ACY2_RAT
ID ACY2_RAT Reviewed; 312 AA.
AC Q9R1T5; Q6AZ03;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Aspartoacylase;
DE EC=3.5.1.15;
DE AltName: Full=Aminoacylase-2;
DE Short=ACY-2;
GN Name=Aspa;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=WTC; TISSUE=Brain;
RA Kitada K., Serikawa T.;
RT "Full length rat cDNA coding for aspartoacylase.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 43-55; 132-143 AND 172-187, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
RN [4]
RP SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=16935940; DOI=10.1096/fj.05-5358fje;
RA Hershfield J.R., Madhavarao C.N., Moffett J.R., Benjamins J.A.,
RA Garbern J.Y., Namboodiri A.;
RT "Aspartoacylase is a regulated nuclear-cytoplasmic enzyme.";
RL FASEB J. 20:2139-2141(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH ZINC IONS, SUBUNIT,
RP AND COFACTOR.
RX PubMed=17194761; DOI=10.1073/pnas.0607817104;
RA Bitto E., Bingman C.A., Wesenberg G.E., McCoy J.G., Phillips G.N. Jr.;
RT "Structure of aspartoacylase, the brain enzyme impaired in Canavan
RT disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:456-461(2007).
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 Evidence={ECO:0000269|PubMed:16935940};
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|PubMed:17194761}.
CC -!- INTERACTION:
CC Q9R1T5; Q9R1T5: Aspa; NbExp=2; IntAct=EBI-15617537, EBI-15617537;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16935940}. Nucleus
CC {ECO:0000269|PubMed:16935940}.
CC -!- TISSUE SPECIFICITY: Detected in kidney proximal tubule cells (at
CC protein level). {ECO:0000269|PubMed:16935940}.
CC -!- SIMILARITY: Belongs to the AspA/AstE family. Aspartoacylase subfamily.
CC {ECO:0000305}.
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DR EMBL; AB023432; BAA82801.1; -; mRNA.
DR EMBL; BC078813; AAH78813.1; -; mRNA.
DR EMBL; BC078814; AAH78814.1; -; mRNA.
DR RefSeq; NP_077375.1; NM_024399.1.
DR RefSeq; XP_006246877.1; XM_006246815.3.
DR PDB; 2GU2; X-ray; 1.80 A; A/B=2-312.
DR PDB; 2Q4Z; X-ray; 1.80 A; A/B=2-312.
DR PDBsum; 2GU2; -.
DR PDBsum; 2Q4Z; -.
DR AlphaFoldDB; Q9R1T5; -.
DR SMR; Q9R1T5; -.
DR DIP; DIP-60794N; -.
DR STRING; 10116.ENSRNOP00000050760; -.
DR iPTMnet; Q9R1T5; -.
DR PhosphoSitePlus; Q9R1T5; -.
DR SwissPalm; Q9R1T5; -.
DR PaxDb; Q9R1T5; -.
DR PRIDE; Q9R1T5; -.
DR Ensembl; ENSRNOT00000084432; ENSRNOP00000072876; ENSRNOG00000019659.
DR GeneID; 79251; -.
DR KEGG; rno:79251; -.
DR CTD; 443; -.
DR RGD; 621693; Aspa.
DR eggNOG; ENOG502QRAK; Eukaryota.
DR GeneTree; ENSGT00390000001189; -.
DR HOGENOM; CLU_083292_0_0_1; -.
DR InParanoid; Q9R1T5; -.
DR OrthoDB; 693004at2759; -.
DR BRENDA; 3.5.1.15; 5301.
DR Reactome; R-RNO-8963693; Aspartate and asparagine metabolism.
DR EvolutionaryTrace; Q9R1T5; -.
DR PRO; PR:Q9R1T5; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000019659; Expressed in kidney and 20 other tissues.
DR ExpressionAtlas; Q9R1T5; baseline and differential.
DR Genevisible; Q9R1T5; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0019807; F:aspartoacylase activity; TAS:RGD.
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; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0022010; P:central nervous system myelination; IEP:RGD.
DR GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IMP:RGD.
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 3D-structure; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Metal-binding; Nucleus; Reference proteome; Zinc.
FT CHAIN 1..312
FT /note="Aspartoacylase"
FT /id="PRO_0000216874"
FT ACT_SITE 177
FT /evidence="ECO:0000250"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 69..70
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 163..167
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 103
FT /note="N -> D (in Ref. 1; BAA82801)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="D -> V (in Ref. 1; BAA82801)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="P -> H (in Ref. 1; BAA82801)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="Q -> QLQ (in Ref. 1; BAA82801)"
FT /evidence="ECO:0000305"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:2GU2"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:2Q4Z"
FT HELIX 24..35
FT /evidence="ECO:0007829|PDB:2Q4Z"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:2Q4Z"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:2Q4Z"
FT HELIX 54..59
FT /evidence="ECO:0007829|PDB:2Q4Z"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:2Q4Z"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:2Q4Z"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:2Q4Z"
FT HELIX 87..99
FT /evidence="ECO:0007829|PDB:2Q4Z"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:2Q4Z"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:2GU2"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:2Q4Z"
FT HELIX 133..146
FT /evidence="ECO:0007829|PDB:2Q4Z"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:2Q4Z"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:2Q4Z"
FT HELIX 166..169
FT /evidence="ECO:0007829|PDB:2Q4Z"
FT STRAND 170..178
FT /evidence="ECO:0007829|PDB:2Q4Z"
FT HELIX 188..209
FT /evidence="ECO:0007829|PDB:2Q4Z"
FT STRAND 217..228
FT /evidence="ECO:0007829|PDB:2Q4Z"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:2GU2"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:2GU2"
FT TURN 244..248
FT /evidence="ECO:0007829|PDB:2Q4Z"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:2Q4Z"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:2Q4Z"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:2GU2"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:2Q4Z"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:2GU2"
FT TURN 288..291
FT /evidence="ECO:0007829|PDB:2Q4Z"
FT STRAND 293..304
FT /evidence="ECO:0007829|PDB:2Q4Z"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:2GU2"
SQ SEQUENCE 312 AA; 35314 MW; D4344BB001BD5814 CRC64;
MTSCVAEEPI KKIAIFGGTH GNELTGVFLV THWLKNGAEV HRAGLEVKPF ITNPRAVEKC
TRYIDCDLNR VFDLENLSKE MSEDLPYEVR RAQEINHLFG PKNSDDAYDV VFDLHNTTSN
MGCTLILEDS RNDFLIQMFH YIKTCMAPLP CSVYLIEHPS LKYATTRSIA KYPVGIEVGP
QPHGVLRADI LDQMRRMLKH ALDFIQRFNE GKEFPPCAID VYKIMEKVDY PRNESGDVAA
VIHPNLQDQD WKPLHPGDPV FVSLDGKVIP LGGDCTVYPV FVNEAAYYEK KEAFAKTTKL
TLNAKSIRST LH
