REP1_ORYSJ
ID REP1_ORYSJ Reviewed; 371 AA.
AC Q7F3A8; O24190; Q0JGS6; Q5N711; Q9SXM1; Q9SYT5;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Cysteine endopeptidase Rep1 {ECO:0000303|PubMed:10394640};
DE EC=3.4.22.- {ECO:0000269|PubMed:8706734};
DE AltName: Full=Cysteine proteinase SAG12 {ECO:0000305};
DE AltName: Full=Protein SENESCENCE-ASSOCIATED GENE 12 {ECO:0000303|PubMed:23938390};
DE Short=OsSAG12 {ECO:0000303|PubMed:23938390};
DE AltName: Full=Senescence-specific cysteine protease SAG12 {ECO:0000305};
DE Flags: Precursor;
GN Name=REP1 {ECO:0000303|PubMed:10394640};
GN Synonyms=EP3A {ECO:0000303|PubMed:10631249},
GN SAG12 {ECO:0000303|PubMed:23938390};
GN OrderedLocusNames=Os01g0907600 {ECO:0000312|EMBL:BAS75803.1},
GN LOC_Os01g67980 {ECO:0000305};
GN ORFNames=OsJ_04473 {ECO:0000312|EMBL:EAZ14551.1},
GN P0497A05.8 {ECO:0000312|EMBL:BAB92565.1};
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 [MRNA], PROTEIN SEQUENCE OF 134-153, FUNCTION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND 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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10394640; DOI=10.1093/oxfordjournals.pcp.a029565;
RA Kato H., Shintani A., Minamikawa T.;
RT "The structure and organization of two cysteine endopeptidase genes from
RT rice.";
RL Plant Cell Physiol. 40:462-467(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10631249; DOI=10.1104/pp.122.1.57;
RA Ho S.L., Tong W.F., Yu S.M.;
RT "Multiple mode regulation of a cysteine proteinase gene expression in
RT rice.";
RL Plant Physiol. 122:57-66(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yoon U.H., Kim Y.H.;
RT "Molecular cloning of cysteine endopeptidase genes in rice seeds.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
RP DEVELOPMENTAL STAGE, AND INDUCTION BY GIBBERELLIN.
RX PubMed=9435140; DOI=10.1093/oxfordjournals.pcp.a029111;
RA Shintani A., Kato H., Minamikawa T.;
RT "Hormonal regulation of expression of two cysteine endopeptidase genes in
RT rice seedlings.";
RL Plant Cell Physiol. 38:1242-1248(1997).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=23938390; DOI=10.1007/s12038-013-9334-7;
RA Singh S., Giri M.K., Singh P.K., Siddiqui A., Nandi A.K.;
RT "Down-regulation of OsSAG12-1 results in enhanced senescence and pathogen-
RT induced cell death in transgenic rice plants.";
RL J. Biosci. 38:583-592(2013).
CC -!- FUNCTION: Cysteine endopeptidase that digests in vitro both the acidic
CC and basic subunits of glutelin, the major seed storage protein of rice
CC (PubMed:8706734). Acts as negative regulator of cell death
CC (PubMed:23938390). {ECO:0000269|PubMed:23938390,
CC ECO:0000269|PubMed:8706734}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.5-6.0. {ECO:0000269|PubMed:8706734};
CC -!- SUBCELLULAR LOCATION: Protein storage vacuole
CC {ECO:0000269|PubMed:23938390}.
CC -!- TISSUE SPECIFICITY: Expressed in germinating seeds.
CC {ECO:0000269|PubMed:8706734}.
CC -!- DEVELOPMENTAL STAGE: Expressed in seedlings, from 6 to 21 days after
CC germination. {ECO:0000269|PubMed:9435140}.
CC -!- INDUCTION: Induced by treatment with gibberellin (GA3)
CC (PubMed:9435140). Induced during senescence and pathogen-induced cell
CC death (PubMed:23938390). {ECO:0000269|PubMed:23938390,
CC ECO:0000269|PubMed:9435140}.
CC -!- MISCELLANEOUS: Plants silencinge REP1 develop early senescence at
CC varying levels and show enhanced cell death when inoculated with the
CC bacterial pathogen Xanthomonas oryzae pv oryzae.
CC {ECO:0000269|PubMed:23938390}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC ECO:0000255|PROSITE-ProRule:PRU10090}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D76415; BAA11170.1; -; mRNA.
DR EMBL; AB004819; BAA83473.1; -; Genomic_DNA.
DR EMBL; AF099203; AAD20453.1; -; Genomic_DNA.
DR EMBL; EF122495; ABL74582.1; -; mRNA.
DR EMBL; AP003380; BAB92565.1; -; Genomic_DNA.
DR EMBL; AP006531; BAD82745.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF07052.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS75803.1; -; Genomic_DNA.
DR EMBL; CM000138; EAZ14551.1; -; Genomic_DNA.
DR PIR; T03694; T03694.
DR RefSeq; XP_015621378.1; XM_015765892.1.
DR SMR; Q7F3A8; -.
DR STRING; 39947.Q7F3A8; -.
DR MEROPS; C01.024; -.
DR PRIDE; Q7F3A8; -.
DR EnsemblPlants; Os01t0907600-01; Os01t0907600-01; Os01g0907600.
DR GeneID; 4324982; -.
DR Gramene; Os01t0907600-01; Os01t0907600-01; Os01g0907600.
DR KEGG; osa:4324982; -.
DR eggNOG; KOG1543; Eukaryota.
DR HOGENOM; CLU_012184_1_0_1; -.
DR OMA; AEWETYK; -.
DR OrthoDB; 1275401at2759; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000007752; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
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 CDD; cd02248; Peptidase_C1A; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Signal; Thiol protease; Vacuole.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT PROPEP 29..133
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:8706734"
FT /id="PRO_0000455739"
FT CHAIN 134..371
FT /note="Cysteine endopeptidase Rep1"
FT /id="PRO_5013421039"
FT ACT_SITE 159
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT ACT_SITE 296
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT ACT_SITE 317
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 83..90
FT /note="GGRGYRLR -> APGYAP (in Ref. 1; BAA11170)"
FT /evidence="ECO:0000305"
FT CONFLICT 83..90
FT /note="GGRGYRLR -> APGYPP (in Ref. 3; AAD20453)"
FT /evidence="ECO:0000305"
FT CONFLICT 238..240
FT /note="RAP -> GG (in Ref. 1; BAA11170 and 3; AAD20453)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="A -> P (in Ref. 1; BAA11170 and 3; AAD20453)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 371 AA; 40720 MW; CA342FA17A852FEE CRC64;
MGRVISSWRV LAVVAALMAM AAVELCAAIP FDERDLESDE ALWDLYERWQ EHHHVPRHHG
EKHRRFGAFK DNVRYIHEHN KRGGRGYRLR LNRFGDMGRE EFRATFAGSH ANDLRRDGLA
APPLPGFMYE GVRDLPRAVD WRRKGAVTGV KDQGKCGSCW AFSTVVSVEG INAIRTGRLV
SLSEQELIDC DTADNSGCQG GLMENAFEYI KHSGGITTES AYPYRAANGT CDAVRARRAP
LVVIDGHQNV PANSEAALAK AVANQPVSVA IDAGDQSFQF YSDGVFAGDC GTDLDHGVAV
VGYGETNDGT EYWIVKNSWG TAWGEGGYIR MQRDSGYDGG LCGIAMEASY PVKFSPNRVT
PRRALGAKET Q
