ASPGA_ARATH
ID ASPGA_ARATH Reviewed; 315 AA.
AC P50287; Q9LEZ6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Isoaspartyl peptidase/L-asparaginase 1;
DE EC=3.4.19.5;
DE AltName: Full=L-asparagine amidohydrolase 1;
DE Contains:
DE RecName: Full=Isoaspartyl peptidase/L-asparaginase 1 subunit alpha;
DE Contains:
DE RecName: Full=Isoaspartyl peptidase/L-asparaginase 1 subunit beta;
DE Flags: Precursor;
GN OrderedLocusNames=At5g08100; ORFNames=T22D6_40;
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;
RX PubMed=7630960; DOI=10.1104/pp.108.3.1321;
RA Casado A., Caballero J.L., Franco A.R., Cardenas J., Grant M.R.,
RA Munoz-Blanco J.;
RT "Molecular cloning of the gene encoding the L-asparaginase gene of
RT Arabidopsis thaliana.";
RL Plant Physiol. 108:1321-1322(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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 PROTEIN SEQUENCE OF 183-191, FUNCTION, SUBUNIT, AND AUTOCATALYTIC CLEAVAGE.
RX PubMed=11988085; DOI=10.1042/bj3640129;
RA Hejazi M., Piotukh K., Mattow J., Deutzmann R., Volkmer-Engert R.,
RA Lockau W.;
RT "Isoaspartyl dipeptidase activity of plant-type asparaginases.";
RL Biochem. J. 364:129-136(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Acts in asparagine catabolism but also in the final steps of
CC protein and degradation via hydrolysis of a range of isoaspartyl
CC dipeptides. The affinity for Asn and at least 4 isoaspartyl dipeptides
CC (L-beta-Asp-Ala, L-beta-Asp-Gly, L-beta-Asp-Leu, L-beta-Asp-Phe) is
CC quite low, KM being greater than 4.0 mM. The enzyme is inactive on
CC alpha-aspartyl dipeptides. {ECO:0000269|PubMed:11988085}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of a beta-linked Asp residue from the N-terminus of a
CC polypeptide.; EC=3.4.19.5;
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains arranged as a
CC dimer of alpha/beta heterodimers. {ECO:0000305|PubMed:11988085}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P50287-1; Sequence=Displayed;
CC -!- PTM: Cleaved into an alpha and beta chain by autocatalysis; this
CC activates the enzyme. The N-terminal residue of the beta subunit is
CC responsible for the nucleophile hydrolase activity.
CC -!- SIMILARITY: Belongs to the Ntn-hydrolase family. {ECO:0000305}.
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DR EMBL; Z34884; CAA84367.1; -; Genomic_DNA.
DR EMBL; AL357612; CAB93711.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91247.1; -; Genomic_DNA.
DR EMBL; AY039555; AAK62610.1; -; mRNA.
DR EMBL; AY093755; AAM10379.1; -; mRNA.
DR PIR; S53127; S53127.
DR PIR; T50495; T50495.
DR RefSeq; NP_196427.1; NM_120892.4. [P50287-1]
DR AlphaFoldDB; P50287; -.
DR SMR; P50287; -.
DR STRING; 3702.AT5G08100.1; -.
DR MEROPS; T02.A01; -.
DR iPTMnet; P50287; -.
DR PaxDb; P50287; -.
DR PRIDE; P50287; -.
DR ProteomicsDB; 246803; -. [P50287-1]
DR EnsemblPlants; AT5G08100.1; AT5G08100.1; AT5G08100. [P50287-1]
DR GeneID; 830704; -.
DR Gramene; AT5G08100.1; AT5G08100.1; AT5G08100. [P50287-1]
DR KEGG; ath:AT5G08100; -.
DR Araport; AT5G08100; -.
DR TAIR; locus:2181509; AT5G08100.
DR eggNOG; KOG1592; Eukaryota.
DR HOGENOM; CLU_021603_1_2_1; -.
DR InParanoid; P50287; -.
DR OMA; YSRMRWK; -.
DR OrthoDB; 797598at2759; -.
DR PhylomeDB; P50287; -.
DR BioCyc; ARA:AT5G08100-MON; -.
DR SABIO-RK; P50287; -.
DR PRO; PR:P50287; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P50287; baseline and differential.
DR Genevisible; P50287; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0004067; F:asparaginase activity; IDA:TAIR.
DR GO; GO:0008798; F:beta-aspartyl-peptidase activity; IBA:GO_Central.
DR GO; GO:0016540; P:protein autoprocessing; IBA:GO_Central.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000246; Peptidase_T2.
DR PANTHER; PTHR10188; PTHR10188; 1.
DR Pfam; PF01112; Asparaginase_2; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Autocatalytic cleavage; Direct protein sequencing;
KW Hydrolase; Phosphoprotein; Protease; Reference proteome.
FT CHAIN 1..182
FT /note="Isoaspartyl peptidase/L-asparaginase 1 subunit
FT alpha"
FT /id="PRO_0000045442"
FT CHAIN 183..315
FT /note="Isoaspartyl peptidase/L-asparaginase 1 subunit beta"
FT /id="PRO_0000045443"
FT ACT_SITE 183
FT /note="Nucleophile"
FT BINDING 211..214
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 233..236
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 182..183
FT /note="Cleavage; by autolysis"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CONFLICT 139
FT /note="D -> Y (in Ref. 1; CAA84367)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 315 AA; 33027 MW; B6D3202B42F94712 CRC64;
MVGWAIALHG GAGDIPIDLP DERRIPRESA LRHCLDLGIS ALKSGKPPLD VAELVVRELE
NHPDFNAGKG SVLTAQGTVE MEASIMDGKT KRCGAVSGLT TVVNPISLAR LVMEKTPHIY
LAFDAAEAFA RAHGVETVDS SHFITPENIA RLKQAKEFNR VQLDYTVPSP KVPDNCGDSQ
IGTVGCVAVD SAGNLASATS TGGYVNKMVG RIGDTPVIGA GTYANHLCAI SATGKGEDII
RGTVARDVAA LMEYKGLSLT EAAAYVVDQS VPRGSCGLVA VSANGEVTMP FNTTGMFRAC
ASEDGYSEIA IWPNN
