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Protein

Aspartoacylase

Gene

Aspa

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the deacetylation of N-acetylaspartic acid (NAA) to produce acetate and L-aspartate. NAA occurs in high concentration in brain and its hydrolysis NAA plays a significant part in the maintenance of intact white matter (By similarity).By similarity

Catalytic activityi

N-acyl-L-aspartate + H2O = a carboxylate + L-aspartate.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi20 – 201ZincBy similarity
Metal bindingi23 – 231ZincBy similarity
Binding sitei62 – 621SubstrateBy similarity
Metal bindingi115 – 1151ZincBy similarity
Active sitei177 – 1771By similarity
Binding sitei177 – 1771SubstrateBy similarity
Binding sitei287 – 2871SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

  • acetate metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.5.1.15. 3474.
ReactomeiR-MMU-70614. Amino acid synthesis and interconversion (transamination).

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartoacylase (EC:3.5.1.15)
Alternative name(s):
Aminoacylase-2
Short name:
ACY-2
Gene namesi
Name:Aspa
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:87914. Aspa.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: UniProtKB
  • extracellular exosome Source: MGI
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 312312AspartoacylasePRO_0000216873Add
BLAST

Proteomic databases

MaxQBiQ8R3P0.
PaxDbiQ8R3P0.
PRIDEiQ8R3P0.

PTM databases

iPTMnetiQ8R3P0.
PhosphoSiteiQ8R3P0.

Expressioni

Gene expression databases

BgeeiQ8R3P0.
CleanExiMM_ASPA.
ExpressionAtlasiQ8R3P0. baseline and differential.
GenevisibleiQ8R3P0. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiQ8R3P0. 1 interaction.
MINTiMINT-4086826.
STRINGi10090.ENSMUSP00000021119.

Structurei

3D structure databases

ProteinModelPortaliQ8R3P0.
SMRiQ8R3P0. Positions 4-310.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni69 – 702Substrate bindingBy similarity
Regioni163 – 1675Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410IERR. Eukaryota.
COG2988. LUCA.
GeneTreeiENSGT00390000001189.
HOGENOMiHOG000232489.
HOVERGENiHBG004172.
InParanoidiQ8R3P0.
KOiK01437.
OMAiNFNEGKE.
OrthoDBiEOG78SQJ6.
PhylomeDBiQ8R3P0.
TreeFamiTF328708.

Family and domain databases

HAMAPiMF_00704. Aspartoacylase.
InterProiIPR016708. Aspartoacylase.
IPR007036. Aste_AspA.
[Graphical view]
PfamiPF04952. AstE_AspA. 1 hit.
[Graphical view]
PIRSFiPIRSF018001. Aspartoacylase. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8R3P0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSCVAKEPI KKIAIFGGTH GNELTGVFLV THWLRNGTEV HRAGLDVKPF
60 70 80 90 100
ITNPRAVEKC TRYIDCDLNR VFDLENLSKE MSEDLPYEVR RAQEINHLFG
110 120 130 140 150
PKNSDDAYDL VFDLHNTTSN MGCTLILEDS RNDFLIQMFH YIKTCMAPLP
160 170 180 190 200
CSVYLIEHPS LKYATTRSIA KYPVGIEVGP QPHGVLRADI LDQMRKMIKH
210 220 230 240 250
ALDFIQHFNE GKEFPPCSID VYKIMEKVDY PRNESGDMAA VIHPNLQDQD
260 270 280 290 300
WKPLHPGDPV FVSLDGKVIP LGGDCTVYPV FVNEAAYYEK KEAFAKTTKL
310
TLSAKSIRST LH
Length:312
Mass (Da):35,345
Last modified:May 1, 2007 - v2
Checksum:iF09E710CC3107108
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti110 – 1101L → I in AAF76459 (PubMed:10837925).Curated
Sequence conflicti110 – 1101L → I in AAH24934 (PubMed:15489334).Curated
Sequence conflicti153 – 1531V → G in BAB25624 (PubMed:16141072).Curated
Sequence conflicti160 – 1601S → L in BAB25624 (PubMed:16141072).Curated
Sequence conflicti275 – 2751C → Y in BAB25624 (PubMed:16141072).Curated
Sequence conflicti312 – 3121H → P in AAF76459 (PubMed:10837925).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF212998 mRNA. Translation: AAF76459.1.
AK002859 mRNA. Translation: BAB22412.1.
AK008354 mRNA. Translation: BAB25624.1.
AL645739 Genomic DNA. Translation: CAI24567.1.
BC024934 mRNA. Translation: AAH24934.1.
CCDSiCCDS25005.1.
RefSeqiNP_075602.2. NM_023113.5.
XP_006532073.2. XM_006532010.2.
XP_006532074.1. XM_006532011.1.
XP_006532075.1. XM_006532012.2.
XP_006536348.2. XM_006536285.2.
XP_006536349.1. XM_006536286.1.
XP_006536350.1. XM_006536287.2.
UniGeneiMm.293574.

