ID ACY1A_RAT Reviewed; 408 AA. AC Q6AYS7; Q6PTT1; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2004, sequence version 1. DT 24-JAN-2024, entry version 120. DE RecName: Full=Aminoacylase-1A; DE Short=ACY-1A; DE EC=3.5.1.14; DE AltName: Full=ACY IA; DE AltName: Full=N-acyl-L-amino-acid amidohydrolase; GN Name=Acy1a; Synonyms=Acy1; 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=Wistar; RX PubMed=15253876; DOI=10.1016/j.cbpc.2004.04.010; RA Perrier J., Durand A., Giardina T., Puigserver A.; RT "The rat kidney acylase 1. Evidence for a new cDNA form and comparisons RT with the porcine intestinal enzyme."; RL Comp. Biochem. Physiol. 138B:277-283(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; 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 89-100; 116-126; 169-190 AND 368-378, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord; RA Lubec G., Afjehi-Sadat L.; RL Submitted (NOV-2006) to UniProtKB. RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). CC -!- FUNCTION: Involved in the hydrolysis of N-acylated or N-acetylated CC amino acids (except L-aspartate). {ECO:0000250}. 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 -!- CATALYTIC ACTIVITY: CC Reaction=an N-acetyl-L-cysteine-S-conjugate + H2O = acetate + an S- CC substituted L-cysteine; Xref=Rhea:RHEA:36855, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:30089, ChEBI:CHEBI:58717, ChEBI:CHEBI:58718; EC=3.5.1.14; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- PTM: The N-terminus is blocked. CC -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}. 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; AY580164; AAS90690.1; -; mRNA. DR EMBL; BC078930; AAH78930.1; -; mRNA. DR RefSeq; NP_001005383.1; NM_001005383.1. DR RefSeq; XP_006243777.1; XM_006243715.3. DR RefSeq; XP_006243778.1; XM_006243716.3. DR AlphaFoldDB; Q6AYS7; -. DR SMR; Q6AYS7; -. DR BioGRID; 256778; 1. DR IntAct; Q6AYS7; 1. DR STRING; 10116.ENSRNOP00000015852; -. DR iPTMnet; Q6AYS7; -. DR PhosphoSitePlus; Q6AYS7; -. DR jPOST; Q6AYS7; -. DR PaxDb; 10116-ENSRNOP00000015852; -. DR Ensembl; ENSRNOT00055022347; ENSRNOP00055018137; ENSRNOG00055013030. DR Ensembl; ENSRNOT00060052661; ENSRNOP00060043789; ENSRNOG00060030246. DR Ensembl; ENSRNOT00065013445; ENSRNOP00065009970; ENSRNOG00065008472. DR GeneID; 300981; -. DR KEGG; rno:300981; -. DR AGR; RGD:2030; -. DR CTD; 95; -. DR RGD; 2030; Acy1. DR VEuPathDB; HostDB:ENSRNOG00000011189; -. DR eggNOG; KOG2275; Eukaryota. DR HOGENOM; CLU_021802_5_0_1; -. DR InParanoid; Q6AYS7; -. DR OrthoDB; 158507at2759; -. DR TreeFam; TF313693; -. DR BRENDA; 3.5.1.14; 5301. DR Reactome; R-RNO-5423646; Aflatoxin activation and detoxification. DR Reactome; R-RNO-9753281; Paracetamol ADME. DR Proteomes; UP000002494; Chromosome 8. DR Bgee; ENSRNOG00000011189; Expressed in adult mammalian kidney and 19 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0070062; C:extracellular exosome; ISO:RGD. DR GO; GO:0004046; F:aminoacylase activity; IDA:RGD. DR GO; GO:0042802; F:identical protein binding; ISO:RGD. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro. DR GO; GO:0030163; P:protein catabolic process; TAS:RGD. 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; Q6AYS7; RN. PE 1: Evidence at protein level; KW Cytoplasm; Direct protein sequencing; Hydrolase; Metal-binding; KW Phosphoprotein; Reference proteome; Zinc. FT CHAIN 1..408 FT /note="Aminoacylase-1A" FT /id="PRO_0000274009" 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" FT BINDING 113 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 113 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 148 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 175 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 373 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT MOD_RES 408 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT CONFLICT 3..8 FT /note="TKGPES -> SKVPEE (in Ref. 1; AAS90690)" FT /evidence="ECO:0000305" FT CONFLICT 132 FT /note="G -> S (in Ref. 1; AAS90690)" FT /evidence="ECO:0000305" SQ SEQUENCE 408 AA; 45804 MW; CC9B4505927D432A CRC64; MTTKGPESEH PSVTLFRQYL RICTVQPNPD YGSAVTFLEE RARQLGLSCQ KIEVAPGYVI TVLTWPGTNP LLHSILLNSH TDVVPVFKEH WHHDPFEAFK DSEGYIYARG AQDMKSVSIQ YLEAVRRLKS EGHRFPRTIH MTFVPDEEVG GHKGMELFVK RPEFQALRAG FALDEGLANP TDAFTVFYSE RSPWWIRVTS TGKPGHASRF IEDTAAEKLH KVVNSILAFR EKERQRLQAN PHLKEGAVTS VNLTKLEGGV AYNVVPATMS ACFDFRVAPD VDMKAFEKQL QSWCQEAGEG VTFEFAQKFT EPRMTPTDDT DPWWAAFSGA CKEMNLTLEP EIFPAATDSR YIRAVGIPAL GFSPMNRTPV LLHDHNERLH EAVFLRGVDI YTRLVAALAS VPALPGES //