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Protein

N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming)

Gene

Acy3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays an important role in deacetylating mercapturic acids in kidney proximal tubules. Also acts on N-acetyl-aromatic amino acids.2 Publications

Catalytic activityi

An N-acyl-aromatic-L-amino acid + H2O = an aromatic-L-amino acid + a carboxylate.
An N-acetyl-L-cysteine-S-conjugate + H2O = an L-cysteine-S-conjugate + acetate.

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Kineticsi

  1. KM=1.1 mM for S-benzyl-N-acetyl-L-cysteine1 Publication
  2. KM=1.8 mM for N-acetyl-L-histidine1 Publication
  3. KM=1.4 mM for N-acetyl-L-tyrosine1 Publication
  4. KM=1.6 mM for N-acetyl-L-phenylalanine1 Publication
  1. Vmax=11.7 µmol/min/mg enzyme with S-benzyl-N-acetyl-L-cysteine as substrate1 Publication
  2. Vmax=5.9 µmol/min/mg enzyme with N-acetyl-L-histidine as substrate1 Publication
  3. Vmax=7.5 µmol/min/mg enzyme with N-acetyl-L-tyrosine as substrate1 Publication
  4. Vmax=7.9 µmol/min/mg enzyme with N-acetyl-L-phenylalanine as substrate1 Publication

pH dependencei

Optimum pH is 7.5 with S-benzyl-N-acetyl-L-cysteine as substrate, 7.6 with N-acetyl-L-histidine as substrate, 7.6 with N-acetyl-L-tyrosine as substrate, and 7.7 with N-acetyl-L-phenylalanine as substrate.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi21Zinc1
Metal bindingi24Zinc1
Binding sitei63Substrate1
Metal bindingi116Zinc1
Binding sitei177Substrate1
Binding sitei287Substrate1

GO - Molecular functioni

  • aminoacylase activity Source: UniProtKB
  • hydrolase activity, acting on ester bonds Source: InterPro
  • identical protein binding Source: MGI
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.5.1.114. 3474.
ReactomeiR-MMU-5423646. Aflatoxin activation and detoxification.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming) (EC:3.5.1.114)
Alternative name(s):
Acylase III
Aminoacylase III
Short name:
AAIII
Aminoacylase-3
Short name:
ACY-3
Aspartoacylase-2
Hepatitis C virus core-binding protein 1
Short name:
HCBP1
Gene namesi
Name:Acy3
Synonyms:Aspa2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1918920. Acy3.

Subcellular locationi

GO - Cellular componenti

  • apical plasma membrane Source: MGI
  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi63R → A: Abolishes activity. 1 Publication1
Mutagenesisi287Y → A: Drastically reduced activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002168761 – 318N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming)Add BLAST318

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei317PhosphothreonineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ91XE4.
PaxDbiQ91XE4.
PeptideAtlasiQ91XE4.
PRIDEiQ91XE4.

PTM databases

iPTMnetiQ91XE4.
PhosphoSitePlusiQ91XE4.

Expressioni

Tissue specificityi

Expressed predominantly in kidney and to a lesser extent in liver. Weakly expressed in heart, small intestine, brain, lung, testis, and stomach.1 Publication

Gene expression databases

BgeeiENSMUSG00000024866.
CleanExiMM_ACY3.
GenevisibleiQ91XE4. MM.

Interactioni

Subunit structurei

Exists as a mixture of homodimers and homotetramer, both catalytically active.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-7378963,EBI-7378963
P266646EBI-7378963,EBI-6941357From a different organism.

GO - Molecular functioni

  • identical protein binding Source: MGI

Protein-protein interaction databases

DIPiDIP-44060N.
IntActiQ91XE4. 5 interactors.
MINTiMINT-1869885.
STRINGi10090.ENSMUSP00000050056.

Structurei

Secondary structure

1318
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi13 – 18Combined sources6
Helixi25 – 36Combined sources12
Helixi38 – 41Combined sources4
Beta strandi46 – 53Combined sources8
Helixi55 – 60Combined sources6
Beta strandi65 – 67Combined sources3
Helixi69 – 71Combined sources3
Helixi75 – 78Combined sources4
Beta strandi84 – 86Combined sources3
Helixi88 – 100Combined sources13
Beta strandi110 – 117Combined sources8
Beta strandi119 – 121Combined sources3
Beta strandi123 – 130Combined sources8
Helixi133 – 145Combined sources13
Beta strandi151 – 155Combined sources5
Beta strandi159 – 161Combined sources3
Helixi167 – 169Combined sources3
Beta strandi170 – 179Combined sources10
Helixi188 – 209Combined sources22
Beta strandi217 – 228Combined sources12
Beta strandi238 – 242Combined sources5
Turni244 – 248Combined sources5
Beta strandi258 – 263Combined sources6
Beta strandi268 – 270Combined sources3
Beta strandi273 – 275Combined sources3
Beta strandi277 – 281Combined sources5
Helixi285 – 287Combined sources3
Turni288 – 291Combined sources4
Beta strandi293 – 304Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3NFZX-ray2.15A1-318[»]
3NH4X-ray2.00A1-318[»]
3NH5X-ray2.09A1-318[»]
3NH8X-ray2.80A1-318[»]
ProteinModelPortaliQ91XE4.
SMRiQ91XE4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ91XE4.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 210Hydrolytic domainAdd BLAST210
Regioni70 – 71Substrate binding2
Regioni211 – 318Shielding domainAdd BLAST108

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410IERR. Eukaryota.
COG2988. LUCA.
GeneTreeiENSGT00390000001189.
HOGENOMiHOG000232489.
HOVERGENiHBG004172.
InParanoidiQ91XE4.
KOiK18458.
OMAiTANMGTC.
OrthoDBiEOG091G0BL6.
PhylomeDBiQ91XE4.
TreeFamiTF328708.

