ID   ASGL1_XENLA             Reviewed;         309 AA.
AC   Q6GM78;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Isoaspartyl peptidase/L-asparaginase;
DE            EC=3.4.19.5 {ECO:0000250|UniProtKB:Q7L266};
DE            EC=3.5.1.1 {ECO:0000250|UniProtKB:Q7L266};
DE   AltName: Full=Asparaginase-like protein 1;
DE   AltName: Full=Beta-aspartyl-peptidase;
DE   AltName: Full=Isoaspartyl dipeptidase;
DE   AltName: Full=L-asparagine amidohydrolase;
DE   Contains:
DE     RecName: Full=Isoaspartyl peptidase/L-asparaginase alpha chain;
DE   Contains:
DE     RecName: Full=Isoaspartyl peptidase/L-asparaginase beta chain;
DE   Flags: Precursor;
GN   Name=asrgl1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Has both L-asparaginase and beta-aspartyl peptidase activity.
CC       Does not have aspartylglucosaminidase activity and is inactive toward
CC       GlcNAc-L-Asn. Likewise, has no activity toward glutamine.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-asparagine = L-aspartate + NH4(+);
CC         Xref=Rhea:RHEA:21016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:58048; EC=3.5.1.1;
CC         Evidence={ECO:0000250|UniProtKB:Q7L266};
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; Evidence={ECO:0000250|UniProtKB:Q7L266};
CC   -!- SUBUNIT: Heterodimer of an alpha and beta chain produced by
CC       autocleavage. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7L266}.
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Ntn-hydrolase family. {ECO:0000305}.
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DR   EMBL; BC074198; AAH74198.1; -; mRNA.
DR   RefSeq; NP_001086107.1; NM_001092638.1.
DR   AlphaFoldDB; Q6GM78; -.
DR   SMR; Q6GM78; -.
DR   GeneID; 444536; -.
DR   KEGG; xla:444536; -.
DR   CTD; 444536; -.
DR   Xenbase; XB-GENE-989505; asrgl1.L.
DR   OrthoDB; 797598at2759; -.
DR   Proteomes; UP000186698; Chromosome 5L.
DR   Bgee; 444536; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0001917; C:photoreceptor inner segment; ISS:UniProtKB.
DR   GO; GO:0004067; F:asparaginase activity; ISS:UniProtKB.
DR   GO; GO:0008798; F:beta-aspartyl-peptidase activity; ISS:UniProtKB.
DR   GO; GO:0033345; P:asparagine catabolic process via L-aspartate; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04702; ASRGL1_like; 1.
DR   InterPro; IPR033844; ASRGL1_meta.
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; Cytoplasm; Hydrolase; Protease; Reference proteome.
FT   CHAIN           1..165
FT                   /note="Isoaspartyl peptidase/L-asparaginase alpha chain"
FT                   /id="PRO_0000420565"
FT   CHAIN           166..309
FT                   /note="Isoaspartyl peptidase/L-asparaginase beta chain"
FT                   /id="PRO_0000420566"
FT   ACT_SITE        166
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         194..197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         217..220
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   309 AA;  32505 MW;  6CFFBEC28270C13D CRC64;
     MKPVIVVHGG AGKIVEELDA TYRAGVKRAV LKGYDVLSQG GSALTAVEEA VIVLEDEQIF
     NAGHGSVLNE KGDIEMDAII MDGKNLDSGA VSAIRNIANP IKLARLVMEK TDHMLLTCEG
     ATLFAKAQGI PEVPNESLVT ERSRKRWMKN LKENSNPVAD QIGLGTVGAV AIDCEGNVAC
     ATSTGGLTNK MVGRVGDTAC IGSGGYADNN VGAVSTTGHG ESIMKVILAR LILHHMEQGK
     SPEEAADAGL NYMKSRVGGI GGVIIVNSSG DWTAKFSTNQ MSWAAVKDDQ LHIGIYHGEN
     NVTPLEKAL