as type 1 or blue, type 2 or normal, and type
CC 3 or coupled binuclear. {ECO:0000250|UniProtKB:P37064};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:19666499}; Peripheral membrane protein
CC {ECO:0000305|PubMed:19666499}. Note=Associates with PDR2 at the ER
CC membrane. {ECO:0000305|PubMed:19666499}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants have reduced inhibition of primary root
CC growth in low inorganic phosphate conditions.
CC {ECO:0000269|PubMed:17496893, ECO:0000269|PubMed:19666499}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51692.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC016972; AAG51692.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35155.1; -; Genomic_DNA.
DR EMBL; AY050818; AAK92753.1; -; mRNA.
DR EMBL; AY062464; AAL32542.1; -; mRNA.
DR EMBL; AY091420; AAM14359.1; -; mRNA.
DR PIR; G96734; G96734.
DR RefSeq; NP_565008.1; NM_105773.3.
DR AlphaFoldDB; Q949X9; -.
DR SMR; Q949X9; -.
DR STRING; 3702.AT1G71040.1; -.
DR PaxDb; Q949X9; -.
DR PRIDE; Q949X9; -.
DR ProteomicsDB; 238608; -.
DR EnsemblPlants; AT1G71040.1; AT1G71040.1; AT1G71040.
DR GeneID; 843444; -.
DR Gramene; AT1G71040.1; AT1G71040.1; AT1G71040.
DR KEGG; ath:AT1G71040; -.
DR Araport; AT1G71040; -.
DR TAIR; locus:2026326; AT1G71040.
DR eggNOG; ENOG502QR4X; Eukaryota.
DR HOGENOM; CLU_009100_4_2_1; -.
DR InParanoid; Q949X9; -.
DR OMA; NASHPVH; -.
DR OrthoDB; 525810at2759; -.
DR PhylomeDB; Q949X9; -.
DR PRO; PR:Q949X9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q949X9; baseline and differential.
DR Genevisible; Q949X9; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IMP:TAIR.
DR GO; GO:0010073; P:meristem maintenance; IGI:TAIR.
DR Gene3D; 2.60.40.420; -; 3.
DR InterPro; IPR001117; Cu-oxidase.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR008972; Cupredoxin.
DR PANTHER; PTHR11709; PTHR11709; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR SUPFAM; SSF49503; SSF49503; 3.
PE 2: Evidence at transcript level;
KW Copper; Endoplasmic reticulum; Glycoprotein; Membrane; Metal-binding;
KW Oxidoreductase; Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..581
FT /note="Multicopper oxidase LPR2"
FT /id="PRO_0000429268"
FT DOMAIN 274..361
FT /note="Plastocyanin-like"
FT BINDING 150
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250|UniProtKB:P37064"
FT BINDING 152
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:P37064"
FT BINDING 198
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:P37064"
FT BINDING 200
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:P37064"
FT BINDING 466
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:P37064"
FT BINDING 469
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250|UniProtKB:P37064"
FT BINDING 471
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:P37064"
FT BINDING 562
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:P37064"
FT BINDING 563
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:P37064"
FT BINDING 564
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:P37064"
FT BINDING 568
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:P37064"
FT BINDING 573
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:P37064"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 511
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 436
FT /note="N -> K (in Ref. 3; AAL32542)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 581 AA; 66165 MW; 64873E43FEC24FBD CRC64;
MEPSRRRMTR DMLLLIVTMA WLVTGDEGGI KQEERLFNLG KLEMFVDKLP HIPTLHGYHF
VNGFLKPKSL HIGMFFKKWK FHRDLPATPV FAYGTSKRSA TVPGPTIEAV YGVDTYVTWR
NHLPLHHILP WDPTISPAIP KHGGIPTVVH LHGGIHEPTS DGNADSWFTA GFKETGSKWT
KKTTHYVNKQ QPGNMWYHDH AAGLTRVNLL AGLLGSYILR HSSVESPLRL PTGREFDRPL
VIFDRSFRKD GSIYMNATGN NPTIHPQWQP EYFGDAIIVN GKAWPRLTVR RRKYRFRITN
ASNARFFRFF FSNGLDFIVV GSDSAYLAKP VSTKSVLLAP SEIVDVLVDF SKSTSKTAIL
ANNAPYPYPS GDPVTEENSK VMKFIINYKS EVDTSIIPKK LIEYPPAHVS TSTRTRYIAM
FEYVSSIDEP THLYINGLPY NAPVTETPKI GTSEVWEVIN LTEDNHPLHI HLGLFKVLEQ
TALVKSEEFI ECMTKRNDAV KCEISKYARG NKTAVTVHER GWKNVFKMMP GHVTKILVRF
SYIHSNESYS FDATQEPGYV YHCHILDHED NMMMRPFAMV L