Family and domain databases

HAMAPiMF_00704. Aspartoacylase. 1 hit.
InterProiIPR016708. Aspartoacylase.
IPR007036. Aste_AspA.
[Graphical view]
PfamiPF04952. AstE_AspA. 1 hit.
[Graphical view]
PIRSFiPIRSF018001. Aspartoacylase. 1 hit.

Sequencei

Sequence statusi: Complete.

Q91XE4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSLPGSREP LLRVAVTGGT HGNEMCGVYL ARYWLQNPGE LQRPSFSAMP
60 70 80 90 100
VLANPAATAA CCRYLDRDLN RSCTLTFLGS TATPDDPYEV KRARELNQLL
110 120 130 140 150
GPKGTGQAFD FTLDLHNTTA NTGVCLISES NISFNLHLCH YLQRQNPGMP
160 170 180 190 200
CRLFLYEPAG TETFSVESIS KNGICLEMGP QPQGVLRADL FSRMRALVAS
210 220 230 240 250
ILDFIELFNQ GMDLPAFEMD IYRNLGSVDF PRTADGDLAG TVHPQLQDHD
260 270 280 290 300
FEPLRPGEPI FKLFSGEDVL YEGDSIVYPV FINEAAYYEK HVAFLKSEKI
310
RVTVPALLRL TPRSTQTP
Length:318
Mass (Da):35,286
Last modified:December 1, 2001 - v1
Checksum:i8332731E7E9B30D2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti66D → G in AAN87897 (PubMed:14656720).Curated1
Sequence conflicti66D → G in AAM46090 (Ref. 4) Curated1
Sequence conflicti66D → G in BAB21963 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF356878 mRNA. Translation: AAM00224.1.
AF356879 mRNA. Translation: AAM00225.1.
AY040762 Genomic DNA. Translation: AAK94771.1.
AY169234 mRNA. Translation: AAN87897.1.
AF375479 mRNA. Translation: AAM46090.1.
AK002247 mRNA. Translation: BAB21963.1.
AK143782 mRNA. Translation: BAE25538.1.
BC010795 mRNA. Translation: AAH10795.1.
CCDSiCCDS29406.1.
RefSeqiNP_001289408.1. NM_001302479.1.
NP_001289409.1. NM_001302480.1.
NP_001289410.1. NM_001302481.1.
NP_001289411.1. NM_001302482.1.
UniGeneiMm.29735.

Genome annotation databases

EnsembliENSMUST00000054030; ENSMUSP00000050056; ENSMUSG00000024866.
GeneIDi71670.
KEGGimmu:71670.
UCSCiuc008fxx.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF356878 mRNA. Translation: AAM00224.1.
AF356879 mRNA. Translation: AAM00225.1.
AY040762 Genomic DNA. Translation: AAK94771.1.
AY169234 mRNA. Translation: AAN87897.1.
AF375479 mRNA. Translation: AAM46090.1.
AK002247 mRNA. Translation: BAB21963.1.
AK143782 mRNA. Translation: BAE25538.1.
BC010795 mRNA. Translation: AAH10795.1.
CCDSiCCDS29406.1.
RefSeqiNP_001289408.1. NM_001302479.1.
NP_001289409.1. NM_001302480.1.
NP_001289410.1. NM_001302481.1.
NP_001289411.1. NM_001302482.1.
UniGeneiMm.29735.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3NFZX-ray2.15A1-318[»]
3NH4X-ray2.00A1-318[»]
3NH5X-ray2.09A1-318[»]
3NH8X-ray2.80A1-318[»]
ProteinModelPortaliQ91XE4.
SMRiQ91XE4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-44060N.
IntActiQ91XE4. 5 interactors.
MINTiMINT-1869885.
STRINGi10090.ENSMUSP00000050056.

PTM databases

iPTMnetiQ91XE4.
PhosphoSitePlusiQ91XE4.

Proteomic databases

MaxQBiQ91XE4.
PaxDbiQ91XE4.
PeptideAtlasiQ91XE4.
PRIDEiQ91XE4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000054030; ENSMUSP00000050056; ENSMUSG00000024866.
GeneIDi71670.
KEGGimmu:71670.
UCSCiuc008fxx.2. mouse.

Organism-specific databases

CTDi91703.
MGIiMGI:1918920. Acy3.

Phylogenomic databases

eggNOGiENOG410IERR. Eukaryota.
COG2988. LUCA.
GeneTreeiENSGT00390000001189.
HOGENOMiHOG000232489.
HOVERGENiHBG004172.
InParanoidiQ91XE4.
KOiK18458.
OMAiTANMGTC.
OrthoDBiEOG091G0BL6.
PhylomeDBiQ91XE4.
TreeFamiTF328708.

Enzyme and pathway databases

BRENDAi3.5.1.114. 3474.
ReactomeiR-MMU-5423646. Aflatoxin activation and detoxification.

Miscellaneous databases

EvolutionaryTraceiQ91XE4.
PROiQ91XE4.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000024866.
CleanExiMM_ACY3.
GenevisibleiQ91XE4. MM.

Family and domain databases

HAMAPiMF_00704. Aspartoacylase. 1 hit.
InterProiIPR016708. Aspartoacylase.
IPR007036. Aste_AspA.
[Graphical view]
PfamiPF04952. AstE_AspA. 1 hit.
[Graphical view]
PIRSFiPIRSF018001. Aspartoacylase. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiACY3_MOUSE
AccessioniPrimary (citable) accession number: Q91XE4
Secondary accession number(s): Q3UP59, Q9DD17
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: December 1, 2001
Last modified: November 2, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.