LPR1_ARATH
ID LPR1_ARATH Reviewed; 581 AA.
AC F4I4K5; O23123; Q8GXX3;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Multicopper oxidase LPR1;
DE EC=1.-.-.-;
DE AltName: Full=Protein LOW PHOSPHATE ROOT 1;
DE Flags: Precursor;
GN Name=LPR1; OrderedLocusNames=At1g23010; ORFNames=F19G10.5;
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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 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 [6]
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 LPR2 and PDR2 in a common pathway that adjusts root meristem
CC activity to phosphate availability. Oxidizes the substrate 2,2'-
CC azinobis-(3-ethylbenzthiazoline-6-sulphonate) in vitro.
CC {ECO:0000269|PubMed:17496893, 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=AAB72167.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF000657; AAB72167.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE30321.1; -; Genomic_DNA.
DR EMBL; AK117988; BAC42623.1; -; mRNA.
DR EMBL; BT005929; AAO64864.1; -; mRNA.
DR PIR; B86364; B86364.
DR RefSeq; NP_173714.2; NM_102149.4.
DR AlphaFoldDB; F4I4K5; -.
DR SMR; F4I4K5; -.
DR STRING; 3702.AT1G23010.1; -.
DR PaxDb; F4I4K5; -.
DR PRIDE; F4I4K5; -.
DR ProteomicsDB; 238669; -.
DR EnsemblPlants; AT1G23010.1; AT1G23010.1; AT1G23010.
DR GeneID; 838909; -.
DR Gramene; AT1G23010.1; AT1G23010.1; AT1G23010.
DR KEGG; ath:AT1G23010; -.
DR Araport; AT1G23010; -.
DR TAIR; locus:2017699; AT1G23010.
DR eggNOG; ENOG502QR4X; Eukaryota.
DR HOGENOM; CLU_009100_4_0_1; -.
DR InParanoid; F4I4K5; -.
DR OMA; LLPKQWG; -.
DR OrthoDB; 525810at2759; -.
DR PRO; PR:F4I4K5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I4K5; baseline and differential.
DR Genevisible; F4I4K5; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IDA:TAIR.
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; IPR011707; Cu-oxidase_N.
DR InterPro; IPR008972; Cupredoxin.
DR PANTHER; PTHR11709; PTHR11709; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 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..28
FT /evidence="ECO:0000255"
FT CHAIN 29..581
FT /note="Multicopper oxidase LPR1"
FT /id="PRO_0000429267"
FT DOMAIN 283..352
FT /note="Plastocyanin-like"
FT BINDING 148
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 150
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 196
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="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:P37064"
FT BINDING 464
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 467
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 469
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 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
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 474
FT /note="K -> E (in Ref. 3; BAC42623 and 4; AAO64864)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 581 AA; 65998 MW; 8FD81219D2015C54 CRC64;
MESLLCRRRI KRVMVLIIAL TWLRSTCGEL EDQLFEVGKL KMFVDDLPDM PRLYGFNSVH
GIIKPASLQI GMFSTKWKFH RDLPATPVFA YGTSRSKATV PGPTIETVYG VDTYVTWRNH
LPKSHILPWD PTISPATPKH GGIPTVVHLH GGIHEPTSDG NADAWFTAGF RETGPKWTKT
TLHYENKQQP GNMWYHDHAM GLTRVNLLAG LVGAYILRHH AVESPFQLPT GDEFDRPLII
FDRSFRKDGS IYMNATGNNP SIHPQWQPEY FGDVIIVNGK AWPRLNVRRR KYRFRIINAS
NARFFKFFFS NGLDFIVVGS DSAYLSKPVM TKSILLSPSE IVDVVVDFYK SPSRTVVLAN
DAPYPYPSGD PVNEENGKVM KFIINNESED DTCTIPKKLI NYPNADVSNA VLTRYISMYE
YVSNSDEPTH LLVNGLPYEA PVTETPKSGT TEVWEVINLT EDNHPLHIHL GLFKVVEQTA
LLAAGLEEFK ECMTKQNDAV KCQISKYARG KKTAVTAHER GWKNVFKMMP GHVTRILVRF
SYIHTNASYP FDPTQEPGYV YHCHILDHED NMMMRPLKVI I
