ACY1B_RAT
ID ACY1B_RAT Reviewed; 408 AA.
AC Q6PTT0;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Aminoacylase-1B;
DE Short=ACY-1B;
DE EC=3.5.1.14 {ECO:0000305|PubMed:11012679};
DE AltName: Full=ACY IB;
DE AltName: Full=N-acyl-L-amino-acid amidohydrolase;
GN Name=Acy1b; 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], PROTEIN SEQUENCE OF 161-178, FUNCTION, TISSUE
RP SPECIFICITY, AND CATALYTIC ACTIVITY.
RC STRAIN=Wistar; TISSUE=Kidney;
RX PubMed=11012679; DOI=10.1046/j.1432-1327.2000.01712.x;
RA Giardina T., Perrier J., Puigserver A.;
RT "The rat kidney acylase I, characterization and molecular cloning.
RT Differences with other acylases I.";
RL Eur. J. Biochem. 267:6249-6255(2000).
RN [2]
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 [3]
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:0000269|PubMed:11012679}.
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:0000305|PubMed:11012679};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15566;
CC Evidence={ECO:0000305|PubMed:11012679};
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 -!- TISSUE SPECIFICITY: Expressed in kidney. {ECO:0000269|PubMed:11012679}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
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DR EMBL; AY580165; AAS90691.1; -; mRNA.
DR AlphaFoldDB; Q6PTT0; -.
DR SMR; Q6PTT0; -.
DR iPTMnet; Q6PTT0; -.
DR jPOST; Q6PTT0; -.
DR PRIDE; Q6PTT0; -.
DR UCSC; RGD:2030; rat.
DR RGD; 2030; Acy1.
DR PhylomeDB; Q6PTT0; -.
DR Proteomes; UP000002494; Unplaced.
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-1B"
FT /id="PRO_0000274010"
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"
SQ SEQUENCE 408 AA; 45823 MW; F335317AF2574927 CRC64;
MTSKGPEEEH PSVTLFRQYL RIRTVQPKPD YGAAVAFFEE TARQLGLGCQ KVEVAPGYVV
TVLTWPGTNP TLSSILLNSH TDVVPVFKEH WSHDPFEAFK DSEGYIYTRG AQDMKCVSIQ
YLEAVKRLKV EGHRFPRTIH MTFVPDEEVG GHQGMELFVQ RHEFHALRAG FALDEGLANP
TDAFTVFYSE RSPWWVRVTS TGRPGHASRF MEDTAAEKLH KVVNSILAFR EKEWQRLQSN
PHLKEGSVTS VNLTKLEGGV AYNVVPATMS ACFDFRVAPD VDMKAFEEQL QSWCQEAGEG
VTFEFAQKFT EPRMTPTDDT DPWWAAFSGA CKEMTLTLEP EIFPAATDSR YIRAVGIPAL
GFSPMNRTPV LLHDHNERLH EAVFLRGVDI YTRLVAALAS VPALPGES
