Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi21 – 211Zinc
Metal bindingi24 – 241Zinc
Binding sitei63 – 631Substrate
Metal bindingi116 – 1161Zinc
Binding sitei177 – 1771Substrate
Binding sitei287 – 2871Substrate

GO - Molecular functioni

  • aminoacylase activity Source: UniProtKB
  • hydrolase activity, acting on ester bonds Source: InterPro
  • identical protein binding Source: IntAct
  • 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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi63 – 631R → A: Abolishes activity. 1 Publication
Mutagenesisi287 – 2871Y → A: Drastically reduced activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 318318N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming)PRO_0000216876Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei317 – 3171PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ91XE4.
MaxQBiQ91XE4.
PaxDbiQ91XE4.
PeptideAtlasiQ91XE4.
PRIDEiQ91XE4.

PTM databases

iPTMnetiQ91XE4.
PhosphoSiteiQ91XE4.

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

BgeeiQ91XE4.
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: IntAct

Protein-protein interaction databases

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

Structurei

Secondary structure

1
318
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi13 – 186Combined sources
Helixi25 – 3612Combined sources
Helixi38 – 414Combined sources
Beta strandi46 – 538Combined sources
Helixi55 – 606Combined sources
Beta strandi65 – 673Combined sources
Helixi69 – 713Combined sources
Helixi75 – 784Combined sources
Beta strandi84 – 863Combined sources
Helixi88 – 10013Combined sources
Beta strandi110 – 1178Combined sources
Beta strandi119 – 1213Combined sources
Beta strandi123 – 1308Combined sources
Helixi133 – 14513Combined sources
Beta strandi151 – 1555Combined sources
Beta strandi159 – 1613Combined sources
Helixi167 – 1693Combined sources
Beta strandi170 – 17910Combined sources
Helixi188 – 20922Combined sources
Beta strandi217 – 22812Combined sources
Beta strandi238 – 2425Combined sources
Turni244 – 2485Combined sources
Beta strandi258 – 2636Combined sources
Beta strandi268 – 2703Combined sources
Beta strandi273 – 2753Combined sources
Beta strandi277 – 2815Combined sources
Helixi285 – 2873Combined sources
Turni288 – 2914Combined sources
Beta strandi293 – 30412Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NFZX-ray2.15A1-318[»]
3NH4X-ray2.00A1-318[»]
3NH5X-ray2.09A1-318[»]
3NH8X-ray2.80A1-318[»]
ProteinModelPortaliQ91XE4.
SMRiQ91XE4. Positions 7-309.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ91XE4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 210210Hydrolytic domainAdd
BLAST
Regioni70 – 712Substrate binding
Regioni211 – 318108Shielding domainAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410IERR. Eukaryota.
COG2988. LUCA.
GeneTreeiENSGT00390000001189.
HOGENOMiHOG000232489.
HOVERGENiHBG004172.
InParanoidiQ91XE4.
KOiK18458.
OMAiTANMGTC.
OrthoDBiEOG78SQJ6.
PhylomeDBiQ91XE4.
TreeFamiTF328708.

Family and domain databases

HAMAPiMF_00704. Aspartoacylase.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti66 – 661D → G in AAN87897 (PubMed:14656720).Curated
Sequence conflicti66 – 661D → G in AAM46090 (Ref. 4) Curated
Sequence conflicti66 – 661D → G in BAB21963 (PubMed:16141072).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
3NFZX-ray2.15A1-318[»]
3NH4X-ray2.00A1-318[»]
3NH5X-ray2.09A1-318[»]
3NH8X-ray2.80A1-318[»]
ProteinModelPortaliQ91XE4.
SMRiQ91XE4. Positions 7-309.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiQ91XE4.
PhosphoSiteiQ91XE4.

Proteomic databases

EPDiQ91XE4.
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.
OrthoDBiEOG78SQJ6.
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

BgeeiQ91XE4.
CleanExiMM_ACY3.
GenevisibleiQ91XE4. MM.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "The mouse aspartoacylase-3 gene (ACY-3) generates two mRNA isoforms by alternative splicing of 5' untranslated region."
    Chen H., Peng J., Huang C.-H.
    Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
    Tissue: Kidney.
  2. "Identification of a novel aspartoacylase homolog (ACY-3) in human and mouse kidneys."
    Huang C.-H., Chen H., Peng J., Chen Y.
    Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: BALB/cJ.
  3. "Structural characterization, tissue distribution, and functional expression of murine aminoacylase III."
    Pushkin A., Carpenito G., Abuladze N., Newman D., Tsuprun V., Ryazantsev S., Motemoturu S., Sassani P., Solovieva N., Dukkipati R., Kurtz I.
    Am. J. Physiol. 286:C848-C856(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: C57BL/6J.
  4. "Cloning and sequence analysis of cDNA encoding hepatitis C virus core-binding protein 1 (HCBP1) from mouse."
    Li K., Cheng J., Zhang L., Wang L., Lu Y., Wang G., Liu Y.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Kidney and Spleen.
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  7. "Specificity of aminoacylase III-mediated deacetylation of mercapturic acids."
    Newman D., Abuladze N., Scholz K., Dekant W., Tsuprun V., Ryazantsev S., Bondar G., Sassani P., Kurtz I., Pushkin A.
    Drug Metab. Dispos. 35:43-50(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen and Testis.
  9. "Structural characterization of dimeric murine aminoacylase III."
    Ryazantsev S., Abuladze N., Newman D., Bondar G., Kurtz I., Pushkin A.
    FEBS Lett. 581:1898-1902(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (16 ANGSTROMS), SUBUNIT.
  10. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATES, ZINC-BINDING SITES, SUBUNIT, COFACTOR, MUTAGENESIS OF ARG-63 AND TYR-287.

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: July 6, 2016
This is version 115 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.