ID M3X3I5_FELCA Unreviewed; 313 AA.
AC M3X3I5;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 67.
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:ENSFCAP00000021185.1,
GN ECO:0000313|VGNC:VGNC:68376};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000021185.1, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000021185.1, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000021185.1,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000021185.1, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000021185.1,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000021185.1}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000021185.1};
RG Ensembl;
RL Submitted (SEP-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AANG04004035; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006940019.1; XM_006939957.3.
DR AlphaFoldDB; M3X3I5; -.
DR SMR; M3X3I5; -.
DR STRING; 9685.ENSFCAP00000021185; -.
DR PaxDb; 9685-ENSFCAP00000021185; -.
DR Ensembl; ENSFCAT00000031989.3; ENSFCAP00000021185.1; ENSFCAG00000029980.3.
DR GeneID; 101094220; -.
DR KEGG; fca:101094220; -.
DR CTD; 443; -.
DR VGNC; VGNC:68376; ASPA.
DR eggNOG; ENOG502QRAK; Eukaryota.
DR GeneTree; ENSGT00390000001189; -.
DR HOGENOM; CLU_083292_0_0_1; -.
DR InParanoid; M3X3I5; -.
DR OMA; THGNEIN; -.
DR OrthoDB; 35794at2759; -.
DR Proteomes; UP000011712; Chromosome E1.
DR Bgee; ENSFCAG00000029980; Expressed in adult mammalian kidney and 9 other cell types or tissues.
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:Ensembl.
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: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:UP000011712};
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; 35632 MW; 0140889F17BAAE17 CRC64;
MTSCHVTEDP IKKVAIFGGT HGNELTGVFL VKRWLENGTE IQRTGLEVKP FITNPRAVKK
CTRYIDCDLN RVFDPESLGK KMSKDLPYEV RRAQEINHLF GPKDNEYSYD IIFDLHNTTS
NMGCTLILED SRNDFLIQMC HYIKTSLAPL PCYVYLIEHP SLKYATTRSI AKYPVGVEVG
PQPQGVLRAD ILDQMRKMIK HALDFIHNFN EGEEFPPCAI EVYKIMEKID YPRNENGDIA
AIIHPNLQDQ DWKPLHPRDP VFLTLDGKII PLGGGSTVYP VFVNEAAYYE KKEAFAKATK
LTLNARSIRS SLP
//
