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P37111

- ACY1_PIG

UniProt

P37111 - ACY1_PIG

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Protein

Aminoacylase-1

Gene
ACY1
Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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.

Cofactori

Binds 2 zinc ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi80 – 801Zinc 1 By similarity
Active sitei82 – 821 By similarity
Metal bindingi113 – 1131Zinc 1 By similarity
Metal bindingi113 – 1131Zinc 2 By similarity
Active sitei147 – 1471Proton acceptor By similarity
Metal bindingi148 – 1481Zinc 2 By similarity
Metal bindingi175 – 1751Zinc 1 By similarity
Metal bindingi372 – 3721Zinc 2 By similarity

GO - Molecular functioni

  1. aminoacylase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW
  3. metallopeptidase activity Source: InterPro

GO - Biological processi

  1. cellular amino acid metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.5.1.14. 6170.
SABIO-RKP37111.

Protein family/group databases

MEROPSiM20.973.

Names & Taxonomyi

Protein namesi
Recommended name:
Aminoacylase-1 (EC:3.5.1.14)
Short name:
ACY-1
Alternative name(s):
N-acyl-L-amino-acid amidohydrolase
Gene namesi
Name:ACY1
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Chromosome 13

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 407406Aminoacylase-1PRO_0000185237Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine

Keywords - PTMi

Acetylation

Interactioni

Subunit structurei

Homodimer. Interacts with SPHK1 By similarity.

Structurei

3D structure databases

ProteinModelPortaliP37111.
SMRiP37111. Positions 7-198, 320-407.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M20A family.

Phylogenomic databases

GeneTreeiENSGT00730000111049.
HOVERGENiHBG000982.
KOiK14677.
OMAiKGMELFV.
OrthoDBiEOG7N8ZVZ.
TreeFamiTF313693.

Family and domain databases

Gene3Di3.30.70.360. 1 hit.
InterProiIPR001261. ArgE/DapE_CS.
IPR010159. N-acyl_aa_amidohydrolase.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]
PfamiPF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view]
PIRSFiPIRSF036696. ACY-1. 1 hit.
SUPFAMiSSF55031. SSF55031. 1 hit.
TIGRFAMsiTIGR01880. Ac-peptdase-euk. 1 hit.
PROSITEiPS00758. ARGE_DAPE_CPG2_1. 1 hit.
PS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P37111-1 [UniParc]FASTAAdd to Basket

« Hide

MASKGREGEH PSVTLFRQYL RIRTVQPEPD YGAAVAFLEE RARQLGLGCQ    50
KVEVVPGHVV TVLTWPGTNP TLSSILLNSH TDVVPVFKEH WSHDPFEGFK 100
DADGYIYGRG AQDMKCVSIQ YLEAVRRLKV EGHHFPRTIH MTFVPDEEVG 150
GHQGMELFVK RPEFQALRAG FALDEGLASP TDAFTVFYSE RSPWWLRVTS 200
TGKPGHGSRF IEDTAAEKLH KVINSILAFR EKEKQRLQSN QLKPGAVTSV 250
NLTMLEGGVA YNVVPATMSA CFDFRVAPDV DLKAFEEQLQ SWCQAAGEGV 300
TFEFVQKWME TQVTSTDDSD PWWAAFSGVF KDMKLALELE ICPASTDARY 350
IRAAGVPALG FSPMNHTPVL LHDHDERLHE AVFLRGVDIY TQLLSALASV 400
PALPSES 407
Length:407
Mass (Da):45,347
Last modified:January 23, 2007 - v2
Checksum:iFCB88982ADBFF3D4
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti395 – 3951Missing in CAA48565. 1 Publication
Sequence conflicti398 – 3981A → T in CAA48565. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D13514 mRNA. Translation: BAA02731.1.
X68564 mRNA. Translation: CAA48565.1.
AB017196 Genomic DNA. Translation: BAA76403.1.
PIRiJN0584.
RefSeqiNP_999061.1. NM_213896.1.
UniGeneiSsc.14528.

Genome annotation databases

EnsembliENSSSCT00000027267; ENSSSCP00000025679; ENSSSCG00000023325.
GeneIDi396930.
KEGGissc:396930.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D13514 mRNA. Translation: BAA02731.1 .
X68564 mRNA. Translation: CAA48565.1 .
AB017196 Genomic DNA. Translation: BAA76403.1 .
PIRi JN0584.
RefSeqi NP_999061.1. NM_213896.1.
UniGenei Ssc.14528.

3D structure databases

ProteinModelPortali P37111.
SMRi P37111. Positions 7-198, 320-407.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M20.973.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSSSCT00000027267 ; ENSSSCP00000025679 ; ENSSSCG00000023325 .
GeneIDi 396930.
KEGGi ssc:396930.

Organism-specific databases

CTDi 95.

Phylogenomic databases

GeneTreei ENSGT00730000111049.
HOVERGENi HBG000982.
KOi K14677.
OMAi KGMELFV.
OrthoDBi EOG7N8ZVZ.
TreeFami TF313693.

Enzyme and pathway databases

BRENDAi 3.5.1.14. 6170.
SABIO-RK P37111.

Family and domain databases

Gene3Di 3.30.70.360. 1 hit.
InterProi IPR001261. ArgE/DapE_CS.
IPR010159. N-acyl_aa_amidohydrolase.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view ]
Pfami PF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view ]
PIRSFi PIRSF036696. ACY-1. 1 hit.
SUPFAMi SSF55031. SSF55031. 1 hit.
TIGRFAMsi TIGR01880. Ac-peptdase-euk. 1 hit.
PROSITEi PS00758. ARGE_DAPE_CPG2_1. 1 hit.
PS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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].

Entry informationi

Entry nameiACY1_PIG
AccessioniPrimary (citable) accession number: P37111
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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