ASPGB_ARATH
ID ASPGB_ARATH Reviewed; 325 AA.
AC Q8GXG1; Q9LW72;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Probable isoaspartyl peptidase/L-asparaginase 2;
DE EC=3.4.19.5;
DE AltName: Full=L-asparagine amidohydrolase 2;
DE Contains:
DE RecName: Full=Isoaspartyl peptidase/L-asparaginase 2 subunit alpha;
DE Contains:
DE RecName: Full=Isoaspartyl peptidase/L-asparaginase 2 subunit beta;
DE Flags: Precursor;
GN OrderedLocusNames=At3g16150; ORFNames=MSL1.19;
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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts in asparagine catabolism and also in the final steps of
CC protein degradation via hydrolysis of a range of isoaspartyl
CC dipeptides. {ECO:0000250}.
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:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8GXG1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8GXG1-2; Sequence=VSP_016936;
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 (By similarity).
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Ntn-hydrolase family. {ECO:0000305}.
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DR EMBL; AB012247; BAB02681.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75777.1; -; Genomic_DNA.
DR EMBL; AK118259; BAC42877.1; -; mRNA.
DR EMBL; AY086130; AAM63335.1; -; mRNA.
DR RefSeq; NP_566536.1; NM_112485.4. [Q8GXG1-1]
DR AlphaFoldDB; Q8GXG1; -.
DR SMR; Q8GXG1; -.
DR BioGRID; 6194; 6.
DR STRING; 3702.AT3G16150.1; -.
DR MEROPS; T02.A02; -.
DR PaxDb; Q8GXG1; -.
DR PRIDE; Q8GXG1; -.
DR ProteomicsDB; 246804; -. [Q8GXG1-1]
DR EnsemblPlants; AT3G16150.1; AT3G16150.1; AT3G16150. [Q8GXG1-1]
DR GeneID; 820860; -.
DR Gramene; AT3G16150.1; AT3G16150.1; AT3G16150. [Q8GXG1-1]
DR KEGG; ath:AT3G16150; -.
DR Araport; AT3G16150; -.
DR TAIR; locus:2093387; AT3G16150.
DR eggNOG; KOG1592; Eukaryota.
DR HOGENOM; CLU_021603_1_2_1; -.
DR InParanoid; Q8GXG1; -.
DR OMA; YTYDGGH; -.
DR PhylomeDB; Q8GXG1; -.
DR BioCyc; ARA:AT3G16150-MON; -.
DR BRENDA; 3.5.1.1; 399.
DR SABIO-RK; Q8GXG1; -.
DR PRO; PR:Q8GXG1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8GXG1; baseline and differential.
DR Genevisible; Q8GXG1; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Alternative splicing; Autocatalytic cleavage; Hydrolase; Protease;
KW Reference proteome.
FT CHAIN 1..194
FT /note="Isoaspartyl peptidase/L-asparaginase 2 subunit
FT alpha"
FT /id="PRO_0000045444"
FT CHAIN 195..325
FT /note="Isoaspartyl peptidase/L-asparaginase 2 subunit beta"
FT /id="PRO_0000045445"
FT ACT_SITE 195
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 223..226
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 245..248
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 194..195
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..149
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11910074"
FT /id="VSP_016936"
SQ SEQUENCE 325 AA; 34341 MW; 91641FA109B50519 CRC64;
MGGWAIAVHG GAGIDPNLPA ERQEEAKQLL TRCLNLGIIA LRSNVSAIDV VELVIRELET
DPLFNSGRGS ALTEKGTVEM EASIMDGTKR RCGAVSGITT VKNPISLARL VMDKSPHSYL
AFSGAEDFAR KQGVEIVDNE YFVTDDNVGM LKLAKEANSI LFDYRIPPMG CAGAAATDSP
IQMNGLPISI YAPETVGCVV VDGKGHCAAG TSTGGLMNKM MGRIGDSPLI GAGTYASEFC
GVSCTGEGEA IIRATLARDV SAVMEYKGLN LQEAVDYVIK HRLDEGFAGL IAVSNKGEVV
CGFNSNGMFR GCATEDGFME VAIWE
