ASPG2_ARATH
ID ASPG2_ARATH Reviewed; 470 AA.
AC Q9LHE3;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Protein ASPARTIC PROTEASE IN GUARD CELL 2;
DE Short=AtASPG2;
DE EC=3.4.23.-;
DE Flags: Precursor;
GN Name=ASPG2; OrderedLocusNames=At3g20015; ORFNames=MZE19.7;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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, AND DISRUPTION PHENOTYPE.
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 that may be involved in drought avoidance
CC through abscisic acid signaling. {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; AP002050; BAB03167.1; -; Genomic_DNA.
DR EMBL; AP000383; BAB03167.1; JOINED; Genomic_DNA.
DR EMBL; CP002686; AEE76319.1; -; Genomic_DNA.
DR EMBL; BT003814; AAO41867.1; -; mRNA.
DR RefSeq; NP_188636.2; NM_112892.6.
DR AlphaFoldDB; Q9LHE3; -.
DR SMR; Q9LHE3; -.
DR STRING; 3702.AT3G20015.1; -.
DR MEROPS; A01.A10; -.
DR PaxDb; Q9LHE3; -.
DR PRIDE; Q9LHE3; -.
DR ProteomicsDB; 246866; -.
DR EnsemblPlants; AT3G20015.1; AT3G20015.1; AT3G20015.
DR GeneID; 821540; -.
DR Gramene; AT3G20015.1; AT3G20015.1; AT3G20015.
DR KEGG; ath:AT3G20015; -.
DR Araport; AT3G20015; -.
DR TAIR; locus:2095365; AT3G20015.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_005738_5_0_1; -.
DR InParanoid; Q9LHE3; -.
DR OMA; DMVWVQC; -.
DR OrthoDB; 753343at2759; -.
DR PhylomeDB; Q9LHE3; -.
DR PRO; PR:Q9LHE3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LHE3; baseline and differential.
DR Genevisible; Q9LHE3; AT.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05472; cnd41_like; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR033873; CND41-like.
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 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 2: Evidence at transcript level;
KW Aspartyl protease; Disulfide bond; DNA-binding; Hydrolase; Protease;
KW Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..470
FT /note="Protein ASPARTIC PROTEASE IN GUARD CELL 2"
FT /id="PRO_0000417496"
FT DOMAIN 131..466
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 149
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 350
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT DISULFID 159..162
FT /evidence="ECO:0000250"
FT DISULFID 165..239
FT /evidence="ECO:0000250"
FT DISULFID 186..204
FT /evidence="ECO:0000250"
FT DISULFID 191..199
FT /evidence="ECO:0000250"
FT DISULFID 278..470
FT /evidence="ECO:0000250"
FT DISULFID 389..431
FT /evidence="ECO:0000250"
SQ SEQUENCE 470 AA; 50545 MW; 32B0CD51AABB5679 CRC64;
MLLPLFFFFL HLHLHLSSSS SISFPDFQII DVLQPPLTVT ATLPDFNNTH FSDESSSKYT
LRLLHRDRFP SVTYRNHHHR LHARMRRDTD RVSAILRRIS GKVIPSSDSR YEVNDFGSDI
VSGMDQGSGE YFVRIGVGSP PRDQYMVIDS GSDMVWVQCQ PCKLCYKQSD PVFDPAKSGS
YTGVSCGSSV CDRIENSGCH SGGCRYEVMY GDGSYTKGTL ALETLTFAKT VVRNVAMGCG
HRNRGMFIGA AGLLGIGGGS MSFVGQLSGQ TGGAFGYCLV SRGTDSTGSL VFGREALPVG
ASWVPLVRNP RAPSFYYVGL KGLGVGGVRI PLPDGVFDLT ETGDGGVVMD TGTAVTRLPT
AAYVAFRDGF KSQTANLPRA SGVSIFDTCY DLSGFVSVRV PTVSFYFTEG PVLTLPARNF
LMPVDDSGTY CFAFAASPTG LSIIGNIQQE GIQVSFDGAN GFVGFGPNVC
