SAG39_ORYSI
ID SAG39_ORYSI Reviewed; 339 AA.
AC A2XQE8;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
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:0000250|UniProtKB:Q7XWK5};
DE Flags: Precursor;
GN ORFNames=OsI_14861 {ECO:0000312|EMBL:EAY93058.1};
OS Oryza sativa subsp. indica (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=39946 {ECO:0000312|EMBL:EAY93058.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
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).
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 -!- 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; CM000129; EAY93058.1; -; Genomic_DNA.
DR AlphaFoldDB; A2XQE8; -.
DR SMR; A2XQE8; -.
DR STRING; 39946.A2XQE8; -.
DR MEROPS; C01.104; -.
DR EnsemblPlants; BGIOSGA015901-TA; BGIOSGA015901-PA; BGIOSGA015901.
DR Gramene; BGIOSGA015901-TA; BGIOSGA015901-PA; BGIOSGA015901.
DR HOGENOM; CLU_012184_1_0_1; -.
DR OMA; FRSTKTN; -.
DR Proteomes; UP000007015; Chromosome 4.
DR GO; GO:0010282; C:senescence-associated vacuole; ISS:UniProtKB.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0007568; P:aging; ISS:UniProtKB.
DR GO; GO:0010150; P:leaf senescence; IEA:EnsemblPlants.
DR GO; GO:0010623; P:programmed cell death involved in cell development; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0009737; P:response to abscisic acid; IEA:EnsemblPlants.
DR GO; GO:0009723; P:response to ethylene; IEA:EnsemblPlants.
DR GO; GO:0009739; P:response to gibberellin; IEA:EnsemblPlants.
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 3: Inferred from homology;
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_0000430526"
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; 36842 MW; E36D71DBE01A0A4B CRC64;
MAMAKALLFA ILGCLCLCSA VLAARELSDD AAMAARHERW MAQYGRVYRD DAEKARRFEV
FKANVAFIES FNAGNHNFWL GVNQFADLTN DEFRWTKTNK GFIPSTTRVP TGFRYENVNI
DALPATVDWR TKGAVTPIKD QGQCGCCWAF SAVAAMEGIV KLSTGKLISL SEQELVDCDV
HGEDQGCEGG LMDDAFKFII KNGGLTTESN YPYAAADDKC KSVSNSVASI KGYEDVPANN
EAALMKAVAN QPVSVAVDGG DMTFQFYKGG VMTGSCGTDL DHGIVAIGYG KASDGTKYWL
LKNSWGTTWG ENGFLRMEKD ISDKRGMCGL AMEPSYPTA