ID   ASGL1_BOVIN             Reviewed;         308 AA.
AC   Q32LE5;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   02-SEP-2026, entry version 110.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Has both L-asparaginase and beta-aspartyl peptidase activity.
CC       May be involved in the production of L-aspartate, which can act as an
CC       excitatory neurotransmitter in some brain regions. Is highly active
CC       with L-Asp beta-methyl ester. Besides, has catalytic activity toward
CC       beta-aspartyl dipeptides and their methyl esters, including beta-L-Asp-
CC       L-Phe, beta-L-Asp-L-Phe methyl ester (aspartame), beta-L-Asp-L-Ala,
CC       beta-L-Asp-L-Leu and beta-L-Asp-L-Lys. Does not have
CC       aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn.
CC       Likewise, has no activity toward glutamine.
CC       {ECO:0000250|UniProtKB:Q7L266}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-asparagine + H2O = 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. This heterodimer may then dimerize in turn, giving rise
CC       to a heterotetramer. {ECO:0000250|UniProtKB:Q7L266}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7L266}.
CC       Note=Midpiece of sperm tail. {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.
CC       {ECO:0000250|UniProtKB:Q7L266}.
CC   -!- SIMILARITY: Belongs to the Ntn-hydrolase family. {ECO:0000305}.
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DR   EMBL; BC109621; AAI09622.1; -; mRNA.
DR   RefSeq; NP_001070503.1; NM_001077035.2.
DR   AlphaFoldDB; Q32LE5; -.
DR   SMR; Q32LE5; -.
DR   FunCoup; Q32LE5; 618.
DR   STRING; 9913.ENSBTAP00000058344; -.
DR   PaxDb; 9913-ENSBTAP00000058344; -.
DR   PeptideAtlas; Q32LE5; -.
DR   GeneID; 767970; -.
DR   KEGG; bta:767970; -.
DR   CTD; 80150; -.
DR   VEuPathDB; HostDB:ENSBTAG00000006910; -.
DR   VGNC; VGNC:26223; ASRGL1.
DR   eggNOG; KOG1592; Eukaryota.
DR   HOGENOM; CLU_021603_1_2_1; -.
DR   InParanoid; Q32LE5; -.
DR   OMA; MGIIMVD; -.
DR   OrthoDB; 2262349at2759; -.
DR   Reactome; R-BTA-8964208; Phenylalanine metabolism.
DR   Proteomes; UP000009136; Chromosome 29.
DR   Bgee; ENSBTAG00000006910; Expressed in blood and 105 other cell types or 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   CDD; cd04702; ASRGL1_like; 1.
DR   FunFam; 3.60.20.30:FF:000001; Isoaspartyl peptidase/L-asparaginase; 1.
DR   Gene3D; 3.60.20.30; (Glycosyl)asparaginase; 1.
DR   InterPro; IPR033844; ASRGL1_meta.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR000246; Peptidase_T2.
DR   PANTHER; PTHR10188:SF41; ISOASPARTYL PEPTIDASE_L-ASPARAGINASE; 1.
DR   PANTHER; PTHR10188; L-ASPARAGINASE; 1.
DR   Pfam; PF01112; Asparaginase_2; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Autocatalytic cleavage; Cytoplasm; Hydrolase; Protease;
KW   Reference proteome.
FT   CHAIN           1..167
FT                   /note="Isoaspartyl peptidase/L-asparaginase alpha chain"
FT                   /id="PRO_0000420554"
FT   CHAIN           168..308
FT                   /note="Isoaspartyl peptidase/L-asparaginase beta chain"
FT                   /id="PRO_0000420555"
FT   ACT_SITE        168
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         196..199
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         219..222
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7L266"
SQ   SEQUENCE   308 AA;  32050 MW;  F17066092C340EE4 CRC64;
     MNPVVVVHGG GASNISKDRK ERVRQGILRA ATVGYNILKQ GGSAVDAVEG AVTVLEDDPD
     FNAGCGSVLN ENGEVEMDAS IMNGKDLSAG AVSAVRCIAN PIKLARLVMD KTPHCFLTDQ
     GAARFAAANG IPTIPGQQLV TERSRKRLEK EKLEKDAQKP DCQKNLGTVG AVALDCQGNL
     AYATSTGGIV NKMPGRVGDT PCVGSGGYAD NDIGAVSTTG HGESILKVNL ARLALFHVEQ
     GKSLEEAANA SLGHMKSKVK GVGGIIMVNK AGEWAVKWTS TSMPWAAAKD GKLHSGIDFG
     DTSIIDLS
//