ID   ACY2_MACFA              Reviewed;         313 AA.
AC   Q60HH2;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Aspartoacylase;
DE            EC=3.5.1.15;
DE   AltName: Full=Aminoacylase-2;
DE            Short=ACY-2;
GN   Name=ASPA; ORFNames=QflA-19595;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Frontal cortex;
RA   Kusuda J., Osada N., Tanuma R., Hirata M., Sugano S., Hashimoto K.;
RT   "Isolation and characterization of cDNA for macaque neurological disease
RT   genes.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the deacetylation of N-acetylaspartic acid (NAA) to
CC       produce acetate and L-aspartate. NAA occurs in high concentration in
CC       brain and its hydrolysis NAA plays a significant part in the
CC       maintenance of intact white matter. In other tissues it act as a
CC       scavenger of NAA from body fluids (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-acyl-L-aspartate = a carboxylate + L-aspartate;
CC         Xref=Rhea:RHEA:10872, ChEBI:CHEBI:15377, ChEBI:CHEBI:29067,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:58497; EC=3.5.1.15;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AspA/AstE family. Aspartoacylase subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AB125155; BAD51943.1; -; mRNA.
DR   RefSeq; NP_001271953.1; NM_001285024.1.
DR   AlphaFoldDB; Q60HH2; -.
DR   SMR; Q60HH2; -.
DR   STRING; 9541.XP_005582568.1; -.
DR   GeneID; 102137549; -.
DR   CTD; 443; -.
DR   eggNOG; ENOG502QRAK; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019807; F:aspartoacylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   HAMAP; MF_00704; Aspartoacylase; 1.
DR   InterPro; IPR016708; Aspartoacylase.
DR   InterPro; IPR007036; Aste_AspA.
DR   Pfam; PF04952; AstE_AspA; 1.
DR   PIRSF; PIRSF018001; Aspartoacylase; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Metal-binding; Nucleus; Reference proteome; Zinc.
FT   CHAIN           1..313
FT                   /note="Aspartoacylase"
FT                   /id="PRO_0000216872"
FT   ACT_SITE        178
FT                   /evidence="ECO:0000250"
FT   BINDING         21
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         24
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         63
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         70..71
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         116
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         164..168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         178
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         288
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   313 AA;  35658 MW;  6AB975BAD1B9F3C2 CRC64;
     MTSCHIAEEP IKKVAIFGGT HGNELTGVFL VKHWLENGAE IQRTGLEVKP FITNPRAVKK
     CTRYIDCDLN RIFDLENLGK KMSEDLPYEV RRAQEIYHLF GPKDGEDSYD IIFDLHNTTS
     NMGCTLILED SRNNFLIQMF HYIKTSLAPL PCYVYLIEHP SLKYATTRSI AKCPVGIEVG
     PQPQGVLRAD ILDQMRKMIK HALDFIHHFN EGKEFPPCAI EVYKIIEKVD YPRDENGEIA
     AVIHPNLQDQ DWKPLHPGDP MFLTLDGKTM PLGGDCTVYP VFVNEAAYYE KKEAFAKTTK
     LMLNAKSIRC SVH