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Q99JW2 (ACY1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length408 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) By similarity.

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 By similarity.

Subunit structure

Homodimer By similarity. Interacts with SPHK1. Ref.3

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the peptidase M20A family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome
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 By similarity
Chain2 – 408407Aminoacylase-1
PRO_0000274007

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 binding3731Zinc 2 By similarity

Experimental info

Sequence conflict1721A → V in BAB22090. Ref.1
Sequence conflict1721A → V in BAB22948. Ref.1
Sequence conflict1971R → Q in BAB22090. Ref.1
Sequence conflict1971R → Q in BAB22948. Ref.1
Sequence conflict3511Y → F in BAB22090. Ref.1
Sequence conflict3511Y → F in BAB22948. Ref.1
Sequence conflict4061G → S in BAB22090. Ref.1
Sequence conflict4061G → S in BAB22948. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q99JW2 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 384C70B9AB87CDC3

FASTA40845,781
        10         20         30         40         50         60 
MTTKDPESEH PSVTLFRQYL RICTVQPNPD YGGAITFLEE RARQLGLSCQ KIEVVPGFVI 

        70         80         90        100        110        120 
TVLTWPGTNP SLPSILLNSH TDVVPVFKEH WHHDPFEAFK DSEGYIYARG SQDMKSVSIQ 

       130        140        150        160        170        180 
YLEAVRRLKS EGHRFPRTIH MTFVPDEEVG GHKGMELFVK RPEFQALRAG FALDEGLANP 

       190        200        210        220        230        240 
TDAFTVFYSE RSPWWVRVTS TGKPGHASRF IEDTAAEKLH KVISSILAFR EKERQRLQAN 

       250        260        270        280        290        300 
PHLKEGAVTS VNLTKLEGGV AYNVVPATMS ASFDFRVAPD VDMKAFEKQL QRWCQEAGEG 

       310        320        330        340        350        360 
VTFEFAQKFT EPRMTPTDDS DPWWAAFSGA CKAMNLTLEP EIFPAATDSR YIRAVGIPAL 

       370        380        390        400 
GFSPMNRTPV LLHDHNERLH EDIFLRGVDI YTGLLSALAS VPTLPGES 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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: 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(2004) [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(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SPHK1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK003703 mRNA. Translation: BAB22948.1.
AK002423 mRNA. Translation: BAB22090.1.
BC005631 mRNA. Translation: AAH05631.1.
CCDSCCDS23477.1.
RefSeqNP_001263371.1. NM_001276442.1.
NP_079647.1. NM_025371.3.
UniGeneMm.7165.

3D structure databases

ProteinModelPortalQ99JW2.
SMRQ99JW2. Positions 7-405.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ99JW2. 3 interactions.
MINTMINT-1856196.
STRING10090.ENSMUSP00000024031.

Protein family/group databases

MEROPSM20.973.

PTM databases

PhosphoSiteQ99JW2.

2D gel databases

REPRODUCTION-2DPAGEQ99JW2.

Proteomic databases

MaxQBQ99JW2.
PaxDbQ99JW2.
PRIDEQ99JW2.

Protocols and materials databases

DNASU109652.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000024031; ENSMUSP00000024031; ENSMUSG00000023262.
GeneID109652.
KEGGmmu:109652.
UCSCuc009rjp.1. mouse.

Organism-specific databases

CTD95.
MGIMGI:87913. Acy1.

Phylogenomic databases

eggNOGCOG0624.
GeneTreeENSGT00730000111049.
HOGENOMHOG000021196.
HOVERGENHBG000982.
InParanoidQ99JW2.
KOK14677.
OrthoDBEOG7N8ZVZ.
PhylomeDBQ99JW2.
TreeFamTF313693.

Enzyme and pathway databases

BRENDA3.5.1.14. 3474.

Gene expression databases

BgeeQ99JW2.
CleanExMM_ACY1.
GenevestigatorQ99JW2.

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...

Other

NextBio362511.
PROQ99JW2.
SOURCESearch...

Entry information

Entry nameACY1_MOUSE
AccessionPrimary (citable) accession number: Q99JW2
Secondary accession number(s): Q9CR15
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 86 of the entry and version 1 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot