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Q99JW2

- ACY1_MOUSE

UniProt

Q99JW2 - ACY1_MOUSE

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Protein

Aminoacylase-1

Gene
Acy1
Organism
Mus musculus (Mouse)
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) 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

Binds 2 zinc ions per subunit By similarity.

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 bindingi373 – 3731Zinc 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. 3474.

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: Chromosome 9

Organism-specific databases

MGIiMGI:87913. Acy1.

Subcellular locationi

Cytoplasm By similarity

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 By similarity
Chaini2 – 408407Aminoacylase-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 SPHK1.1 Publication

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ99JW2.
SMRiQ99JW2. Positions 7-405.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M20A family.

Phylogenomic databases

eggNOGiCOG0624.
GeneTreeiENSGT00730000111049.
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.

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

Q99JW2-1 [UniParc]FASTAAdd to Basket

« Hide

MTTKDPESEH PSVTLFRQYL RICTVQPNPD YGGAITFLEE RARQLGLSCQ    50
KIEVVPGFVI TVLTWPGTNP SLPSILLNSH TDVVPVFKEH WHHDPFEAFK 100
DSEGYIYARG SQDMKSVSIQ YLEAVRRLKS EGHRFPRTIH MTFVPDEEVG 150
GHKGMELFVK RPEFQALRAG FALDEGLANP TDAFTVFYSE RSPWWVRVTS 200
TGKPGHASRF IEDTAAEKLH KVISSILAFR EKERQRLQAN PHLKEGAVTS 250
VNLTKLEGGV AYNVVPATMS ASFDFRVAPD VDMKAFEKQL QRWCQEAGEG 300
VTFEFAQKFT EPRMTPTDDS DPWWAAFSGA CKAMNLTLEP EIFPAATDSR 350
YIRAVGIPAL GFSPMNRTPV LLHDHNERLH EDIFLRGVDI YTGLLSALAS 400
VPTLPGES 408
Length:408
Mass (Da):45,781
Last modified:June 1, 2001 - v1
Checksum:i384C70B9AB87CDC3
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti172 – 1721A → V in BAB22090. 1 Publication
Sequence conflicti172 – 1721A → V in BAB22948. 1 Publication
Sequence conflicti197 – 1971R → Q in BAB22090. 1 Publication
Sequence conflicti197 – 1971R → Q in BAB22948. 1 Publication
Sequence conflicti351 – 3511Y → F in BAB22090. 1 Publication
Sequence conflicti351 – 3511Y → F in BAB22948. 1 Publication
Sequence conflicti406 – 4061G → S in BAB22090. 1 Publication
Sequence conflicti406 – 4061G → S in BAB22948. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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

EnsembliENSMUST00000024031; ENSMUSP00000024031; ENSMUSG00000023262.
GeneIDi109652.
KEGGimmu:109652.
UCSCiuc009rjp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK003703 mRNA. Translation: BAB22948.1 .
AK002423 mRNA. Translation: BAB22090.1 .
BC005631 mRNA. Translation: AAH05631.1 .
CCDSi CCDS23477.1.
RefSeqi NP_001263371.1. NM_001276442.1.
NP_079647.1. NM_025371.3.
UniGenei Mm.7165.

3D structure databases

ProteinModelPortali Q99JW2.
SMRi Q99JW2. Positions 7-405.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q99JW2. 3 interactions.
MINTi MINT-1856196.
STRINGi 10090.ENSMUSP00000024031.

Protein family/group databases

MEROPSi M20.973.

PTM databases

PhosphoSitei Q99JW2.

2D gel databases

REPRODUCTION-2DPAGE Q99JW2.

Proteomic databases

MaxQBi Q99JW2.
PaxDbi Q99JW2.
PRIDEi Q99JW2.

Protocols and materials databases

DNASUi 109652.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000024031 ; ENSMUSP00000024031 ; ENSMUSG00000023262 .
GeneIDi 109652.
KEGGi mmu:109652.
UCSCi uc009rjp.1. mouse.

Organism-specific databases

CTDi 95.
MGIi MGI:87913. Acy1.

Phylogenomic databases

eggNOGi COG0624.
GeneTreei ENSGT00730000111049.
HOGENOMi HOG000021196.
HOVERGENi HBG000982.
InParanoidi Q99JW2.
KOi K14677.
OrthoDBi EOG7N8ZVZ.
PhylomeDBi Q99JW2.
TreeFami TF313693.

Enzyme and pathway databases

BRENDAi 3.5.1.14. 3474.

Miscellaneous databases

NextBioi 362511.
PROi Q99JW2.
SOURCEi Search...

Gene expression databases

Bgeei Q99JW2.
CleanExi MM_ACY1.
Genevestigatori Q99JW2.

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

« 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(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.

Entry informationi

Entry nameiACY1_MOUSE
AccessioniPrimary (citable) accession number: Q99JW2
Secondary accession number(s): Q9CR15
Entry historyi
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 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

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