SAG12_ARATH
ID SAG12_ARATH Reviewed; 346 AA.
AC Q9FJ47; Q38886; Q8H7B7;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Senescence-specific cysteine protease SAG12 {ECO:0000305};
DE EC=3.4.22.- {ECO:0000305};
DE AltName: Full=Cysteine proteinase SAG12 {ECO:0000305};
DE AltName: Full=Protein SENESCENCE-ASSOCIATED GENE 12 {ECO:0000303|Ref.6};
DE Flags: Precursor;
GN Name=SAG12 {ECO:0000303|Ref.6};
GN OrderedLocusNames=At5g45890 {ECO:0000312|Araport:AT5G45890};
GN ORFNames=K15I22.9 {ECO:0000312|EMBL:BAB09317.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta; TISSUE=Rosette leaf;
RX PubMed=8592746; DOI=10.1126/science.270.5244.1986;
RA Gan S., Amasino R.M.;
RT "Inhibition of leaf senescence by autoregulated production of cytokinin.";
RL Science 270:1986-1988(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-142.
RA Stracke R., Palme K.;
RT "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT and guard cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX DOI=10.1111/j.1399-3054.1994.tb05343.x;
RA Lohman K.N., Gan S., John M.C., Amasino R.M.;
RT "Molecular analysis of natural leaf senescence in Arabidopsis thaliana.";
RL Physiol. Plantarum 92:322-328(1994).
RN [7]
RP DEVELOPMENTAL STAGE, INDUCTION BY ABSCISIC ACID, AND BIOTECHNOLOGY.
RX PubMed=9617813; DOI=10.1023/a:1005934428906;
RA Weaver L.M., Gan S., Quirino B., Amasino R.M.;
RT "A comparison of the expression patterns of several senescence-associated
RT genes in response to stress and hormone treatment.";
RL Plant Mol. Biol. 37:455-469(1998).
RN [8]
RP INDUCTION BY SENESCENCE, DEVELOPMENTAL STAGE, BIOTECHNOLOGY, AND REGULATION
RP BY CYTOKININ; AUXIN AND SUGARS.
RC STRAIN=cv. Columbia;
RX PubMed=10579486; DOI=10.1023/a:1006342412688;
RA Noh Y.S., Amasino R.M.;
RT "Identification of a promoter region responsible for the senescence-
RT specific expression of SAG12.";
RL Plant Mol. Biol. 41:181-194(1999).
RN [9]
RP INDUCTION BY COPPER; PROGRAMMED CELL DEATH AND HYPERSENSITIVE RESPONSE.
RX PubMed=10380810; DOI=10.1023/a:1006133311402;
RA Pontier D., Gan S., Amasino R.M., Roby D., Lam E.;
RT "Markers for hypersensitive response and senescence show distinct patterns
RT of expression.";
RL Plant Mol. Biol. 39:1243-1255(1999).
RN [10]
RP INDUCTION BY SENESCENCE.
RC STRAIN=cv. Columbia;
RX PubMed=10972893; DOI=10.1046/j.1365-313x.2000.00836.x;
RA Morris K., MacKerness S.A., Page T., John C.F., Murphy A.M., Carr J.P.,
RA Buchanan-Wollaston V.;
RT "Salicylic acid has a role in regulating gene expression during leaf
RT senescence.";
RL Plant J. 23:677-685(2000).
RN [11]
RP INDUCTION BY UV-B.
RC STRAIN=cv. Columbia;
RX PubMed=11432956; DOI=10.1093/jxb/52.359.1367;
RA John C.F., Morris K., Jordan B.R., Thomas B., A-H-Mackerness S.;
RT "Ultraviolet-B exposure leads to up-regulation of senescence-associated
RT genes in Arabidopsis thaliana.";
RL J. Exp. Bot. 52:1367-1373(2001).
RN [12]
RP DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15743448; DOI=10.1111/j.1365-313x.2005.02346.x;
RA Otegui M.S., Noh Y.-S., Martinez D.E., Vila Petroff M.G., Staehelin L.A.,
RA Amasino R.M., Guiamet J.J.;
RT "Senescence-associated vacuoles with intense proteolytic activity develop
RT in leaves of Arabidopsis and soybean.";
RL Plant J. 41:831-844(2005).
RN [13]
RP INDUCTION BY HISTONE H3 DEACETYLATION.
RX PubMed=18212027; DOI=10.1093/jxb/erm300;
RA Wu K., Zhang L., Zhou C., Yu C.W., Chaikam V.;
RT "HDA6 is required for jasmonate response, senescence and flowering in
RT Arabidopsis.";
RL J. Exp. Bot. 59:225-234(2008).
