ASPG3_ARATH
ID ASPG3_ARATH Reviewed; 359 AA.
AC Q56W64; Q27GI5; Q5M760; Q9FKG7;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Probable isoaspartyl peptidase/L-asparaginase 3;
DE EC=3.4.19.5;
DE AltName: Full=L-asparagine amidohydrolase 3;
DE Contains:
DE RecName: Full=Isoaspartyl peptidase/L-asparaginase 3 subunit alpha;
DE Contains:
DE RecName: Full=Isoaspartyl peptidase/L-asparaginase 3 subunit beta;
DE Flags: Precursor;
GN OrderedLocusNames=At5g61540; ORFNames=K11J9.7;
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=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts in asparagine catabolism but 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=Q56W64-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q56W64-2; Sequence=VSP_016937;
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 or to a
CC competing acceptor splice site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Ntn-hydrolase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB08998.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB012239; BAB08998.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97483.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97484.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97485.1; -; Genomic_DNA.
DR EMBL; BT020388; AAV91334.1; -; mRNA.
DR EMBL; BT022060; AAY25472.1; -; mRNA.
DR EMBL; AK222183; BAD95316.1; -; mRNA.
DR EMBL; AK230301; BAF02102.1; -; mRNA.
DR RefSeq; NP_001032119.1; NM_001037042.1. [Q56W64-2]
DR RefSeq; NP_200962.2; NM_125547.4. [Q56W64-1]
DR RefSeq; NP_974974.1; NM_203245.2. [Q56W64-2]
DR AlphaFoldDB; Q56W64; -.
DR SMR; Q56W64; -.
DR STRING; 3702.AT5G61540.1; -.
DR MEROPS; T02.001; -.
DR PaxDb; Q56W64; -.
DR PRIDE; Q56W64; -.
DR ProteomicsDB; 246697; -. [Q56W64-1]
DR EnsemblPlants; AT5G61540.1; AT5G61540.1; AT5G61540. [Q56W64-1]
DR EnsemblPlants; AT5G61540.2; AT5G61540.2; AT5G61540. [Q56W64-2]
DR EnsemblPlants; AT5G61540.3; AT5G61540.3; AT5G61540. [Q56W64-2]
DR GeneID; 836275; -.
DR Gramene; AT5G61540.1; AT5G61540.1; AT5G61540. [Q56W64-1]
DR Gramene; AT5G61540.2; AT5G61540.2; AT5G61540. [Q56W64-2]
DR Gramene; AT5G61540.3; AT5G61540.3; AT5G61540. [Q56W64-2]
DR KEGG; ath:AT5G61540; -.
DR Araport; AT5G61540; -.
DR TAIR; locus:2151626; AT5G61540.
DR eggNOG; KOG1593; Eukaryota.
DR InParanoid; Q56W64; -.
DR OMA; PDENCET; -.
DR PhylomeDB; Q56W64; -.
DR BioCyc; ARA:AT5G61540-MON; -.
DR PRO; PR:Q56W64; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q56W64; baseline and differential.
DR Genevisible; Q56W64; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008798; F:beta-aspartyl-peptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0003948; F:N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity; IBA:GO_Central.
DR GO; GO:0006517; P:protein deglycosylation; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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..223
FT /note="Isoaspartyl peptidase/L-asparaginase 3 subunit
FT alpha"
FT /id="PRO_0000045446"
FT CHAIN 224..359
FT /note="Isoaspartyl peptidase/L-asparaginase 3 subunit beta"
FT /id="PRO_0000045447"
FT ACT_SITE 224
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 252..255
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 275..278
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 223..224
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..102
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3, ECO:0000303|Ref.4"
FT /id="VSP_016937"
SQ SEQUENCE 359 AA; 38249 MW; 6E8829A1318D82D8 CRC64;
MARSDVLIFV STLLLFLSLL TVADAELVKS DKFPVVVSTW PFLEAVRAAW RAVDNGSSAV
EAVVEGCSAC EELRCDGTVG PGGSPDENGE TMIDALVMDG VTMEVGAVAA MRYVKDGIRA
AHLVMKYSQH TLLAGEGASA FAISMGLPGP MNLSSPESVK KWSDWKENQC QPNFRKNVVP
ANDCGPYKPN NSAMNVFVDK STESCEMGAI EYKPPLVGPH NHDTISMAVI DRMGHIAVGT
STNGATYKIP GRVGDGPIVG SSAYADDEVG GCGATGDGDT MMRFLPCYQV VESMRQGMKP
EEAAKDAISR IARKFPDFVG AVVAVDKNGS HAGACYGWTF QYSVQNPDMN DVQVFTVLP
