ID   ASPG_LUPAR              Reviewed;         306 AA.
AC   P30362;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Isoaspartyl peptidase/L-asparaginase;
DE            EC=3.4.19.5;
DE   AltName: Full=L-asparagine amidohydrolase;
DE   Contains:
DE     RecName: Full=Isoaspartyl peptidase/L-asparaginase subunit alpha;
DE   Contains:
DE     RecName: Full=Isoaspartyl peptidase/L-asparaginase subunit beta;
DE   Flags: Precursor; Fragment;
OS   Lupinus arboreus (Tree lupine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX   NCBI_TaxID=3872;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Seed;
RX   PubMed=1377963; DOI=10.1007/bf00023386;
RA   Lough T.J., Reddington B.D., Grant M.R., Hill D.F., Reynolds P.H.S.,
RA   Farnden K.J.F.;
RT   "The isolation and characterisation of a cDNA clone encoding L-asparaginase
RT   from developing seeds of lupin (Lupinus arboreus).";
RL   Plant Mol. Biol. 19:391-399(1992).
CC   -!- FUNCTION: Degrades proteins damaged by L-isoaspartyl residue formation
CC       (also known as beta-Asp residues). Also has L-asparaginase activity,
CC       which is used to liberate stored nitrogen during seed development.
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.
CC   -!- TISSUE SPECIFICITY: Developing seeds.
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   -!- SIMILARITY: Belongs to the Ntn-hydrolase family. {ECO:0000305}.
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DR   EMBL; X52588; CAA36824.1; -; mRNA.
DR   PIR; S22523; S22523.
DR   AlphaFoldDB; P30362; -.
DR   SMR; P30362; -.
DR   MEROPS; T02.A01; -.
DR   GO; GO:0008798; F:beta-aspartyl-peptidase activity; IEA:UniProtKB-EC.
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   Autocatalytic cleavage; Hydrolase; Protease.
FT   CHAIN           <1..173
FT                   /note="Isoaspartyl peptidase/L-asparaginase subunit alpha"
FT                   /id="PRO_0000045454"
FT   CHAIN           174..306
FT                   /note="Isoaspartyl peptidase/L-asparaginase subunit beta"
FT                   /id="PRO_0000045455"
FT   ACT_SITE        174
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         202..205
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         224..227
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            173..174
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   306 AA;  32463 MW;  9E0E19F64B30A2F2 CRC64;
     PPERRKPREE GLRHCLQIGV EALKARKSPL DVVELVVREL ENNEHFNAGI GSVLTNSGTV
     EMEASIMDGK SMKCGAVSGL STVLNPISLA RLVMEKTPHM YLAFQGAQDF AKQQGVETVD
     SSHFITAENV ERLKLAIEAN RVQIDYSQYN YTQPVQDDAE KELPVANGDS QIGTVGCVAV
     DSQGNLASAT STGGLVNKMV GRIGDTPLIG AGTYANELCA VSATGKGEAI IQATVARDVA
     ALMEFKGLSL KEAADYVVHE RTPKGTVGLI AVSAAGEIAM PFNTTGMFRA CATEDGNSEI
     AIWPPA