RN [14]
RP INDUCTION BY SENESCENCE.
RX PubMed=18721318; DOI=10.1111/j.1438-8677.2008.00108.x;
RA Balazadeh S., Parlitz S., Mueller-Roeber B., Meyer R.C.;
RT "Natural developmental variations in leaf and plant senescence in
RT Arabidopsis thaliana.";
RL Plant Biol. 10S1:136-147(2008).
RN [15]
RP INDUCTION BY WRKY53.
RX PubMed=19143996; DOI=10.1111/j.1365-313x.2008.03782.x;
RA Ay N., Irmler K., Fischer A., Uhlemann R., Reuter G., Humbeck K.;
RT "Epigenetic programming via histone methylation at WRKY53 controls leaf
RT senescence in Arabidopsis thaliana.";
RL Plant J. 58:333-346(2009).
RN [16]
RP INDUCTION BY CADMIUM.
RX PubMed=19261736; DOI=10.1104/pp.108.133397;
RA De Michele R., Vurro E., Rigo C., Costa A., Elviri L., Di Valentin M.,
RA Careri M., Zottini M., Sanita di Toppi L., Lo Schiavo F.;
RT "Nitric oxide is involved in cadmium-induced programmed cell death in
RT Arabidopsis suspension cultures.";
RL Plant Physiol. 150:217-228(2009).
RN [17]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=21575215; DOI=10.1186/1471-2229-11-84;
RA Carbonell-Bejerano P., Urbez C., Granell A., Carbonell J.,
RA Perez-Amador M.A.;
RT "Ethylene is involved in pistil fate by modulating the onset of ovule
RT senescence and the GA-mediated fruit set in Arabidopsis.";
RL BMC Plant Biol. 11:84-84(2011).
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:0000305|PubMed:10380810, ECO:0000305|PubMed:10579486,
CC ECO:0000305|PubMed:18212027, ECO:0000305|PubMed:18721318,
CC ECO:0000305|PubMed:19143996, ECO:0000305|PubMed:19261736}.
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:15743448}.
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:0000269|PubMed:15743448}.
CC -!- TISSUE SPECIFICITY: Found in senescent leaves, especially in
CC senescence-associated vacuoles- (SAVs) containing cells (e.g. mesophyll
CC and guard cells), and in senescencing ovules of unfertilised pistils.
CC {ECO:0000269|PubMed:15743448, ECO:0000269|PubMed:21575215,
CC ECO:0000269|Ref.6}.
CC -!- DEVELOPMENTAL STAGE: Senescent tissues specific expression (Ref.6,
CC PubMed:10579486). Detected only after significant visible yellowing
CC (PubMed:9617813). In unfertilised pistils, accumulates transiently
CC shortly after anthesis, and increased again at the end of pistil
CC development (PubMed:21575215). In ovules, first observed at the basal
CC zone of the ovary, and progressively extend acropetally along the ovary
CC (PubMed:21575215). {ECO:0000269|PubMed:10579486,
CC ECO:0000269|PubMed:21575215, ECO:0000269|PubMed:9617813,
CC ECO:0000269|Ref.6}.
CC -!- INDUCTION: Expression activated by developmentally controlled
CC senescence pathways leading to programmed cell death (PCD), probably by
CC epigenetic regulation via histone H3 deacetylation and by WRKY53
CC activation (PubMed:10579486, PubMed:10380810, PubMed:18212027,
CC PubMed:18721318, PubMed:19143996). Strongly up-regulated upon abscisic
CC acid treatment (PubMed:9617813). Repressed by cytokinin, auxin (IAA),
CC and sugars (sucrose, glucose and fructose) which can thus repress
CC developmental senescence (PubMed:10579486). The senescence-associated
CC accumulation is salicylic acid- (SA) dependent (PubMed:10972893).
CC Induced slightly in outer leaves by UV-B exposure (PubMed:11432956).
CC Expressed in late stages of heavy-metal- (e.g. copper) and
CC hypersensitive response- (HR) mediated lesions, in chlorotic tissues
CC surrounding the necrosis (PubMed:10380810). The induction by cadmium is
CC nitric oxyde- (NO) dependent and occurs one day before cell death
CC (PubMed:19261736). {ECO:0000269|PubMed:10380810,
CC ECO:0000269|PubMed:10579486, ECO:0000269|PubMed:10972893,
CC ECO:0000269|PubMed:11432956, ECO:0000269|PubMed:18212027,
CC ECO:0000269|PubMed:18721318, ECO:0000269|PubMed:19143996,
CC ECO:0000269|PubMed:19261736, ECO:0000269|PubMed:9617813}.
