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P37111 (ACY1_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Aminoacylase-1

Short name=ACY-1
EC=3.5.1.14
Alternative name(s):
N-acyl-L-amino-acid amidohydrolase
Gene names
Name:ACY1
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length407 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate).

Catalytic activity

An N-acyl-aliphatic-L-amino acid + H2O = an aliphatic L-amino acid + a carboxylate.

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

Cofactor

Binds 2 zinc ions per subunit.

Subunit structure

Homodimer. Interacts with SPHK1 By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the peptidase M20A family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular amino acid metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionaminoacylase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

metallopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 407406Aminoacylase-1
PRO_0000185237

Sites

Active site821 By similarity
Active site1471Proton acceptor By similarity
Metal binding801Zinc 1 By similarity
Metal binding1131Zinc 1 By similarity
Metal binding1131Zinc 2 By similarity
Metal binding1481Zinc 2 By similarity
Metal binding1751Zinc 1 By similarity
Metal binding3721Zinc 2 By similarity

Amino acid modifications

Modified residue21N-acetylalanine

Experimental info

Sequence conflict3951Missing in CAA48565. Ref.2
Sequence conflict3981A → T in CAA48565. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P37111 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: FCB88982ADBFF3D4

FASTA40745,347
        10         20         30         40         50         60 
MASKGREGEH PSVTLFRQYL RIRTVQPEPD YGAAVAFLEE RARQLGLGCQ KVEVVPGHVV 

        70         80         90        100        110        120 
TVLTWPGTNP TLSSILLNSH TDVVPVFKEH WSHDPFEGFK DADGYIYGRG AQDMKCVSIQ 

       130        140        150        160        170        180 
YLEAVRRLKV EGHHFPRTIH MTFVPDEEVG GHQGMELFVK RPEFQALRAG FALDEGLASP 

       190        200        210        220        230        240 
TDAFTVFYSE RSPWWLRVTS TGKPGHGSRF IEDTAAEKLH KVINSILAFR EKEKQRLQSN 

       250        260        270        280        290        300 
QLKPGAVTSV NLTMLEGGVA YNVVPATMSA CFDFRVAPDV DLKAFEEQLQ SWCQAAGEGV 

       310        320        330        340        350        360 
TFEFVQKWME TQVTSTDDSD PWWAAFSGVF KDMKLALELE ICPASTDARY IRAAGVPALG 

       370        380        390        400 
FSPMNHTPVL LHDHDERLHE AVFLRGVDIY TQLLSALASV PALPSES 

« Hide

References

[1]"The primary structure of porcine aminoacylase 1 deduced from cDNA sequence."
Mitta M., Ohnogi H., Yamamoto A., Kato I., Sakiyama F., Tsunasawa S.
J. Biochem. 112:737-742(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Kidney.
[2]"Cloning and sequence analyses of cDNAs encoding aminoacylase I from porcine kidney."
Jakob M., Miller Y.E., Roehm K.H.
Biol. Chem. Hoppe-Seyler 373:1227-1231(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[3]"Porcine cosmid clone containing the ACY-1 and rpL29/HIP genes."
Sawazaki T., Hamasima N.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D13514 mRNA. Translation: BAA02731.1.
X68564 mRNA. Translation: CAA48565.1.
AB017196 Genomic DNA. Translation: BAA76403.1.
PIRJN0584.
RefSeqNP_999061.1. NM_213896.1.
UniGeneSsc.14528.

3D structure databases

ProteinModelPortalP37111.
SMRP37111. Positions 7-198, 320-407.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM20.973.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSSSCT00000027267; ENSSSCP00000025679; ENSSSCG00000023325.
GeneID396930.
KEGGssc:396930.

Organism-specific databases

CTD95.

Phylogenomic databases

GeneTreeENSGT00730000111049.
HOVERGENHBG000982.
KOK14677.
OMAKGMELFV.
OrthoDBEOG7N8ZVZ.
TreeFamTF313693.

Enzyme and pathway databases

BRENDA3.5.1.14. 6170.
SABIO-RKP37111.

Family and domain databases

Gene3D3.30.70.360. 1 hit.
InterProIPR001261. ArgE/DapE_CS.
IPR010159. N-acyl_aa_amidohydrolase.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]
PfamPF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view]
PIRSFPIRSF036696. ACY-1. 1 hit.
SUPFAMSSF55031. SSF55031. 1 hit.
TIGRFAMsTIGR01880. Ac-peptdase-euk. 1 hit.
PROSITEPS00758. ARGE_DAPE_CPG2_1. 1 hit.
PS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACY1_PIG
AccessionPrimary (citable) accession number: P37111
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries