ID A0A384CGD8_URSMA Unreviewed; 313 AA.
AC A0A384CGD8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Aspartoacylase {ECO:0000256|ARBA:ARBA00040105};
DE EC=3.5.1.15 {ECO:0000256|ARBA:ARBA00039016};
DE AltName: Full=Aminoacylase-2 {ECO:0000256|ARBA:ARBA00042829};
GN Name=ASPA {ECO:0000313|Ensembl:ENSUMAP00000010817,
GN ECO:0000313|RefSeq:XP_008693480.1};
OS Ursus maritimus (Polar bear) (Thalarctos maritimus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=29073 {ECO:0000313|Proteomes:UP000261680, ECO:0000313|RefSeq:XP_008693480.1};
RN [1] {ECO:0000313|Ensembl:ENSUMAP00000010817}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_008693480.1}
RP IDENTIFICATION.
RC TISSUE=Whole blood {ECO:0000313|RefSeq:XP_008693480.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 acts as a
CC scavenger of NAA from body fluids. {ECO:0000256|ARBA:ARBA00043907}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR018001-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR018001-3};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the AspA/AstE family. Aspartoacylase subfamily.
CC {ECO:0000256|ARBA:ARBA00006173}.
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DR RefSeq; XP_008693480.1; XM_008695258.2.
DR STRING; 29073.ENSUMAP00000010817; -.
DR Ensembl; ENSUMAT00000012892.1; ENSUMAP00000010817.1; ENSUMAG00000008150.1.
DR GeneID; 103667137; -.
DR KEGG; umr:103667137; -.
DR CTD; 443; -.
DR OMA; THGNEIN; -.
DR OrthoDB; 35794at2759; -.
DR Proteomes; UP000261680; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019807; F:aspartoacylase activity; IEA:Ensembl.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006083; P:acetate metabolic process; IEA:Ensembl.
DR GO; GO:0006531; P:aspartate metabolic process; IEA:Ensembl.
DR CDD; cd06909; M14_ASPA; 1.
DR Gene3D; 2.20.25.160; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR HAMAP; MF_00704; Aspartoacylase; 1.
DR InterPro; IPR016708; Aspartoacylase.
DR InterPro; IPR007036; Aste_AspA.
DR PANTHER; PTHR15162; ASPARTOACYLASE; 1.
DR PANTHER; PTHR15162:SF9; ASPARTOACYLASE; 1.
DR Pfam; PF04952; AstE_AspA; 1.
DR PIRSF; PIRSF018001; Aspartoacylase; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR018001-3}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000261680};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR018001-3}.
FT ACT_SITE 178
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-1"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-3"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-3"
FT BINDING 63
FT /ligand="N-acetyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:16953"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-2"
FT BINDING 70..71
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-2"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-3"
FT BINDING 164..168
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-2"
FT BINDING 178
FT /ligand="N-acetyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:16953"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-2"
FT BINDING 288
FT /ligand="N-acetyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:16953"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-2"
SQ SEQUENCE 313 AA; 35626 MW; 95A935C35B1AA4DE CRC64;
MTSCHVIEDP IKKVAIFGGT HGNELTGVFL VKHWLENGTE IQRTGLEVKP FITNPRAVKK
RTRYIDCDLN RVFDPENLGK KMSKDLPYEV TRAQEINHLF GPKDNEDSYD IIFDLHNTTS
NMGCTLILED SRNDFLIQMF HYIKISLAPV PCYVYLIEHP SLKYATARSI ARYPVGIEVG
PQPQGVLRAD ILDQMRKMIK HALDFIHNFN EGKEFPPCAI EVYKIMEKVD YPRNENGDIA
AIIHPNLQDQ DWKPLHPGDP VFLTLDGQII PLGGDGTVYP VFVNEAAYYE KREAFAKTTK
LTLNAKSIRS SVH
//
