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Protein

Aminoacylase-1

Gene

Acy1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

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

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi80 – 801Zinc 1By similarity
Active sitei82 – 821By similarity
Metal bindingi113 – 1131Zinc 1By similarity
Metal bindingi113 – 1131Zinc 2By similarity
Active sitei147 – 1471Proton acceptorBy similarity
Metal bindingi148 – 1481Zinc 2By similarity
Metal bindingi175 – 1751Zinc 1By similarity
Metal bindingi373 – 3731Zinc 2By 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. 3474.
ReactomeiREACT_288150. Aflatoxin activation and detoxification.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:87913. Acy1.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. extracellular vesicular exosome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 408408Aminoacylase-1PRO_0000274007Add
BLAST

Proteomic databases

MaxQBiQ99JW2.
PaxDbiQ99JW2.
PRIDEiQ99JW2.

2D gel databases

REPRODUCTION-2DPAGEQ99JW2.

PTM databases

PhosphoSiteiQ99JW2.

Expressioni

Gene expression databases

BgeeiQ99JW2.
CleanExiMM_ACY1.
GenevestigatoriQ99JW2.

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with SPHK1.By similarity1 Publication

Protein-protein interaction databases

IntActiQ99JW2. 3 interactions.
MINTiMINT-1856196.
STRINGi10090.ENSMUSP00000024031.

Structurei

3D structure databases

ProteinModelPortaliQ99JW2.
SMRiQ99JW2. Positions 7-405.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M20A family.Curated

Phylogenomic databases

eggNOGiCOG0624.
HOGENOMiHOG000021196.
HOVERGENiHBG000982.
InParanoidiQ99JW2.
KOiK14677.
OrthoDBiEOG7N8ZVZ.
PhylomeDBiQ99JW2.
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.

Q99JW2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTKDPESEH PSVTLFRQYL RICTVQPNPD YGGAITFLEE RARQLGLSCQ
60 70 80 90 100
KIEVVPGFVI TVLTWPGTNP SLPSILLNSH TDVVPVFKEH WHHDPFEAFK
110 120 130 140 150
DSEGYIYARG SQDMKSVSIQ YLEAVRRLKS EGHRFPRTIH MTFVPDEEVG
160 170 180 190 200
GHKGMELFVK RPEFQALRAG FALDEGLANP TDAFTVFYSE RSPWWVRVTS
210 220 230 240 250
TGKPGHASRF IEDTAAEKLH KVISSILAFR EKERQRLQAN PHLKEGAVTS
260 270 280 290 300
VNLTKLEGGV AYNVVPATMS ASFDFRVAPD VDMKAFEKQL QRWCQEAGEG
310 320 330 340 350
VTFEFAQKFT EPRMTPTDDS DPWWAAFSGA CKAMNLTLEP EIFPAATDSR
360 370 380 390 400
YIRAVGIPAL GFSPMNRTPV LLHDHNERLH EDIFLRGVDI YTGLLSALAS

VPTLPGES
Length:408
Mass (Da):45,781
Last modified:May 31, 2001 - v1
Checksum:i384C70B9AB87CDC3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti172 – 1721A → V in BAB22090 (PubMed:16141072).Curated
Sequence conflicti172 – 1721A → V in BAB22948 (PubMed:16141072).Curated
Sequence conflicti197 – 1971R → Q in BAB22090 (PubMed:16141072).Curated
Sequence conflicti197 – 1971R → Q in BAB22948 (PubMed:16141072).Curated
Sequence conflicti351 – 3511Y → F in BAB22090 (PubMed:16141072).Curated
Sequence conflicti351 – 3511Y → F in BAB22948 (PubMed:16141072).Curated
Sequence conflicti406 – 4061G → S in BAB22090 (PubMed:16141072).Curated
Sequence conflicti406 – 4061G → S in BAB22948 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003703 mRNA. Translation: BAB22948.1.
AK002423 mRNA. Translation: BAB22090.1.
BC005631 mRNA. Translation: AAH05631.1.
CCDSiCCDS23477.1.
RefSeqiNP_001263371.1. NM_001276442.1.
NP_079647.1. NM_025371.3.
UniGeneiMm.7165.

Genome annotation databases

GeneIDi109652.
KEGGimmu:109652.
UCSCiuc009rjp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003703 mRNA. Translation: BAB22948.1.
AK002423 mRNA. Translation: BAB22090.1.
BC005631 mRNA. Translation: AAH05631.1.
CCDSiCCDS23477.1.
RefSeqiNP_001263371.1. NM_001276442.1.
NP_079647.1. NM_025371.3.
UniGeneiMm.7165.

3D structure databases

ProteinModelPortaliQ99JW2.
SMRiQ99JW2. Positions 7-405.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ99JW2. 3 interactions.
MINTiMINT-1856196.
STRINGi10090.ENSMUSP00000024031.

Protein family/group databases

MEROPSiM20.973.

PTM databases

PhosphoSiteiQ99JW2.

2D gel databases

REPRODUCTION-2DPAGEQ99JW2.

Proteomic databases

MaxQBiQ99JW2.
PaxDbiQ99JW2.
PRIDEiQ99JW2.

Protocols and materials databases

DNASUi109652.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi109652.
KEGGimmu:109652.
UCSCiuc009rjp.1. mouse.

Organism-specific databases

CTDi95.
MGIiMGI:87913. Acy1.

Phylogenomic databases

eggNOGiCOG0624.
HOGENOMiHOG000021196.
HOVERGENiHBG000982.
InParanoidiQ99JW2.
KOiK14677.
OrthoDBiEOG7N8ZVZ.
PhylomeDBiQ99JW2.
TreeFamiTF313693.

Enzyme and pathway databases

BRENDAi3.5.1.14. 3474.
ReactomeiREACT_288150. Aflatoxin activation and detoxification.

Miscellaneous databases

NextBioi362511.
PROiQ99JW2.
SOURCEiSearch...

Gene expression databases

BgeeiQ99JW2.
CleanExiMM_ACY1.
GenevestigatoriQ99JW2.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo and Kidney.
  2. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. "Aminoacylase 1 is a sphingosine kinase 1-interacting protein."
    Maceyka M., Nava V.E., Milstien S., Spiegel S.
    FEBS Lett. 568:30-34(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPHK1.

Entry informationi

Entry nameiACY1_MOUSE
AccessioniPrimary (citable) accession number: Q99JW2
Secondary accession number(s): Q9CR15
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 22, 2007
Last sequence update: May 31, 2001
Last modified: March 31, 2015
This is version 93 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.