CC -!- DISRUPTION PHENOTYPE: No visible effect on senescence.
CC {ECO:0000269|PubMed:15743448}.
CC -!- BIOTECHNOLOGY: Good molecular marker for age-induced senescence onset
CC measurement. {ECO:0000269|PubMed:10579486, ECO:0000269|PubMed:9617813}.
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}.
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DR EMBL; U37336; AAC49135.1; -; Genomic_DNA.
DR EMBL; AB016870; BAB09317.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95312.1; -; Genomic_DNA.
DR EMBL; AF370131; AAK43946.1; -; mRNA.
DR EMBL; AY040073; AAK64131.1; -; mRNA.
DR EMBL; AF083753; AAN60311.1; -; mRNA.
DR RefSeq; NP_568651.1; NM_123957.3.
DR AlphaFoldDB; Q9FJ47; -.
DR SMR; Q9FJ47; -.
DR BioGRID; 19878; 1.
DR IntAct; Q9FJ47; 1.
DR STRING; 3702.AT5G45890.1; -.
DR MEROPS; C01.117; -.
DR PaxDb; Q9FJ47; -.
DR PRIDE; Q9FJ47; -.
DR ProMEX; Q9FJ47; -.
DR ProteomicsDB; 232834; -.
DR EnsemblPlants; AT5G45890.1; AT5G45890.1; AT5G45890.
DR GeneID; 834629; -.
DR Gramene; AT5G45890.1; AT5G45890.1; AT5G45890.
DR KEGG; ath:AT5G45890; -.
DR Araport; AT5G45890; -.
DR TAIR; locus:2152445; AT5G45890.
DR eggNOG; KOG1543; Eukaryota.
DR HOGENOM; CLU_012184_1_0_1; -.
DR InParanoid; Q9FJ47; -.
DR OMA; GMEKCDG; -.
DR OrthoDB; 1275401at2759; -.
DR PhylomeDB; Q9FJ47; -.
DR PRO; PR:Q9FJ47; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJ47; baseline and differential.
DR Genevisible; Q9FJ47; AT.
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; IDA:TAIR.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0007568; P:aging; IEP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IEP:TAIR.
DR GO; GO:0080187; P:floral organ senescence; IEP:UniProtKB.
DR GO; GO:0010150; P:leaf senescence; IEP:UniProtKB.
DR GO; GO:0009626; P:plant-type hypersensitive response; IEP:UniProtKB.
DR GO; GO:0010623; P:programmed cell death involved in cell development; IEP:UniProtKB.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR GO; GO:0009733; P:response to auxin; IEP:UniProtKB.
DR GO; GO:0009735; P:response to cytokinin; IEP:UniProtKB.
DR GO; GO:0009750; P:response to fructose; IEP:UniProtKB.
DR GO; GO:0009749; P:response to glucose; IEP:UniProtKB.
DR GO; GO:0009744; P:response to sucrose; IEP:UniProtKB.
DR GO; GO:0010224; P:response to UV-B; IEP:UniProtKB.
DR GO; GO:1990169; P:stress response to copper ion; 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 1: Evidence at protein level;
KW Apoptosis; Glycoprotein; Hydrolase; Hypersensitive response; Plant defense;
KW Protease; Reference proteome; Signal; Thiol protease; Vacuole.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..346
FT /note="Senescence-specific cysteine protease SAG12"
FT /evidence="ECO:0000255"
FT /id="PRO_0000430524"
FT ACT_SITE 154
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT ACT_SITE 289
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT ACT_SITE 310
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 97
FT /note="R -> C (in Ref. 1; AAC49135)"
FT CONFLICT 215
FT /note="N -> D (in Ref. 1; AAC49135)"
SQ SEQUENCE 346 AA; 38234 MW; 2BE574417D50F167 CRC64;
MALKHMQIFL FVAIFSSFCF SITLSRPLDN ELIMQKRHIE WMTKHGRVYA DVKEENNRYV
VFKNNVERIE HLNSIPAGRT FKLAVNQFAD LTNDEFRSMY TGFKGVSALS SQSQTKMSPF
RYQNVSSGAL PVSVDWRKKG AVTPIKNQGS CGCCWAFSAV AAIEGATQIK KGKLISLSEQ
QLVDCDTNDF GCEGGLMDTA FEHIKATGGL TTESNYPYKG EDATCNSKKT NPKATSITGY
EDVPVNDEQA LMKAVAHQPV SVGIEGGGFD FQFYSSGVFT GECTTYLDHA VTAIGYGEST
NGSKYWIIKN SWGTKWGESG YMRIQKDVKD KQGLCGLAMK ASYPTI
