ASPG1_ARATH
ID ASPG1_ARATH Reviewed; 500 AA.
AC Q9LS40; Q8RXI1;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Protein ASPARTIC PROTEASE IN GUARD CELL 1;
DE Short=AtASPG1;
DE EC=3.4.23.-;
DE Flags: Precursor;
GN Name=ASPG1; OrderedLocusNames=At3g18490; ORFNames=MYF24.22;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [2]
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 [3]
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 [4]
RP IDENTIFICATION.
RX PubMed=14697270; DOI=10.1016/j.phytochem.2003.09.005;
RA Beers E.P., Jones A.M., Dickerman A.W.;
RT "The S8 serine, C1A cysteine and A1 aspartic protease families in
RT Arabidopsis.";
RL Phytochemistry 65:43-58(2004).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY ABSCISIC ACID AND DROUGHT,
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-180 AND
RP ASP-379, AND ACTIVITY REGULATION.
RC STRAIN=cv. Columbia;
RX PubMed=22268147; DOI=10.1093/jxb/err433;
RA Yao X., Xiong W., Ye T., Wu Y.;
RT "Overexpression of the aspartic protease ASPG1 gene confers drought
RT avoidance in Arabidopsis.";
RL J. Exp. Bot. 63:2579-2593(2012).
CC -!- FUNCTION: Aspartic protease involved in drought avoidance through
CC abscisic acid signaling. {ECO:0000269|PubMed:22268147}.
CC -!- ACTIVITY REGULATION: Inhibited by pepstatin A.
CC {ECO:0000269|PubMed:22268147}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:22268147}.
CC -!- TISSUE SPECIFICITY: Expressed in young seedlings, leaves, guard-cells,
CC stems, flowers and siliques, but not in roots or mesophyll cells.
CC {ECO:0000269|PubMed:22268147}.
CC -!- INDUCTION: Up-regulated by abscisic acid and drought.
CC {ECO:0000269|PubMed:22268147}.
CC -!- DISRUPTION PHENOTYPE: No effect on stomatal closure.
CC {ECO:0000269|PubMed:22268147}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; AB026658; BAB01116.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76104.1; -; Genomic_DNA.
DR EMBL; AY150497; AAN13013.1; -; mRNA.
DR EMBL; AY080874; AAL87345.1; -; mRNA.
DR RefSeq; NP_188478.1; NM_112734.3.
DR AlphaFoldDB; Q9LS40; -.
DR SMR; Q9LS40; -.
DR BioGRID; 6712; 1.
DR IntAct; Q9LS40; 1.
DR STRING; 3702.AT3G18490.1; -.
DR MEROPS; A01.A09; -.
DR iPTMnet; Q9LS40; -.
DR SwissPalm; Q9LS40; -.
DR PaxDb; Q9LS40; -.
DR PRIDE; Q9LS40; -.
DR ProteomicsDB; 246865; -.
DR EnsemblPlants; AT3G18490.1; AT3G18490.1; AT3G18490.
DR GeneID; 821379; -.
DR Gramene; AT3G18490.1; AT3G18490.1; AT3G18490.
DR KEGG; ath:AT3G18490; -.
DR Araport; AT3G18490; -.
DR TAIR; locus:2095042; AT3G18490.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_005738_5_0_1; -.
DR InParanoid; Q9LS40; -.
DR OMA; YCFAFAP; -.
DR OrthoDB; 753343at2759; -.
DR PhylomeDB; Q9LS40; -.
DR PRO; PR:Q9LS40; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LS40; baseline and differential.
DR Genevisible; Q9LS40; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0070001; F:aspartic-type peptidase activity; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR GO; GO:0009627; P:systemic acquired resistance; IMP:TAIR.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033148; ASPG1.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR032799; TAXi_C.
DR InterPro; IPR032861; TAXi_N.
DR PANTHER; PTHR13683; PTHR13683; 1.
DR PANTHER; PTHR13683:SF815; PTHR13683:SF815; 1.
DR Pfam; PF14541; TAXi_C; 1.
DR Pfam; PF14543; TAXi_N; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Disulfide bond; DNA-binding; Endoplasmic reticulum;
KW Hydrolase; Protease; Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..500
FT /note="Protein ASPARTIC PROTEASE IN GUARD CELL 1"
FT /id="PRO_0000417495"
FT DOMAIN 162..496
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 379
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT DISULFID 190..193
FT /evidence="ECO:0000250"
FT DISULFID 196..271
FT /evidence="ECO:0000250"
FT DISULFID 217..235
FT /evidence="ECO:0000250"
FT DISULFID 222..230
FT /evidence="ECO:0000250"
FT DISULFID 307..500
FT /evidence="ECO:0000250"
FT DISULFID 419..461
FT /evidence="ECO:0000250"
FT MUTAGEN 180
FT /note="D->N: Loss of protease activity. Loss of protease
FT activity; when associated with N-379."
FT /evidence="ECO:0000269|PubMed:22268147"
FT MUTAGEN 379
FT /note="D->N: Loss of protease activity. Loss of protease
FT activity; when associated with N-180."
FT /evidence="ECO:0000269|PubMed:22268147"
FT CONFLICT 174
FT /note="E -> D (in Ref. 3; AAL87345)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 500 AA; 53234 MW; F5DF2E1CF9CB306C CRC64;
MAFPRFLSLL AVVTLSLFLT TTDASSRSLS TPPKTNVLDV VSSLQQTQTI LSLDPTRSSL
TTTKPESLSD PVFFNSSSPL SLELHSRDTF VASQHKDYKS LTLSRLERDS SRVAGIVAKI
RFAVEGVDRS DLKPVYNEDT RYQTEDLTTP VVSGASQGSG EYFSRIGVGT PAKEMYLVLD
TGSDVNWIQC EPCADCYQQS DPVFNPTSSS TYKSLTCSAP QCSLLETSAC RSNKCLYQVS
YGDGSFTVGE LATDTVTFGN SGKINNVALG CGHDNEGLFT GAAGLLGLGG GVLSITNQMK
ATSFSYCLVD RDSGKSSSLD FNSVQLGGGD ATAPLLRNKK IDTFYYVGLS GFSVGGEKVV
LPDAIFDVDA SGSGGVILDC GTAVTRLQTQ AYNSLRDAFL KLTVNLKKGS SSISLFDTCY
DFSSLSTVKV PTVAFHFTGG KSLDLPAKNY LIPVDDSGTF CFAFAPTSSS LSIIGNVQQQ
GTRITYDLSK NVIGLSGNKC
