LPR4_ORYSJ
ID LPR4_ORYSJ Reviewed; 588 AA.
AC Q7F757; Q5ZE01;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Multicopper oxidase LPR1 homolog 4 {ECO:0000305};
DE EC=1.-.-.- {ECO:0000305};
DE Flags: Precursor;
GN Name=LPR4 {ECO:0000303|PubMed:27716044};
GN OrderedLocusNames=Os01g0126900 {ECO:0000312|EMBL:BAF03813.1},
GN LOC_Os01g03620 {ECO:0000305};
GN ORFNames=P0044F08.29 {ECO:0000312|EMBL:BAB21194.1},
GN P0409B08.14 {ECO:0000312|EMBL:BAD52543.1};
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] (ISOFORM 2).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7F757-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7F757-2; Sequence=VSP_058782;
CC -!- TISSUE SPECIFICITY: Highly expressed in roots and basal stems.
CC Expressed in leaf sheaths. {ECO:0000269|PubMed:27716044}.
CC -!- INDUCTION: Induced by phosphate or potassium deficiency.
CC {ECO:0000269|PubMed:27716044}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; AP002860; BAD52543.1; -; Genomic_DNA.
DR EMBL; AP002909; BAB21194.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF03813.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS70179.1; -; Genomic_DNA.
DR EMBL; AK109876; BAG98941.1; -; mRNA.
DR RefSeq; XP_015629398.1; XM_015773912.1. [Q7F757-2]
DR RefSeq; XP_015629404.1; XM_015773918.1. [Q7F757-1]
DR AlphaFoldDB; Q7F757; -.
DR SMR; Q7F757; -.
DR STRING; 4530.OS01T0126900-01; -.
DR PRIDE; Q7F757; -.
DR EnsemblPlants; Os01t0126900-01; Os01t0126900-01; Os01g0126900. [Q7F757-2]
DR GeneID; 4325983; -.
DR Gramene; Os01t0126900-01; Os01t0126900-01; Os01g0126900. [Q7F757-2]
DR KEGG; osa:4325983; -.
DR eggNOG; ENOG502QR4X; Eukaryota.
DR OMA; PTIMARH; -.
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 Alternative splicing; Copper; Endoplasmic reticulum; Glycoprotein;
KW Membrane; Metal-binding; Oxidoreductase; Reference proteome; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..588
FT /note="Multicopper oxidase LPR1 homolog 4"
FT /id="PRO_0000439061"
FT DOMAIN 288..357
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000255"
FT BINDING 154
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 156
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 202
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 204
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 473
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 476
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 478
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 569
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 570
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 571
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 575
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 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 CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 553
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 572..588
FT /note="ILDHEDNAMIRPLKLLA -> VSATLNATCLSYWVNFFSNRIYMF (in
FT isoform 2)"
FT /id="VSP_058782"
SQ SEQUENCE 588 AA; 64291 MW; 6C6CB995060C4A82 CRC64;
MMGENRARVV ALVVAVVVVV VGVAGNVAAA QAAVTVADLQ RVAGSLQMYV DALPQMAKIR
GYGFQRGQAV PINLTIGMYQ KTWKFHRDLP ATPVFVYGQC PDSATFPGPT IMARHDVPLF
VRWENHLPAS HILPWDPTVP TAIPKNGGVP TVVHLHGSAH PPQSDGSAFA WFTAGFAEKG
PAWTQATYRY PNVQPPGNLW YHDHALGLTR ANLLAGLLGA YVIEKPEVDT PMDLPCDDDD
LHLVIADRSF NVDGSLYMNS TGVAPNIHPQ WAPEYFGEAI TVNGKAWPFL VVHRRRYRLR
ILNASNARYF NVSLSNGLPI HVVGSDASYL SAPVTVSNLL LSPAEIFDVV VDFSQSPTAE
IELLNSAPYP FPTGAAPGPL NGKVMKFIVQ PNGPLDPPDN STVPDHEVPY ASVTALPPTT
MTRYIVMYEY LTPTGQSTHL YINGLRLEDP VTETPKSGTT ELWQVINLTG DNHPLHIHLG
MFQAVKMQQL VNLQAFTDCM TAVNDAVKCN VDQHAVGPVV PVPDHEKTWK NVIKVPPGFV
TSVVIAFKLV DTNQTYPFDT TAEPGYVYHC HILDHEDNAM IRPLKLLA
