ID   ACY1_HUMAN              Reviewed;         408 AA.
AC   Q03154; C9J6I6; C9J9D8; C9JWD4;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   27-MAR-2024, entry version 215.
DE   RecName: Full=Aminoacylase-1;
DE            Short=ACY-1;
DE            EC=3.5.1.14 {ECO:0000269|PubMed:12933810};
DE   AltName: Full=N-acyl-L-amino-acid amidohydrolase;
GN   Name=ACY1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=8357837; DOI=10.1016/0167-4781(93)90116-u;
RA   Mitta M., Kato I., Tsunasawa S.;
RT   "The nucleotide sequence of human aminoacylase-1.";
RL   Biochim. Biophys. Acta 1174:201-203(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Liver;
RX   PubMed=8394326; DOI=10.1016/s0021-9258(19)85294-8;
RA   Cook R.M., Burke B.J., Buchhagen D.L., Minna J.D., Miller Y.E.;
RT   "Human aminoacylase-1. Cloning, sequence, and expression analysis of a
RT   chromosome 3p21 gene inactivated in small cell lung cancer.";
RL   J. Biol. Chem. 268:17010-17017(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Iwaki K., Tanaka Y., Ohta T., Fukuda S., Kurimoto M.;
RL   Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain, Lung, and Skin;
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   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH ZINC IONS, FUNCTION,
RP   CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF
RP   HIS-80; ASP-113; GLU-147; GLU-148; GLU-175; HIS-206 AND HIS-373.
RX   PubMed=12933810; DOI=10.1074/jbc.m304233200;
RA   Lindner H.A., Lunin V.V., Alary A., Hecker R., Cygler M., Menard R.;
RT   "Essential roles of zinc ligation and enzyme dimerization for catalysis in
RT   the aminoacylase-1/M20 family.";
RL   J. Biol. Chem. 278:44496-44504(2003).
RN   [7]
RP   VARIANT ACY1D CYS-353.
RX   PubMed=16274666; DOI=10.1016/j.bbrc.2005.10.126;
RA   Van Coster R.N., Gerlo E.A., Giardina T.G., Engelke U.F., Smet J.E.,
RA   De Praeter C.M., Meersschaut V.A., De Meirleir L.J., Seneca S.H.,
RA   Devreese B., Leroy J.G., Herga S., Perrier J.P., Wevers R.A., Lissens W.;
RT   "Aminoacylase I deficiency: a novel inborn error of metabolism.";
RL   Biochem. Biophys. Res. Commun. 338:1322-1326(2005).
RN   [8]
RP   VARIANTS ACY1D ASP-233 AND CYS-353, AND TISSUE SPECIFICITY.
RX   PubMed=16465618; DOI=10.1086/500563;
RA   Sass J.O., Mohr V., Olbrich H., Engelke U., Horvath J., Fliegauf M.,
RA   Loges N.T., Schweitzer-Krantz S., Moebus R., Weiler P., Kispert A.,
RA   Superti-Furga A., Wevers R.A., Omran H.;
RT   "Mutations in ACY1, the gene encoding aminoacylase 1, cause a novel inborn
RT   error of metabolism.";
RL   Am. J. Hum. Genet. 78:401-409(2006).
RN   [9]
RP   VARIANT [LARGE SCALE ANALYSIS] ASP-381.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
RN   [10]
RP   VARIANTS ACY1D TRP-197; CYS-353 AND HIS-393.
RX   PubMed=17562838; DOI=10.1212/01.wnl.0000264933.56204.e8;
RA   Sass J.O., Olbrich H., Mohr V., Hart C., Woldseth B., Krywawych S.,
RA   Bjurulf B., Lakhani P.K., Buchdahl R.M., Omran H.;
RT   "Neurological findings in aminoacylase 1 deficiency.";
RL   Neurology 68:2151-2153(2007).
RN   [11]
RP   VARIANTS ACY1D GLN-378; TRP-378 AND CYS-386, AND CHARACTERIZATION OF
RP   VARIANTS ACY1D TRP-197; ASP-233; CYS-353; TRP-378 AND CYS-386.
