ACY3_RAT
ID ACY3_RAT Reviewed; 319 AA.
AC Q5M876;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming);
DE EC=3.5.1.114;
DE AltName: Full=Aminoacylase-3;
DE Short=ACY-3;
DE AltName: Full=Aspartoacylase-2;
GN Name=Acy3;
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 [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-318, 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: Plays an important role in deacetylating mercapturic acids in
CC kidney proximal tubules. Also acts on N-acetyl-aromatic amino acids (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acyl-aromatic L-alpha-amino acid + H2O = a carboxylate +
CC an aromatic L-alpha-amino acid; Xref=Rhea:RHEA:54184,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:29067, ChEBI:CHEBI:84824,
CC ChEBI:CHEBI:138093; EC=3.5.1.114;
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;
CC EC=3.5.1.114;
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: Exists as a mixture of homodimers and homotetramer, both
CC catalytically active. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane; Peripheral membrane
CC protein. Cytoplasm. Note=Predominantly localized in the apical membrane
CC of cells in the S1 segment. In the proximal straight tubules (S2 and S3
CC segments) is expressed diffusely throughout the cytoplasm (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AspA/AstE family. Aspartoacylase subfamily.
CC {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; BC088190; AAH88190.1; -; mRNA.
DR RefSeq; NP_001009603.1; NM_001009603.1.
DR RefSeq; XP_006230795.1; XM_006230733.3.
DR RefSeq; XP_008758320.1; XM_008760098.2.
DR AlphaFoldDB; Q5M876; -.
DR SMR; Q5M876; -.
DR STRING; 10116.ENSRNOP00000024112; -.
DR iPTMnet; Q5M876; -.
DR PhosphoSitePlus; Q5M876; -.
DR PaxDb; Q5M876; -.
DR PRIDE; Q5M876; -.
DR Ensembl; ENSRNOT00000024112; ENSRNOP00000024112; ENSRNOG00000017901.
DR GeneID; 293653; -.
DR KEGG; rno:293653; -.
DR UCSC; RGD:1305394; rat.
DR CTD; 91703; -.
DR RGD; 1305394; Acy3.
DR eggNOG; ENOG502QRAK; Eukaryota.
DR GeneTree; ENSGT00390000001189; -.
DR HOGENOM; CLU_083292_0_0_1; -.
DR InParanoid; Q5M876; -.
DR OMA; YPRDPTT; -.
DR OrthoDB; 1074294at2759; -.
DR PhylomeDB; Q5M876; -.
DR TreeFam; TF328708; -.
DR BRENDA; 3.5.1.114; 5301.
DR Reactome; R-RNO-5423646; Aflatoxin activation and detoxification.
DR PRO; PR:Q5M876; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000017901; Expressed in adult mammalian kidney and 18 other tissues.
DR Genevisible; Q5M876; RN.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0004046; F:aminoacylase activity; ISO:RGD.
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:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Cell membrane; Cytoplasm; Hydrolase; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..319
FT /note="N-acyl-aromatic-L-amino acid amidohydrolase
FT (carboxylate-forming)"
FT /id="PRO_0000363362"
FT REGION 1..210
FT /note="Hydrolytic domain"
FT /evidence="ECO:0000250"
FT REGION 211..318
FT /note="Shielding domain"
FT /evidence="ECO:0000250"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 70..71
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 288
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 318
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 319 AA; 35419 MW; AA6849FBE91D62E2 CRC64;
MCSLPGSRKP LLRVAVTGGT HGNEMCGVYL ARYWLQNPGE LQRPSFSAMP VLANPAATAA
CRRYIDRDLN RTFTLTFLGS TATPDDPYEV KRAQELNQLL GPKGTCQAFD FILDLHNTTA
NTGACLISEV SQNPFNLHLC HYLQLQNPGL PCRLFQFEPP GTESYSMDSV SKNGISLELG
PQPQGVLRAE LFSQMRAMVA SILDFIELFN QGMEFPAFEM EVYKNLGSVD FPRTTDGHLT
GTVHSRLQDH DFEPLRPGEP IFKLFSGEDV LYEGDSVVYP LFVNEAAYYE KRVAFLKSEK
IRISVPALPG LTPSSTQTP
