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Q96HD9 (ACY3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming)

EC=3.5.1.114
Alternative name(s):
Acylase III
Aminoacylase-3
Short name=ACY-3
Aspartoacylase-2
Hepatitis C virus core-binding protein 1
Short name=HCBP1
Short name=HCV core-binding protein 1
Gene names
Name:ACY3
Synonyms:ASPA2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length319 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays an important role in deacetylating mercapturic acids in kidney proximal tubules. Also acts on N-acetyl-aromatic amino acids By similarity. HAMAP-Rule MF_00704

Catalytic activity

An N-acyl-aromatic-L-amino acid + H2O = an aromatic-L-amino acid + a carboxylate. HAMAP-Rule MF_00704

An N-acetyl-L-cysteine-S-conjugate + H2O = an L-cysteine-S-conjugate + acetate. HAMAP-Rule MF_00704

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_00704

Subunit structure

Exists as a mixture of homodimers and homotetramer, both catalytically active By similarity. Interacts with HCV core protein. Ref.4

Subcellular location

Apical cell membrane; Peripheral membrane protein. Cytoplasm. Note: Predominantly localized in the apical membrane of cells in the S1 segment. In the proximal straight tubules (S2 and S3 segments) is expressed diffusely throughout the cytoplasm. Ref.4

Sequence similarities

Belongs to the AspA/AstE family. Aspartoacylase subfamily.

Ontologies

Keywords
   Biological processHost-virus interaction
   Cellular componentCell membrane
Cytoplasm
Membrane
   Coding sequence diversityPolymorphism
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processviral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentapical plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

   Molecular_functionaminoacylase activity

Inferred from sequence or structural similarity. Source: UniProt

hydrolase activity, acting on ester bonds

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 319319N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming) HAMAP-Rule MF_00704
PRO_0000216875

Regions

Region1 – 210210Hydrolytic domain By similarity
Region70 – 712Substrate binding By similarity
Region211 – 318108Shielding domain By similarity

Sites

Metal binding211Zinc By similarity
Metal binding241Zinc By similarity
Metal binding1161Zinc By similarity
Binding site631Substrate By similarity
Binding site1781Substrate By similarity
Binding site2881Substrate By similarity

Natural variations

Natural variant81R → Q.
Corresponds to variant rs948445 [ dbSNP | Ensembl ].
VAR_048341
Natural variant2811V → M.
Corresponds to variant rs2290959 [ dbSNP | Ensembl ].
VAR_048342

Sequences

Sequence LengthMass (Da)Tools
Q96HD9 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 2595358AC8B5BEFB

FASTA31935,241
        10         20         30         40         50         60 
MCSLPVPREP LRRVAVTGGT HGNEMSGVYL ARHWLHAPAE LQRASFSAVP VLANPAATSG 

        70         80         90        100        110        120 
CRRYVDHDLN RTFTSSFLNS RPTPDDPYEV TRARELNQLL GPKASGQAFD FVLDLHNTTA 

       130        140        150        160        170        180 
NMGTCLIAKS SHEVFAMHLC RHLQLQYPEL SCQVFLYQRS GEESYNLDSV AKNGLGLELG 

       190        200        210        220        230        240 
PQPQGVLRAD IFSRMRTLVA TVLDFIELFN QGTAFPAFEM EAYRPVGVVD FPRTEAGHLA 

       250        260        270        280        290        300 
GTVHPQLQDR DFQPLQPGAP IFQMFSGEDL LYEGESTVYP VFINEAAYYE KGVAFVQTEK 

       310 
FTFTVPAMPA LTPAPSPAS 

« Hide

References

« Hide 'large scale' references
[1]"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 [MRNA].
[2]Pushkin A., Carpenito G., Abuladze N., Newman D., Kurtz I.
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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: Colon.
[4]"Identification of a novel protein binding to hepatitis C virus core protein."
Chen Y.R., Chen T.Y., Zhang S.L., Lin S.M., Zhao Y.R., Ye F., Zhang X., Shi L., Dang S.S., Liu M.
J. Gastroenterol. Hepatol. 24:1300-1304(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HCV CORE PROTEIN, SUBCELLULAR LOCATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY040761 mRNA. Translation: AAK94770.1.
AY169233 mRNA. Translation: AAN87896.1.
BC008689 mRNA. Translation: AAH08689.1.
RefSeqNP_542389.1. NM_080658.1.
UniGeneHs.126265.

3D structure databases

ProteinModelPortalQ96HD9.
SMRQ96HD9. Positions 8-308.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124869. 4 interactions.
IntActQ96HD9. 4 interactions.
STRING9606.ENSP00000255082.

Chemistry

DrugBankDB00128. L-Aspartic Acid.

PTM databases

PhosphoSiteQ96HD9.

Polymorphism databases

DMDM34395507.

Proteomic databases

PaxDbQ96HD9.
PRIDEQ96HD9.

Protocols and materials databases

DNASU91703.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000255082; ENSP00000255082; ENSG00000132744.
GeneID91703.
KEGGhsa:91703.
UCSCuc001omq.3. human.

Organism-specific databases

CTD91703.
GeneCardsGC11M067411.
HGNCHGNC:24104. ACY3.
HPAHPA039219.
MIM614413. gene.
neXtProtNX_Q96HD9.
PharmGKBPA134936640.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2988.
HOGENOMHOG000232489.
HOVERGENHBG004172.
InParanoidQ96HD9.
KOK01437.
OMAVFAMHLC.
OrthoDBEOG78SQJ6.
PhylomeDBQ96HD9.
TreeFamTF328708.

Enzyme and pathway databases

BioCycMetaCyc:HS13441-MONOMER.

Gene expression databases

ArrayExpressQ96HD9.
BgeeQ96HD9.
CleanExHS_ACY3.
GenevestigatorQ96HD9.

Family and domain databases

HAMAPMF_00704. Aspartoacylase.
InterProIPR016708. Aspartoacylase.
IPR007036. Aste_AspA.
[Graphical view]
PfamPF04952. AstE_AspA. 1 hit.
[Graphical view]
PIRSFPIRSF018001. Aspartoacylase. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi91703.
NextBio77411.
PROQ96HD9.
SOURCESearch...

Entry information

Entry nameACY3_HUMAN
AccessionPrimary (citable) accession number: Q96HD9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: December 1, 2001
Last modified: March 19, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM