LPR2_ORYSJ
ID LPR2_ORYSJ Reviewed; 598 AA.
AC Q5ZE07; Q0JR18;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Multicopper oxidase LPR1 homolog 2 {ECO:0000305};
DE EC=1.-.-.- {ECO:0000305};
DE Flags: Precursor;
GN Name=LPR2 {ECO:0000303|PubMed:27716044};
GN OrderedLocusNames=Os01g0126200 {ECO:0000312|EMBL:BAS70176.1},
GN LOC_Os01g03549 {ECO:0000305};
GN ORFNames=P0409B08.2 {ECO:0000312|EMBL:BAD52537.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP TISSUE SPECIFICITY, INDUCTION, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=27716044; DOI=10.1186/s12870-016-0853-x;
RA Cao Y., Ai H., Jain A., Wu X., Zhang L., Pei W., Chen A., Xu G., Sun S.;
RT "Identification and expression analysis of OsLPR family revealed the
RT potential roles of OsLPR3 and 5 in maintaining phosphate homeostasis in
RT rice.";
RL BMC Plant Biol. 16:210-210(2016).
CC -!- FUNCTION: Multicopper oxidase that may play a role in the maintenance
CC of inorganic phosphate homeostasis. {ECO:0000250|UniProtKB:Q5ZE00}.
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:0000250|UniProtKB:F4I4K5}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:F4I4K5}.
CC -!- TISSUE SPECIFICITY: Expressed in leaf blades.
CC {ECO:0000269|PubMed:27716044}.
CC -!- INDUCTION: Induced by potassium deficiency.
CC {ECO:0000269|PubMed:27716044}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF03810.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP002860; BAD52537.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF03810.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014957; BAS70176.1; -; Genomic_DNA.
DR EMBL; AK121464; BAH00505.1; -; mRNA.
DR RefSeq; XP_015622027.1; XM_015766541.1.
DR RefSeq; XP_015622028.1; XM_015766542.1.
DR AlphaFoldDB; Q5ZE07; -.
DR SMR; Q5ZE07; -.
DR STRING; 4530.OS01T0126200-01; -.
DR PaxDb; Q5ZE07; -.
DR PRIDE; Q5ZE07; -.
DR EnsemblPlants; Os01t0126200-01; Os01t0126200-01; Os01g0126200.
DR GeneID; 4326011; -.
DR Gramene; Os01t0126200-01; Os01t0126200-01; Os01g0126200.
DR KEGG; osa:4326011; -.
DR eggNOG; ENOG502QR4X; Eukaryota.
DR HOGENOM; CLU_009100_4_2_1; -.
DR InParanoid; Q5ZE07; -.
DR OMA; LLPKQWG; -.
DR OrthoDB; 525810at2759; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
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 Gene3D; 2.60.40.420; -; 3.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR008972; Cupredoxin.
DR PANTHER; PTHR11709; PTHR11709; 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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..598
FT /note="Multicopper oxidase LPR1 homolog 2"
FT /id="PRO_5008970829"
FT DOMAIN 285..355
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000255"
FT REGION 391..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 149
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 151
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 476
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 479
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 481
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 579
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 580
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 581
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 585
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 590
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 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 598 AA; 65839 MW; E136C1C46F460996 CRC64;
MEKRRFLGVC LLVAVLVLRA AVLGRGDDGG GGGRLLDPGK LEMFVDELPD MPRMRGYGVA
EGGKLVAGNL TIGMYETMWK FHRDLPATRV FAYGTSKETA TVPGPTIEAM QGVPTYVTWT
NHLPPRHFLP WDPTLTAAAP GSGVPAVVHL HGGVQHSGSD GHSLAWFTAG FAATGPRFSS
PAAYEYPNQQ PPGNLWYHDH AMGLTRVNIL AGLLGAYRVA SPAEEAALNL PSGEAFDRNL
VLFDRDFLAD GSLFMNRTGN NPSVHPQWQP EYFGAVVVAN GKAWPYLRVR RRRYRLRILN
ASNARFFRLS LSGGLRFVHV ASDSVYLARP VPTRAFLLAP SEIADVVVDF VESGNATAIV
LRSDAPAPYP GDPGDKAETV PVMKFVIDDD DDALSTEPDT SSVPARLTSP SQYAKPDARE
AVLMRRIAMY EYTKEGTDEP THLYLNARSY MDPVTETPRE GTSELWDVIN LTDDNHPLHV
HLALFVALEQ RSLRDVDDLK ECMMARGSGG GGADACGLER HLAGGRKHVV PKQERGWKNV
FKVRPGTVTR LLVRFRPLSP PDSRRFPFDV AAGPGYVYHC HILDHEDNEM MRPMKIVR
