ACY2_MOUSE
ID ACY2_MOUSE Reviewed; 312 AA.
AC Q8R3P0; Q5SV07; Q9D876; Q9DCE2; Q9JIN8;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Aspartoacylase;
DE EC=3.5.1.15;
DE AltName: Full=Aminoacylase-2;
DE Short=ACY-2;
GN Name=Aspa;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10837925; DOI=10.1016/s0169-328x(00)00068-1;
RA Namboodiri M.A., Corigliano-Murphy A., Jiang G., Rollag M., Provencio I.;
RT "Murine aspartoacylase: cloning, expression and comparison with the human
RT enzyme.";
RL Brain Res. Mol. Brain Res. 77:285-289(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Small intestine;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP PROTEIN SEQUENCE OF 172-187 AND 200-212, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; AF212998; AAF76459.1; -; mRNA.
DR EMBL; AK002859; BAB22412.1; -; mRNA.
DR EMBL; AK008354; BAB25624.1; -; mRNA.
DR EMBL; AL645739; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024934; AAH24934.1; -; mRNA.
DR CCDS; CCDS25005.1; -.
DR RefSeq; NP_075602.2; NM_023113.5.
DR RefSeq; XP_006532073.2; XM_006532010.3.
DR RefSeq; XP_006532074.1; XM_006532011.2.
DR RefSeq; XP_006532075.1; XM_006532012.3.
DR AlphaFoldDB; Q8R3P0; -.
DR SMR; Q8R3P0; -.
DR BioGRID; 197958; 1.
DR IntAct; Q8R3P0; 3.
DR MINT; Q8R3P0; -.
DR STRING; 10090.ENSMUSP00000021119; -.
DR iPTMnet; Q8R3P0; -.
DR PhosphoSitePlus; Q8R3P0; -.
DR SwissPalm; Q8R3P0; -.
DR jPOST; Q8R3P0; -.
DR MaxQB; Q8R3P0; -.
DR PaxDb; Q8R3P0; -.
DR PeptideAtlas; Q8R3P0; -.
DR PRIDE; Q8R3P0; -.
DR ProteomicsDB; 285662; -.
DR Antibodypedia; 10844; 291 antibodies from 32 providers.
DR DNASU; 11484; -.
DR Ensembl; ENSMUST00000021119; ENSMUSP00000021119; ENSMUSG00000020774.
DR Ensembl; ENSMUST00000184572; ENSMUSP00000139318; ENSMUSG00000020774.
DR GeneID; 11484; -.
DR KEGG; mmu:11484; -.
DR UCSC; uc007kal.2; mouse.
DR CTD; 443; -.
DR MGI; MGI:87914; Aspa.
DR VEuPathDB; HostDB:ENSMUSG00000020774; -.
DR eggNOG; ENOG502QRAK; Eukaryota.
DR GeneTree; ENSGT00390000001189; -.
DR HOGENOM; CLU_083292_0_0_1; -.
DR InParanoid; Q8R3P0; -.
DR OMA; THGNEIN; -.
DR OrthoDB; 1074294at2759; -.
DR PhylomeDB; Q8R3P0; -.
DR TreeFam; TF328708; -.
DR BRENDA; 3.5.1.15; 3474.
DR Reactome; R-MMU-8963693; Aspartate and asparagine metabolism.
DR BioGRID-ORCS; 11484; 0 hits in 72 CRISPR screens.
DR PRO; PR:Q8R3P0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8R3P0; protein.
DR Bgee; ENSMUSG00000020774; Expressed in right kidney and 214 other tissues.
DR ExpressionAtlas; Q8R3P0; baseline and differential.
DR Genevisible; Q8R3P0; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0004046; F:aminoacylase activity; TAS:MGI.
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:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006083; P:acetate metabolic process; TAS:MGI.
DR GO; GO:0022010; P:central nervous system myelination; IEA:Ensembl.
DR GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; ISO:MGI.
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..312
FT /note="Aspartoacylase"
FT /id="PRO_0000216873"
FT ACT_SITE 177
FT /evidence="ECO:0000250"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
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 /evidence="ECO:0000250"
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 110
FT /note="L -> I (in Ref. 1; AAF76459 and 4; AAH24934)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="V -> G (in Ref. 2; BAB25624)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="S -> L (in Ref. 2; BAB25624)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="C -> Y (in Ref. 2; BAB25624)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="H -> P (in Ref. 1; AAF76459)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 312 AA; 35345 MW; F09E710CC3107108 CRC64;
MTSCVAKEPI KKIAIFGGTH GNELTGVFLV THWLRNGTEV HRAGLDVKPF ITNPRAVEKC
TRYIDCDLNR VFDLENLSKE MSEDLPYEVR RAQEINHLFG PKNSDDAYDL VFDLHNTTSN
MGCTLILEDS RNDFLIQMFH YIKTCMAPLP CSVYLIEHPS LKYATTRSIA KYPVGIEVGP
QPHGVLRADI LDQMRKMIKH ALDFIQHFNE GKEFPPCSID VYKIMEKVDY PRNESGDMAA
VIHPNLQDQD WKPLHPGDPV FVSLDGKVIP LGGDCTVYPV FVNEAAYYEK KEAFAKTTKL
TLSAKSIRST LH
