REP2_ORYSJ
ID REP2_ORYSJ Reviewed; 496 AA.
AC Q8GS39; A0A0P0VMC1; A0A8J8YSV5; A3A9I7; Q0DZ62; Q6H662;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Asparaginyl endopeptidase Rep2 {ECO:0000303|PubMed:12684786};
DE EC=3.4.22.- {ECO:0000269|PubMed:12684786};
DE AltName: Full=Vacuolar-processing enzyme 3 {ECO:0000303|PubMed:21972902};
DE Short=OsVPE3 {ECO:0000303|PubMed:21972902};
DE Flags: Precursor;
GN Name=REP2 {ECO:0000303|PubMed:12684786};
GN OrderedLocusNames=Os02g0644000 {ECO:0000312|EMBL:BAS80008.1},
GN LOC_Os02g43010 {ECO:0000305};
GN ORFNames=OJ1282_H11.16-2 {ECO:0000312|EMBL:BAD25787.1},
GN OsJ_07703 {ECO:0000312|EMBL:EAZ23976.1};
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 [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 58-69,
RP FUNCTION, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=12684786; DOI=10.1007/s00425-003-1024-5;
RA Kato H., Sutoh K., Minamikawa T.;
RT "Identification, cDNA cloning and possible roles of seed-specific rice
RT asparaginyl endopeptidase, REP-2.";
RL Planta 217:676-685(2003).
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 GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=8706734; DOI=10.1111/j.1432-1033.1996.0310u.x;
RA Kato H., Minamikawa T.;
RT "Identification and characterization of a rice cysteine endopeptidase that
RT digests glutelin.";
RL Eur. J. Biochem. 239:310-316(1996).
RN [7]
RP INDUCTION BY HYDROGEN PEROXIDE.
RX PubMed=21972902; DOI=10.1111/j.1742-4658.2011.08380.x;
RA Deng M., Bian H., Xie Y., Kim Y., Wang W., Lin E., Zeng Z., Guo F., Pan J.,
RA Han N., Wang J., Qian Q., Zhu M.;
RT "Bcl-2 suppresses hydrogen peroxide-induced programmed cell death via
RT OsVPE2 and OsVPE3, but not via OsVPE1 and OsVPE4, in rice.";
RL FEBS J. 278:4797-4810(2011).
CC -!- FUNCTION: Asparaginyl endopeptidase that may act as an activator of
CC REP1. {ECO:0000269|PubMed:12684786}.
CC -!- TISSUE SPECIFICITY: Expressed in germinating seeds.
CC {ECO:0000269|PubMed:8706734}.
CC -!- DEVELOPMENTAL STAGE: Expressed in aleurone layers of germinating seeds
CC 4 days after imbibition (PubMed:12684786). Expressed in developing
CC seeds from 25 to 35 days after flowering (PubMed:12684786).
CC {ECO:0000269|PubMed:12684786}.
CC -!- INDUCTION: Down-regulated by treatment with gibberellin (GA3) (at
CC protein level) (PubMed:12684786). Induced by hydrogen peroxide
CC (PubMed:21972902). {ECO:0000269|PubMed:12684786,
CC ECO:0000269|PubMed:21972902}.
CC -!- SIMILARITY: Belongs to the peptidase C13 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF09476.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAS80007.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB081464; BAC41386.1; -; mRNA.
DR EMBL; AB081465; BAC41387.1; -; Genomic_DNA.
DR EMBL; AP005291; BAD25787.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF09476.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014958; BAS80007.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014958; BAS80008.1; -; Genomic_DNA.
DR EMBL; CM000139; EAZ23976.1; -; Genomic_DNA.
DR RefSeq; XP_015625561.1; XM_015770075.1.
DR SMR; Q8GS39; -.
DR STRING; 39947.Q8GS39; -.
DR MEROPS; C13.001; -.
DR PRIDE; Q8GS39; -.
DR EnsemblPlants; Os02t0644000-02; Os02t0644000-02; Os02g0644000.
DR GeneID; 4330133; -.
DR Gramene; Os02t0644000-02; Os02t0644000-02; Os02g0644000.
DR KEGG; osa:4330133; -.
DR eggNOG; KOG1348; Eukaryota.
DR HOGENOM; CLU_024160_0_0_1; -.
DR OMA; MPYLYGK; -.
DR OrthoDB; 826971at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR ExpressionAtlas; Q8GS39; baseline and differential.
DR GO; GO:0005773; C:vacuole; IEA:GOC.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR GO; GO:0006624; P:vacuolar protein processing; IBA:GO_Central.
DR InterPro; IPR043577; AE.
DR InterPro; IPR033165; Legumain_beta.
DR InterPro; IPR001096; Peptidase_C13.
DR PANTHER; PTHR12000; PTHR12000; 1.
DR PANTHER; PTHR12000:SF25; PTHR12000:SF25; 1.
DR Pfam; PF01650; Peptidase_C13; 1.
DR PIRSF; PIRSF500139; AE; 1.
DR PIRSF; PIRSF019663; Legumain; 1.
DR PRINTS; PR00776; HEMOGLOBNASE.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Signal; Thiol protease.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..57
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:12684786"
FT /id="PRO_0000455740"
FT CHAIN 58..496
FT /note="Asparaginyl endopeptidase Rep2"
FT /id="PRO_5013535553"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 496 AA; 54848 MW; 7E583C3E8AB8860D CRC64;
MAARWCFALL LALSAAAAGA GAKRTWEPVI RMPGEVVEEE VATVPRGSEG TEEEEKDGVG
TRWAVLVAGS SGYGNYRHQA DVCHAYQILR KGGLKEENIV VFMYDDIANN ILNPRPGVIV
NHPQGEDVYA GVPKDYTGDE VTAKNFYAVL LGNKTAVTGG SRKVIDSKPN DHIFIFYSDH
GGPGVLGMPN LPYLYAADFM KVLQEKHASN TYAKMVIYVE ACESGSIFEG LMPEDLNIYV
TTASNAEESS WGTYCPGMEP SPPSEYITCL GDLYSVSWME DSETHNLKEE SIKKQYEVVK
KRTSDMNSYG AGSHVMEYGD RTFKDDKLYL YQGFDPANAE VKNKLSWEGP KAAVNQRDAD
LLFLWRRYEL LHDKSEEKLK ALREISDTVM HRKLLDSSVD LVGKLLFGFG NGPSVLQAVR
PSGQPLVDDW DCLKRMVRIF ESHCGPLTQY GMKHMRAFAN ICNNGISGAS MKEASIATCS
SHNSGRWSSL VQGYSA
