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Protein

Aspartoacylase

Gene

Aspa

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 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.1 Publication

Cofactori

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

Sites

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

GO - Molecular functioni

  • aspartoacylase activity Source: RGD
  • hydrolase activity, acting on ester bonds Source: InterPro
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • central nervous system myelination Source: RGD
  • metabolic process Source: InterPro
  • positive regulation of oligodendrocyte differentiation Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.5.1.15. 5301.
ReactomeiR-RNO-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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi621693. Aspa.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • nucleus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 312312AspartoacylasePRO_0000216874Add
BLAST

Proteomic databases

PaxDbiQ9R1T5.
PRIDEiQ9R1T5.

PTM databases

iPTMnetiQ9R1T5.

Expressioni

Tissue specificityi

Detected in kidney proximal tubule cells (at protein level).1 Publication

Gene expression databases

ExpressionAtlasiQ9R1T5. baseline and differential.
GenevisibleiQ9R1T5. RN.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

DIPiDIP-60794N.
STRINGi10116.ENSRNOP00000050760.

Structurei

Secondary structure

1
312
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 73Combined sources
Beta strandi13 – 175Combined sources
Helixi24 – 3512Combined sources
Helixi38 – 403Combined sources
Beta strandi48 – 525Combined sources
Helixi54 – 596Combined sources
Beta strandi64 – 663Combined sources
Helixi68 – 703Combined sources
Helixi74 – 774Combined sources
Helixi87 – 9913Combined sources
Beta strandi109 – 1168Combined sources
Beta strandi118 – 1203Combined sources
Beta strandi123 – 1286Combined sources
Helixi133 – 14614Combined sources
Beta strandi151 – 1555Combined sources
Helixi160 – 1634Combined sources
Helixi166 – 1694Combined sources
Beta strandi170 – 1789Combined sources
Helixi188 – 20922Combined sources
Beta strandi217 – 22812Combined sources
Beta strandi236 – 2383Combined sources
Beta strandi240 – 2423Combined sources
Turni244 – 2485Combined sources
Beta strandi258 – 2625Combined sources
Beta strandi268 – 2703Combined sources
Beta strandi273 – 2753Combined sources
Beta strandi277 – 2815Combined sources
Helixi285 – 2873Combined sources
Turni288 – 2914Combined sources
Beta strandi293 – 30412Combined sources
Beta strandi307 – 3093Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GU2X-ray1.80A/B2-312[»]
2Q4ZX-ray1.80A/B2-312[»]
ProteinModelPortaliQ9R1T5.
SMRiQ9R1T5. Positions 4-310.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9R1T5.

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.
InParanoidiQ9R1T5.
KOiK01437.
OMAiNFNEGKE.
OrthoDBiEOG78SQJ6.

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.

Q9R1T5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSCVAEEPI KKIAIFGGTH GNELTGVFLV THWLKNGAEV HRAGLEVKPF
60 70 80 90 100
ITNPRAVEKC TRYIDCDLNR VFDLENLSKE MSEDLPYEVR RAQEINHLFG
110 120 130 140 150
PKNSDDAYDV VFDLHNTTSN MGCTLILEDS RNDFLIQMFH YIKTCMAPLP
160 170 180 190 200
CSVYLIEHPS LKYATTRSIA KYPVGIEVGP QPHGVLRADI LDQMRRMLKH
210 220 230 240 250
ALDFIQRFNE GKEFPPCAID VYKIMEKVDY PRNESGDVAA VIHPNLQDQD
260 270 280 290 300
WKPLHPGDPV FVSLDGKVIP LGGDCTVYPV FVNEAAYYEK KEAFAKTTKL
310
TLNAKSIRST LH
Length:312
Mass (Da):35,314
Last modified:January 9, 2007 - v2
Checksum:iD4344BB001BD5814
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti103 – 1031N → D in BAA82801 (Ref. 1) Curated
Sequence conflicti113 – 1131D → V in BAA82801 (Ref. 1) Curated
Sequence conflicti182 – 1821P → H in BAA82801 (Ref. 1) Curated
Sequence conflicti247 – 2471Q → QLQ in BAA82801 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB023432 mRNA. Translation: BAA82801.1.
BC078813 mRNA. Translation: AAH78813.1.
BC078814 mRNA. Translation: AAH78814.1.
RefSeqiNP_077375.1. NM_024399.1.
XP_006246877.1. XM_006246815.2.
UniGeneiRn.21677.

Genome annotation databases

EnsembliENSRNOT00000084432; ENSRNOP00000072876; ENSRNOG00000019659.
GeneIDi79251.
KEGGirno:79251.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB023432 mRNA. Translation: BAA82801.1.
BC078813 mRNA. Translation: AAH78813.1.
BC078814 mRNA. Translation: AAH78814.1.
RefSeqiNP_077375.1. NM_024399.1.
XP_006246877.1. XM_006246815.2.
UniGeneiRn.21677.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GU2X-ray1.80A/B2-312[»]
2Q4ZX-ray1.80A/B2-312[»]
ProteinModelPortaliQ9R1T5.
SMRiQ9R1T5. Positions 4-310.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60794N.
STRINGi10116.ENSRNOP00000050760.

PTM databases

iPTMnetiQ9R1T5.

Proteomic databases

PaxDbiQ9R1T5.
PRIDEiQ9R1T5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000084432; ENSRNOP00000072876; ENSRNOG00000019659.
GeneIDi79251.
KEGGirno:79251.

Organism-specific databases

CTDi443.
RGDi621693. Aspa.

Phylogenomic databases

eggNOGiENOG410IERR. Eukaryota.
COG2988. LUCA.
GeneTreeiENSGT00390000001189.
HOGENOMiHOG000232489.
HOVERGENiHBG004172.
InParanoidiQ9R1T5.
KOiK01437.
OMAiNFNEGKE.
OrthoDBiEOG78SQJ6.

Enzyme and pathway databases

BRENDAi3.5.1.15. 5301.
ReactomeiR-RNO-70614. Amino acid synthesis and interconversion (transamination).

Miscellaneous databases

EvolutionaryTraceiQ9R1T5.
PROiQ9R1T5.

Gene expression databases

ExpressionAtlasiQ9R1T5. baseline and differential.
GenevisibleiQ9R1T5. RN.

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. "Full length rat cDNA coding for aspartoacylase."
    Kitada K., Serikawa T.
    Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: WTC.
    Tissue: Brain.
  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].
    Tissue: Kidney and Testis.
  3. Lubec G., Afjehi-Sadat L.
    Submitted (NOV-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 43-55; 132-143 AND 172-187, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Spinal cord.
  4. Cited for: SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
  5. "Structure of aspartoacylase, the brain enzyme impaired in Canavan disease."
    Bitto E., Bingman C.A., Wesenberg G.E., McCoy J.G., Phillips G.N. Jr.
    Proc. Natl. Acad. Sci. U.S.A. 104:456-461(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH ZINC IONS, SUBUNIT, COFACTOR.

Entry informationi

Entry nameiACY2_RAT
AccessioniPrimary (citable) accession number: Q9R1T5
Secondary accession number(s): Q6AZ03
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: January 9, 2007
Last modified: July 6, 2016
This is version 96 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.