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ACY2_BOVIN
ID   ACY2_BOVIN              Reviewed;         313 AA.
AC   P46446;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Aspartoacylase;
DE            EC=3.5.1.15;
DE   AltName: Full=Aminoacylase-2;
DE            Short=ACY-2;
GN   Name=ASPA; Synonyms=ACY2;
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 [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=8252036; DOI=10.1038/ng1093-118;
RA   Kaul R., Gao G.P., Balamurugan K., Matalon R.;
RT   "Cloning of the human aspartoacylase cDNA and a common missense mutation in
RT   Canavan disease.";
RL   Nat. Genet. 5:118-123(1993).
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:0000305}.
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; S74726; AAD14980.1; -; Genomic_DNA.
DR   AlphaFoldDB; P46446; -.
DR   SMR; P46446; -.
DR   STRING; 9913.ENSBTAP00000004734; -.
DR   PaxDb; P46446; -.
DR   PRIDE; P46446; -.
DR   eggNOG; ENOG502QRAK; Eukaryota.
DR   InParanoid; P46446; -.
DR   Proteomes; UP000009136; 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   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Hydrolase; Metal-binding; Nucleus;
KW   Reference proteome; Zinc.
FT   CHAIN           1..313
FT                   /note="Aspartoacylase"
FT                   /id="PRO_0000216870"
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;  35738 MW;  1414D37921891009 CRC64;
     MTSCHVAEDP IKKVAIFGGT HGNELTGVFL VKHWLENSTE IQRTGLEVKP FITNPRAVKK
     CTRYIDCDLN RVFDPENLGK KKSEDLPYEV RRAQEINHLF GPKDSEDSYD IIFDLHNTTS
     NMGCTLILED SRNDFLIQMF HYIKTSLAPL PCYVYLIEHP SLKYATTRSI AKYPVGIEVG
     PQPQGVLRAD ILDQMRKMIQ HALDFIHNFN EGKEFPPCAI EVYKIMRKVD YPRNESGEIS
     AIIHPKLQDQ DWKPLHPEDP VFLTLDGKTI PLGGDQTVYP VFVNEAAYYE KKEAFAKTTK
     LTLNANSIRS SLH
 
 
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