RX   PubMed=21414403; DOI=10.1016/j.bbadis.2011.03.005;
RA   Sommer A., Christensen E., Schwenger S., Seul R., Haas D., Olbrich H.,
RA   Omran H., Sass J.O.;
RT   "The molecular basis of aminoacylase 1 deficiency.";
RL   Biochim. Biophys. Acta 1812:685-690(2011).
CC   -!- FUNCTION: Catalyzes the hydrolysis of N-acetylated amino acids to
CC       acetate and free amino acids. {ECO:0000269|PubMed:12933810}.
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:12933810};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15566;
CC         Evidence={ECO:0000305|PubMed:12933810};
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:0000269|PubMed:12933810};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67441;
CC         Evidence={ECO:0000305|PubMed:12933810};
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:0000250|UniProtKB:Q99JW2};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67369;
CC         Evidence={ECO:0000250|UniProtKB:Q99JW2};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:12933810};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:12933810};
CC   -!- SUBUNIT: Homodimer. Interacts with SPHK1 (By similarity).
CC       {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q03154; Q03154: ACY1; NbExp=7; IntAct=EBI-742064, EBI-742064;
CC       Q03154; O75934: BCAS2; NbExp=3; IntAct=EBI-742064, EBI-1050106;
CC       Q03154; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-742064, EBI-741158;
CC       Q03154; P36639-2: NUDT1; NbExp=4; IntAct=EBI-742064, EBI-12380931;
CC       Q03154; P0CG20: PRR35; NbExp=3; IntAct=EBI-742064, EBI-11986293;
CC       Q03154; Q96A09: TENT5B; NbExp=3; IntAct=EBI-742064, EBI-752030;
CC       Q03154; P54274: TERF1; NbExp=2; IntAct=EBI-742064, EBI-710997;
CC       Q03154; O43711: TLX3; NbExp=3; IntAct=EBI-742064, EBI-3939165;
CC       Q03154; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-742064, EBI-12040603;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q03154-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q03154-2; Sequence=VSP_046877;
CC       Name=3;
CC         IsoId=Q03154-3; Sequence=VSP_046878;
CC       Name=4;
CC         IsoId=Q03154-4; Sequence=VSP_046876;
CC   -!- TISSUE SPECIFICITY: Expression is highest in kidney, strong in brain
CC       and weaker in placenta and spleen. {ECO:0000269|PubMed:16465618}.
CC   -!- DISEASE: Aminoacylase-1 deficiency (ACY1D) [MIM:609924]: An enzymatic
CC       deficiency resulting in encephalopathy, unspecific psychomotor delay,
CC       psychomotor delay with atrophy of the vermis and syringomyelia, marked
CC       muscular hypotonia or normal clinical features. Epileptic seizures are
CC       a frequent feature. All affected individuals exhibit markedly increased
CC       urinary excretion of several N-acetylated amino acids.
CC       {ECO:0000269|PubMed:16274666, ECO:0000269|PubMed:16465618,
CC       ECO:0000269|PubMed:17562838, ECO:0000269|PubMed:21414403}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
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DR   EMBL; L07548; AAA02852.1; -; mRNA.
DR   EMBL; D14524; BAA03397.1; -; mRNA.
DR   EMBL; D16307; BAA03814.1; -; mRNA.
DR   EMBL; AC115284; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC000545; AAH00545.1; -; mRNA.
DR   EMBL; BC003023; AAH03023.1; -; mRNA.
DR   EMBL; BC014112; AAH14112.1; -; mRNA.
DR   CCDS; CCDS2844.1; -. [Q03154-1]
DR   CCDS; CCDS56261.1; -. [Q03154-2]
DR   CCDS; CCDS56262.1; -. [Q03154-3]
DR   CCDS; CCDS56263.1; -. [Q03154-4]
DR   PIR; A47488; A47488.
DR   RefSeq; NP_000657.1; NM_000666.2. [Q03154-1]
DR   RefSeq; NP_001185824.1; NM_001198895.1. [Q03154-1]
DR   RefSeq; NP_001185825.1; NM_001198896.1. [Q03154-2]
DR   RefSeq; NP_001185826.1; NM_001198897.1. [Q03154-3]
DR   RefSeq; NP_001185827.1; NM_001198898.1. [Q03154-4]
DR   PDB; 1Q7L; X-ray; 1.40 A; A/C=1-198, B/D=321-408.