Genome annotation databases

EnsembliENSMUST00000021119; ENSMUSP00000021119; ENSMUSG00000020774.
ENSMUST00000184572; ENSMUSP00000139318; ENSMUSG00000020774.
GeneIDi11484.
KEGGimmu:11484.
UCSCiuc007kal.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF212998 mRNA. Translation: AAF76459.1.
AK002859 mRNA. Translation: BAB22412.1.
AK008354 mRNA. Translation: BAB25624.1.
AL645739 Genomic DNA. Translation: CAI24567.1.
BC024934 mRNA. Translation: AAH24934.1.
CCDSiCCDS25005.1.
RefSeqiNP_075602.2. NM_023113.5.
XP_006532073.2. XM_006532010.2.
XP_006532074.1. XM_006532011.1.
XP_006532075.1. XM_006532012.2.
XP_006536348.2. XM_006536285.2.
XP_006536349.1. XM_006536286.1.
XP_006536350.1. XM_006536287.2.
UniGeneiMm.293574.

3D structure databases

ProteinModelPortaliQ8R3P0.
SMRiQ8R3P0. Positions 4-310.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8R3P0. 1 interaction.
MINTiMINT-4086826.
STRINGi10090.ENSMUSP00000021119.

PTM databases

iPTMnetiQ8R3P0.
PhosphoSiteiQ8R3P0.

Proteomic databases

MaxQBiQ8R3P0.
PaxDbiQ8R3P0.
PRIDEiQ8R3P0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000021119; ENSMUSP00000021119; ENSMUSG00000020774.
ENSMUST00000184572; ENSMUSP00000139318; ENSMUSG00000020774.
GeneIDi11484.
KEGGimmu:11484.
UCSCiuc007kal.2. mouse.

Organism-specific databases

CTDi443.
MGIiMGI:87914. Aspa.

Phylogenomic databases

eggNOGiENOG410IERR. Eukaryota.
COG2988. LUCA.
GeneTreeiENSGT00390000001189.
HOGENOMiHOG000232489.
HOVERGENiHBG004172.
InParanoidiQ8R3P0.
KOiK01437.
OMAiNFNEGKE.
OrthoDBiEOG78SQJ6.
PhylomeDBiQ8R3P0.
TreeFamiTF328708.

Enzyme and pathway databases

BRENDAi3.5.1.15. 3474.
ReactomeiR-MMU-70614. Amino acid synthesis and interconversion (transamination).

Miscellaneous databases

NextBioi278840.
PROiQ8R3P0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8R3P0.
CleanExiMM_ASPA.
ExpressionAtlasiQ8R3P0. baseline and differential.
GenevisibleiQ8R3P0. MM.

Family and domain databases

HAMAPiMF_00704. Aspartoacylase.
InterProiIPR016708. Aspartoacylase.
IPR007036. Aste_AspA.
[Graphical view]
PfamiPF04952. AstE_AspA. 1 hit.
[Graphical view]
PIRSFiPIRSF018001. Aspartoacylase. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Murine aspartoacylase: cloning, expression and comparison with the human enzyme."
    Namboodiri M.A., Corigliano-Murphy A., Jiang G., Rollag M., Provencio I.
    Brain Res. Mol. Brain Res. 77:285-289(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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: Kidney and Small intestine.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "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].
  5. Lubec G., Klug S.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 172-187 AND 200-212, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hippocampus.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney and Liver.

Entry informationi

Entry nameiACY2_MOUSE
AccessioniPrimary (citable) accession number: Q8R3P0
Secondary accession number(s): Q5SV07
, Q9D876, Q9DCE2, Q9JIN8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: May 1, 2007
Last modified: February 17, 2016
This is version 114 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.