ACY1A_RAT
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 03-AUG-2022, entry version 114.
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}.
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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; Q6AYS7; -.
DR PRIDE; Q6AYS7; -.
DR GeneID; 300981; -.
DR KEGG; rno:300981; -.
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 OMA; GTDAKQF; -.
DR OrthoDB; 1432382at2759; -.
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 tissues.
DR Genevisible; Q6AYS7; RN.
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:cellular amino acid metabolic process; IEA:InterPro.
DR GO; GO:0030163; P:protein catabolic process; TAS:RGD.
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; 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
