ID   ACY2_PIG                Reviewed;         313 AA.
AC   B1PK17;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Aspartoacylase;
DE            EC=3.5.1.15;
DE   AltName: Full=Aminoacylase-2;
DE            Short=ACY-2;
GN   Name=ASPA;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Shu X., Liu Y.G.;
RL   Submitted (FEB-2008) 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 (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; EU442574; ACA43014.1; -; mRNA.
DR   RefSeq; NP_001116549.1; NM_001123077.1.
DR   AlphaFoldDB; B1PK17; -.
DR   SMR; B1PK17; -.
DR   STRING; 9823.ENSSSCP00000018920; -.
DR   PaxDb; B1PK17; -.
DR   PeptideAtlas; B1PK17; -.
DR   PRIDE; B1PK17; -.
DR   GeneID; 100142661; -.
DR   KEGG; ssc:100142661; -.
DR   CTD; 443; -.
DR   eggNOG; ENOG502QRAK; Eukaryota.
DR   HOGENOM; CLU_083292_0_0_1; -.
DR   InParanoid; B1PK17; -.
DR   OrthoDB; 1074294at2759; -.
DR   TreeFam; TF328708; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019807; F:aspartoacylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IBA:GO_Central.
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_0000363359"
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;  35605 MW;  91E89A52CF8A40FC CRC64;
     MTSCQVAEDP IKKVAIFGGT HGNELTGVFL VKHWLENNTE IQRTGLEVKP FITNPRAVEK
     CTRYIDCDLN RVFDPENLGK RMSEDLPYEV RRAQEISRLF GPKDSEDSYD IIFDLHNTTS
     NMGCTLILED SRNDFLIQMF HYIKTSLAPL PCYVYLIEHP SLKYATTRSI AKYPVGIEVG
     PQPQGVLRAD ILDQMRKMIK HALDFIHNFN EGKEFPPCAI EVYKIMEKVD YPRNESGEIA
     AIIHPKLQDQ DWKPLHPGDP VFLTLDGKTI PLGGDCTVYP VFVNEAAYYE KKEAFAKTTK
     LTLNAKGIHS SLH