SAG39_ORYSJ
ID SAG39_ORYSJ Reviewed; 339 AA.
AC Q7XWK5; A0A0P0W7K3;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Senescence-specific cysteine protease SAG39 {ECO:0000305};
DE EC=3.4.22.- {ECO:0000305};
DE AltName: Full=Cysteine proteinase SAG39 {ECO:0000305};
DE AltName: Full=Protein SENESCENCE-ASSOCIATED GENE 39 {ECO:0000303|PubMed:20439547};
DE Flags: Precursor;
GN Name=SAG39 {ECO:0000303|PubMed:20439547};
GN OrderedLocusNames=Os04g0206300 {ECO:0000305};
GN ORFNames=OsJ_13822 {ECO:0000312|EMBL:EAZ29764.1},
GN OSJNBa0052O21.11 {ECO:0000312|EMBL:CAD40026.2};
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=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(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 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, INDUCTION BY SENESCENCE; ETHYLENE; GIBBERELLIN AND
RP ABSCISIC ACID, DEVELOPMENTAL STAGE, AND BIOTECHNOLOGY.
RC STRAIN=cv. Nipponbare;
RX PubMed=20439547; DOI=10.1104/pp.110.157123;
RA Liu L., Zhou Y., Szczerba M.W., Li X., Lin Y.;
RT "Identification and application of a rice senescence-associated promoter.";
RL Plant Physiol. 153:1239-1249(2010).
CC -!- FUNCTION: Cysteine protease that may have a developmental senescence
CC specific cell death function during apoptosis, heavy metal
CC detoxification, and hypersensitive response.
CC {ECO:0000250|UniProtKB:Q9FJ47}.
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250|UniProtKB:Q9FJ47}.
CC Note=Localized in senescence-associated vacuoles (SAVs) with intense
CC proteolytic activity that develop in the peripheral cytoplasm of
CC mesophyll and guard cells. {ECO:0000250|UniProtKB:Q9FJ47}.
CC -!- TISSUE SPECIFICITY: Low expression in mature leaves.
CC {ECO:0000269|PubMed:20439547}.
CC -!- DEVELOPMENTAL STAGE: Senescent tissues specific expression.
CC {ECO:0000269|PubMed:20439547}.
CC -!- INDUCTION: Accumulates progressively during senescence with maximum
CC levels at late senescence stages. Induced by abscisic acid (ABA),
CC ethylene (ACC) and gibberellin (GA(3)). {ECO:0000269|PubMed:20439547}.
CC -!- BIOTECHNOLOGY: The senescence specific expression can be use to monitor
CC cytokinin synthases (e.g. IPT) in order to promote yield and early
CC maturation of panicles, and to delay senescence.
CC {ECO:0000303|PubMed:20439547}.
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; AL606590; CAD40026.2; -; Genomic_DNA.
DR EMBL; AP008210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP014960; BAS88099.1; -; Genomic_DNA.
DR EMBL; CM000141; EAZ29764.1; -; Genomic_DNA.
DR RefSeq; XP_015635487.1; XM_015780001.1.
DR AlphaFoldDB; Q7XWK5; -.
DR SMR; Q7XWK5; -.
DR STRING; 4530.OS04T0206300-00; -.
DR MEROPS; C01.104; -.
DR PRIDE; Q7XWK5; -.
DR EnsemblPlants; Os04t0206300-00; Os04t0206300-00; Os04g0206300.
DR GeneID; 107276017; -.
DR Gramene; Os04t0206300-00; Os04t0206300-00; Os04g0206300.
DR KEGG; osa:107276017; -.
DR eggNOG; KOG1543; Eukaryota.
DR HOGENOM; CLU_012184_1_0_1; -.
DR InParanoid; Q7XWK5; -.
DR OMA; FRSTKTN; -.
DR OrthoDB; 508327at2759; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR Genevisible; Q7XWK5; OS.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0010282; C:senescence-associated vacuole; ISS:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0007568; P:aging; ISS:UniProtKB.
DR GO; GO:0010150; P:leaf senescence; IEP:UniProtKB.
DR GO; GO:0010623; P:programmed cell death involved in cell development; ISS:UniProtKB.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009723; P:response to ethylene; IEP:UniProtKB.
DR GO; GO:0009739; P:response to gibberellin; IEP:UniProtKB.
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 2: Evidence at transcript level;
KW Hydrolase; Protease; Reference proteome; Signal; Thiol protease; Vacuole.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..339
FT /note="Senescence-specific cysteine protease SAG39"
FT /evidence="ECO:0000255"
FT /id="PRO_0000430525"
FT ACT_SITE 147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT ACT_SITE 282
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT ACT_SITE 303
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
SQ SEQUENCE 339 AA; 36872 MW; 136D71DF5E22E9CF CRC64;
MAMAKALLFA ILGCLCLCSA VLAARELSDD AAMAARHERW MAQYGRVYRD DAEKARRFEV
FKANVAFIES FNAGNHNFWL GVNQFADLTN DEFRWMKTNK GFIPSTTRVP TGFRYENVNI
DALPATVDWR TKGAVTPIKD QGQCGCCWAF SAVAAMEGIV KLSTGKLISL SEQELVDCDV
HGEDQGCEGG LMDDAFKFII KNGGLTTESN YPYAAADDKC KSVSNSVASI KGYEDVPANN
EAALMKAVAN QPVSVAVDGG DMTFQFYKGG VMTGSCGTDL DHGIVAIGYG KASDGTKYWL
LKNSWGTTWG ENGFLRMEKD ISDKRGMCGL AMEPSYPTA