DR   PDBsum; 1Q7L; -.
DR   AlphaFoldDB; Q03154; -.
DR   SMR; Q03154; -.
DR   BioGRID; 106610; 69.
DR   IntAct; Q03154; 24.
DR   MINT; Q03154; -.
DR   STRING; 9606.ENSP00000384296; -.
DR   DrugBank; DB06151; Acetylcysteine.
DR   DrugBank; DB00128; Aspartic acid.
DR   DrugBank; DB09130; Copper.
DR   DrugCentral; Q03154; -.
DR   MEROPS; M20.973; -.
DR   GlyGen; Q03154; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q03154; -.
DR   PhosphoSitePlus; Q03154; -.
DR   BioMuta; ACY1; -.
DR   DMDM; 461466; -.
DR   REPRODUCTION-2DPAGE; IPI00009268; -.
DR   EPD; Q03154; -.
DR   jPOST; Q03154; -.
DR   MassIVE; Q03154; -.
DR   MaxQB; Q03154; -.
DR   PaxDb; 9606-ENSP00000384296; -.
DR   PeptideAtlas; Q03154; -.
DR   ProteomicsDB; 11969; -.
DR   ProteomicsDB; 58194; -. [Q03154-1]
DR   ProteomicsDB; 8777; -.
DR   ProteomicsDB; 9178; -.
DR   Pumba; Q03154; -.
DR   Antibodypedia; 34911; 587 antibodies from 34 providers.
DR   DNASU; 95; -.
DR   Ensembl; ENST00000404366.7; ENSP00000384296.2; ENSG00000243989.9. [Q03154-1]
DR   Ensembl; ENST00000476351.5; ENSP00000417056.1; ENSG00000243989.9. [Q03154-4]
DR   Ensembl; ENST00000476854.5; ENSP00000419262.1; ENSG00000243989.9. [Q03154-3]
DR   Ensembl; ENST00000494103.5; ENSP00000417618.1; ENSG00000243989.9. [Q03154-2]
DR   Ensembl; ENST00000636358.2; ENSP00000490149.1; ENSG00000243989.9. [Q03154-1]
DR   GeneID; 95; -.
DR   KEGG; hsa:95; -.
DR   MANE-Select; ENST00000636358.2; ENSP00000490149.1; NM_000666.3; NP_000657.1.
DR   UCSC; uc021wzb.2; human. [Q03154-1]
DR   AGR; HGNC:177; -.
DR   CTD; 95; -.
DR   DisGeNET; 95; -.
DR   GeneCards; ACY1; -.
DR   HGNC; HGNC:177; ACY1.
DR   HPA; ENSG00000243989; Group enriched (intestine, kidney, liver).
DR   MalaCards; ACY1; -.
DR   MIM; 104620; gene.
DR   MIM; 609924; phenotype.
DR   neXtProt; NX_Q03154; -.
DR   OpenTargets; ENSG00000243989; -.
DR   Orphanet; 137754; Neurological conditions associated with aminoacylase 1 deficiency.
DR   PharmGKB; PA24497; -.
DR   VEuPathDB; HostDB:ENSG00000243989; -.
DR   eggNOG; KOG2275; Eukaryota.
DR   GeneTree; ENSGT00940000155631; -.
DR   HOGENOM; CLU_021802_5_0_1; -.
DR   InParanoid; Q03154; -.
DR   OMA; TFIETEQ; -.
DR   OrthoDB; 158507at2759; -.
DR   PhylomeDB; Q03154; -.
DR   TreeFam; TF313693; -.
DR   BioCyc; MetaCyc:HS03800-MONOMER; -.
DR   BRENDA; 3.5.1.14; 2681.
DR   PathwayCommons; Q03154; -.
DR   Reactome; R-HSA-5423646; Aflatoxin activation and detoxification.
DR   Reactome; R-HSA-5579007; Defective ACY1 causes encephalopathy.
DR   Reactome; R-HSA-9753281; Paracetamol ADME.
DR   SABIO-RK; Q03154; -.
DR   SignaLink; Q03154; -.
DR   BioGRID-ORCS; 95; 12 hits in 1161 CRISPR screens.
DR   EvolutionaryTrace; Q03154; -.
DR   GeneWiki; ACY1; -.
