LPR1_ORYSJ
ID LPR1_ORYSJ Reviewed; 582 AA.
AC Q9AWU4;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Multicopper oxidase LPR1 homolog 1 {ECO:0000305};
DE EC=1.-.-.- {ECO:0000305};
DE Flags: Precursor;
GN Name=LPR1 {ECO:0000303|PubMed:27716044};
GN OrderedLocusNames=Os01g0126100 {ECO:0000312|EMBL:BAF03809.1},
GN LOC_Os01g03530 {ECO:0000305};
GN ORFNames=P0037C04.37 {ECO:0000312|EMBL:BAB55542.1},
GN P0044F08.18 {ECO:0000312|EMBL:BAB21188.1};
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 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: Highly expressed in roots, and at lower levels in
CC basal stems and leaf blades. {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}.
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DR EMBL; AP002909; BAB21188.1; -; Genomic_DNA.
DR EMBL; AP003233; BAB55542.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF03809.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS70174.1; -; Genomic_DNA.
DR RefSeq; XP_015625956.1; XM_015770470.1.
DR AlphaFoldDB; Q9AWU4; -.
DR SMR; Q9AWU4; -.
DR STRING; 4530.OS01T0126100-01; -.
DR PaxDb; Q9AWU4; -.
DR PRIDE; Q9AWU4; -.
DR EnsemblPlants; Os01t0126100-01; Os01t0126100-01; Os01g0126100.
DR GeneID; 4326010; -.
DR Gramene; Os01t0126100-01; Os01t0126100-01; Os01g0126100.
DR KEGG; osa:4326010; -.
DR eggNOG; ENOG502QR4X; Eukaryota.
DR HOGENOM; CLU_009100_4_2_1; -.
DR InParanoid; Q9AWU4; -.
DR OMA; PYSGRYV; -.
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; IPR001117; Cu-oxidase.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
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.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 2: Evidence at transcript level;
KW Copper; Endoplasmic reticulum; Glycoprotein; Membrane; Metal-binding;
KW Oxidoreductase; Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..582
FT /note="Multicopper oxidase LPR1 homolog 1"
FT /id="PRO_5008974037"
FT DOMAIN 285..354
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000255"
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 467
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 470
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 472
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="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:P37064"
FT BINDING 564
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 565
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 569
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 574
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|PROSITE-ProRule:PRU00498"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 582 AA; 64050 MW; B5054EECB2C5C1DA CRC64;
MRAKVELAVL LLVLVGVAAG TRPPSAPPPV TEDTLQKVAG SLEMYVDELP QMPKIYGFSM
RHGHPSPIRL TIGMYQKKWK FHRDLPASTV FVFGTSAATA TFPGPTIEAA QGVPLSVTWQ
NYLPARHILP WDPTVPTAIP RRGGVPTVVH LHGGAHPPQS DGSAFAWFTA GFGETGPAWS
TPTYTYPNAQ SPGVLWYHDH ALGLTRANLL AGLLGAYVIR NPAVEAPLGL PCGDEFDRVL
MLADRSFYAD GSIYMNYTGI IPNIHPQWQP EYFGEAITVN GKAWPFLAVA RRRYRFRIIN
TSNARYFNLS LTNGLPFTVV GSDTNYLSKP VTAASLLVSV AETFDVVVDF SQSTSSEAEL
VNTAPYPYPD GQAPNDLNGK VMKFVISPAK AKDTSRVPAK LLDYVAVAEE EAVQRRYIVM
YEYEDAATGN PTHLYINGKR LEDPATETPR PGTTEVWEVI NLTPDNHPLH LHLATFQATR
VRGLVDEDAF KGCMAKLNDA VRCNVSRHAV GEEVAVPEHE KGWKNVVKIA PGYMTTIVVK
FFMVDSGKPY PFDATAEPGY VYHCHILDHE DNAMIRPLKL IK
