ACY1_MOUSE
ID ACY1_MOUSE Reviewed; 408 AA.
AC Q99JW2; Q9CR15;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Aminoacylase-1;
DE Short=ACY-1;
DE EC=3.5.1.14 {ECO:0000269|PubMed:31587987};
DE AltName: Full=N-acyl-L-amino-acid amidohydrolase;
GN Name=Acy1;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Kidney;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 INTERACTION WITH SPHK1.
RX PubMed=15196915; DOI=10.1016/j.febslet.2004.04.093;
RA Maceyka M., Nava V.E., Milstien S., Spiegel S.;
RT "Aminoacylase 1 is a sphingosine kinase 1-interacting protein.";
RL FEBS Lett. 568:30-34(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
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).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=31587987; DOI=10.1016/j.chembiol.2019.09.009;
RA Kim J.T., Li V.L., Terrell S.M., Fischer C.R., Long J.Z.;
RT "Family-wide Annotation of Enzymatic Pathways by Parallel In Vivo
RT Metabolomics.";
RL Cell Chem. Biol. 26:1623-1629(2019).
CC -!- FUNCTION: Catalyzes the hydrolysis of N-acetylated amino acids to
CC acetate and free amino acids. {ECO:0000269|PubMed:31587987}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acyl-L-amino acid + H2O = a carboxylate + an L-alpha-
CC amino acid; Xref=Rhea:RHEA:15565, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:59869, ChEBI:CHEBI:59874; EC=3.5.1.14;
CC Evidence={ECO:0000269|PubMed:31587987};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15566;
CC Evidence={ECO:0000269|PubMed:31587987};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(alpha)-acetyl-L-methionine = acetate + L-methionine;
CC Xref=Rhea:RHEA:67440, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:71670;
CC Evidence={ECO:0000250|UniProtKB:Q03154};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67441;
CC Evidence={ECO:0000250|UniProtKB:Q03154};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyl-L-glutamine = acetate + L-glutamine;
CC Xref=Rhea:RHEA:67368, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:143879;
CC Evidence={ECO:0000269|PubMed:31587987};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67369;
CC Evidence={ECO:0000269|PubMed:31587987};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q03154};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q03154};
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with SPHK1. {ECO:0000250,
CC ECO:0000269|PubMed:15196915}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
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DR EMBL; AK003703; BAB22948.1; -; mRNA.
DR EMBL; AK002423; BAB22090.1; -; mRNA.
DR EMBL; BC005631; AAH05631.1; -; mRNA.
DR CCDS; CCDS23477.1; -.
DR RefSeq; NP_001263371.1; NM_001276442.1.
DR RefSeq; NP_079647.1; NM_025371.3.
DR AlphaFoldDB; Q99JW2; -.
DR SMR; Q99JW2; -.
DR BioGRID; 224933; 2.
DR IntAct; Q99JW2; 1.
DR STRING; 10090.ENSMUSP00000024031; -.
DR MEROPS; M20.973; -.
DR iPTMnet; Q99JW2; -.
DR MetOSite; Q99JW2; -.
DR PhosphoSitePlus; Q99JW2; -.
DR REPRODUCTION-2DPAGE; Q99JW2; -.
DR EPD; Q99JW2; -.
DR jPOST; Q99JW2; -.
DR MaxQB; Q99JW2; -.
DR PaxDb; Q99JW2; -.
DR PeptideAtlas; Q99JW2; -.
DR PRIDE; Q99JW2; -.
DR ProteomicsDB; 281934; -.
DR DNASU; 109652; -.
DR GeneID; 109652; -.
DR KEGG; mmu:109652; -.
DR UCSC; uc009rjp.2; mouse.
DR CTD; 95; -.
DR MGI; MGI:87913; Acy1.
DR eggNOG; KOG2275; Eukaryota.
DR InParanoid; Q99JW2; -.
DR OrthoDB; 1432382at2759; -.
DR PhylomeDB; Q99JW2; -.
DR TreeFam; TF313693; -.
DR BRENDA; 3.5.1.14; 3474.
DR Reactome; R-MMU-5423646; Aflatoxin activation and detoxification.
DR Reactome; R-MMU-9753281; Paracetamol ADME.
DR BioGRID-ORCS; 109652; 5 hits in 71 CRISPR screens.
DR PRO; PR:Q99JW2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q99JW2; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR GO; GO:0004046; F:aminoacylase activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR010159; N-acyl_aa_amidohydrolase.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
DR TIGRFAMs; TIGR01880; Ac-peptdase-euk; 1.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..408
FT /note="Aminoacylase-1"
FT /id="PRO_0000274007"
FT ACT_SITE 82
FT /evidence="ECO:0000250"
FT ACT_SITE 147
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q03154"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q03154"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q03154"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q03154"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q03154"
FT BINDING 373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q03154"
FT CONFLICT 172
FT /note="A -> V (in Ref. 1; BAB22090/BAB22948)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="R -> Q (in Ref. 1; BAB22090/BAB22948)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="Y -> F (in Ref. 1; BAB22090/BAB22948)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="G -> S (in Ref. 1; BAB22090/BAB22948)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 408 AA; 45781 MW; 384C70B9AB87CDC3 CRC64;
MTTKDPESEH PSVTLFRQYL RICTVQPNPD YGGAITFLEE RARQLGLSCQ KIEVVPGFVI
TVLTWPGTNP SLPSILLNSH TDVVPVFKEH WHHDPFEAFK DSEGYIYARG SQDMKSVSIQ
YLEAVRRLKS EGHRFPRTIH MTFVPDEEVG GHKGMELFVK RPEFQALRAG FALDEGLANP
TDAFTVFYSE RSPWWVRVTS TGKPGHASRF IEDTAAEKLH KVISSILAFR EKERQRLQAN
PHLKEGAVTS VNLTKLEGGV AYNVVPATMS ASFDFRVAPD VDMKAFEKQL QRWCQEAGEG
VTFEFAQKFT EPRMTPTDDS DPWWAAFSGA CKAMNLTLEP EIFPAATDSR YIRAVGIPAL
GFSPMNRTPV LLHDHNERLH EDIFLRGVDI YTGLLSALAS VPTLPGES