DR   GenomeRNAi; 95; -.
DR   Pharos; Q03154; Tbio.
DR   PRO; PR:Q03154; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q03154; Protein.
DR   Bgee; ENSG00000243989; Expressed in duodenum and 97 other cell types or tissues.
DR   ExpressionAtlas; Q03154; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR   GO; GO:0004046; F:aminoacylase activity; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd05646; M20_AcylaseI_like; 1.
DR   Gene3D; 1.10.150.900; -; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
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   NCBIfam; TIGR01880; Ac-peptdase-euk; 1.
DR   PANTHER; PTHR45892; AMINOACYLASE-1; 1.
DR   PANTHER; PTHR45892:SF1; AMINOACYLASE-1; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF036696; ACY-1; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
DR   Genevisible; Q03154; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Disease variant; Hydrolase;
KW   Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..408
FT                   /note="Aminoacylase-1"
FT                   /id="PRO_0000185236"
FT   ACT_SITE        82
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        147
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000269|PubMed:12933810"
FT   BINDING         80
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:12933810"
FT   BINDING         113
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:12933810"
FT   BINDING         113
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:12933810"
FT   BINDING         148
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:12933810"
FT   BINDING         175
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:12933810"
FT   BINDING         373
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:12933810"
FT   VAR_SEQ         32..66
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_046876"
FT   VAR_SEQ         103..174
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_046877"
FT   VAR_SEQ         220..284
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_046878"
FT   VARIANT         179
FT                   /note="N -> S (in dbSNP:rs887540)"
FT                   /id="VAR_051805"
FT   VARIANT         197
FT                   /note="R -> W (in ACY1D; loss of activity;
FT                   dbSNP:rs121912700)"
FT                   /evidence="ECO:0000269|PubMed:17562838,
FT                   ECO:0000269|PubMed:21414403"
FT                   /id="VAR_043113"
FT   VARIANT         233
FT                   /note="E -> D (in ACY1D; loss of activity;
FT                   dbSNP:rs121912699)"
FT                   /evidence="ECO:0000269|PubMed:16465618,
FT                   ECO:0000269|PubMed:21414403"
FT                   /id="VAR_026104"
FT   VARIANT         353
FT                   /note="R -> C (in ACY1D; loss of activity;
FT                   dbSNP:rs121912698)"
FT                   /evidence="ECO:0000269|PubMed:16274666,
FT                   ECO:0000269|PubMed:16465618, ECO:0000269|PubMed:17562838,
FT                   ECO:0000269|PubMed:21414403"
FT                   /id="VAR_026105"
FT   VARIANT         378
FT                   /note="R -> Q (in ACY1D; dbSNP:rs150480963)"
FT                   /evidence="ECO:0000269|PubMed:21414403"
FT                   /id="VAR_065562"
FT   VARIANT         378
FT                   /note="R -> W (in ACY1D; slightly reduced activity;
FT                   dbSNP:rs148346337)"
FT                   /evidence="ECO:0000269|PubMed:21414403"
FT                   /id="VAR_065563"
FT   VARIANT         381
FT                   /note="E -> D (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036076"
FT   VARIANT         386
FT                   /note="R -> C (in ACY1D; loss of activity;
FT                   dbSNP:rs2229152)"
FT                   /evidence="ECO:0000269|PubMed:21414403"
FT                   /id="VAR_020452"
FT   VARIANT         393
FT                   /note="R -> H (in ACY1D; dbSNP:rs121912701)"
FT                   /evidence="ECO:0000269|PubMed:17562838"
FT                   /id="VAR_043114"
FT   MUTAGEN         80
FT                   /note="H->A: Almost abolishes enzyme activity."
FT                   /evidence="ECO:0000269|PubMed:12933810"
FT   MUTAGEN         113
FT                   /note="D->A: Almost abolishes enzyme activity."
FT                   /evidence="ECO:0000269|PubMed:12933810"
FT   MUTAGEN         147
FT                   /note="E->A,Q: Almost abolishes enzyme activity."
FT                   /evidence="ECO:0000269|PubMed:12933810"
FT   MUTAGEN         147
FT                   /note="E->D: Decreased protein stability. Loss of enzyme
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:12933810"
FT   MUTAGEN         148
FT                   /note="E->A: Almost abolishes enzyme activity."
FT                   /evidence="ECO:0000269|PubMed:12933810"
FT   MUTAGEN         175
FT                   /note="E->A: Almost abolishes enzyme activity."
FT                   /evidence="ECO:0000269|PubMed:12933810"
FT   MUTAGEN         206
FT                   /note="H->N: Almost abolishes enzyme activity."
FT                   /evidence="ECO:0000269|PubMed:12933810"
FT   MUTAGEN         373
FT                   /note="H->A: Almost abolishes enzyme activity."
FT                   /evidence="ECO:0000269|PubMed:12933810"
FT   HELIX           11..20
FT                   /evidence="ECO:0007829|PDB:1Q7L"
FT   HELIX           31..45
FT                   /evidence="ECO:0007829|PDB:1Q7L"
FT   STRAND          48..55
FT                   /evidence="ECO:0007829|PDB:1Q7L"
FT   STRAND          58..65
FT                   /evidence="ECO:0007829|PDB:1Q7L"
FT   STRAND          74..80
FT                   /evidence="ECO:0007829|PDB:1Q7L"
FT   HELIX           88..90
FT                   /evidence="ECO:0007829|PDB:1Q7L"
FT   TURN            95..97
FT                   /evidence="ECO:0007829|PDB:1Q7L"
FT   STRAND          104..107
FT                   /evidence="ECO:0007829|PDB:1Q7L"
FT   TURN            109..114
FT                   /evidence="ECO:0007829|PDB:1Q7L"
FT   HELIX           115..130
FT                   /evidence="ECO:0007829|PDB:1Q7L"
FT   STRAND          139..145
FT                   /evidence="ECO:0007829|PDB:1Q7L"
FT   HELIX           147..149
FT                   /evidence="ECO:0007829|PDB:1Q7L"
FT   TURN            152..154
FT                   /evidence="ECO:0007829|PDB:1Q7L"
FT   HELIX           155..158
FT                   /evidence="ECO:0007829|PDB:1Q7L"
FT   HELIX           162..165
FT                   /evidence="ECO:0007829|PDB:1Q7L"
FT   STRAND          169..174
FT                   /evidence="ECO:0007829|PDB:1Q7L"
FT   STRAND          180..188
FT                   /evidence="ECO:0007829|PDB:1Q7L"
FT   HELIX           194..196
FT                   /evidence="ECO:0007829|PDB:1Q7L"
FT   HELIX           322..333
FT                   /evidence="ECO:0007829|PDB:1Q7L"
FT   STRAND          338..342
FT                   /evidence="ECO:0007829|PDB:1Q7L"
FT   HELIX           348..354
FT                   /evidence="ECO:0007829|PDB:1Q7L"
FT   STRAND          359..362
FT                   /evidence="ECO:0007829|PDB:1Q7L"
FT   STRAND          378..380
FT                   /evidence="ECO:0007829|PDB:1Q7L"
FT   HELIX           381..399
FT                   /evidence="ECO:0007829|PDB:1Q7L"
FT   HELIX           405..407
FT                   /evidence="ECO:0007829|PDB:1Q7L"
SQ   SEQUENCE   408 AA;  45885 MW;  293350CD7759826C CRC64;
     MTSKGPEEEH PSVTLFRQYL RIRTVQPKPD YGAAVAFFEE TARQLGLGCQ KVEVAPGYVV
     TVLTWPGTNP TLSSILLNSH TDVVPVFKEH WSHDPFEAFK DSEGYIYARG AQDMKCVSIQ
     YLEAVRRLKV EGHRFPRTIH MTFVPDEEVG GHQGMELFVQ RPEFHALRAG FALDEGIANP
     TDAFTVFYSE RSPWWVRVTS TGRPGHASRF MEDTAAEKLH KVVNSILAFR EKEWQRLQSN
     PHLKEGSVTS VNLTKLEGGV AYNVIPATMS ASFDFRVAPD VDFKAFEEQL QSWCQAAGEG
     VTLEFAQKWM HPQVTPTDDS NPWWAAFSRV CKDMNLTLEP EIMPAATDNR YIRAVGVPAL
     GFSPMNRTPV LLHDHDERLH EAVFLRGVDI YTRLLPALAS VPALPSDS
//