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Protein

Aspartoacylase

Gene

Aspa

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Metal bindingi20Zinc1
Metal bindingi23Zinc1
Binding sitei62SubstrateBy similarity1
Metal bindingi115Zinc1
Active sitei177By similarity1
Binding sitei177SubstrateBy similarity1
Binding sitei287SubstrateBy similarity1

GO - Molecular functioni

  • aspartoacylase activity Source: RGD
  • hydrolase activity, acting on ester bonds Source: InterPro
  • identical protein binding Source: IntAct
  • 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

Keywordsi

Molecular functionHydrolase
LigandMetal-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi621693 Aspa

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002168741 – 312AspartoacylaseAdd BLAST312

Proteomic databases

PaxDbiQ9R1T5
PRIDEiQ9R1T5

PTM databases

iPTMnetiQ9R1T5
PhosphoSitePlusiQ9R1T5
SwissPalmiQ9R1T5

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSRNOG00000019659
ExpressionAtlasiQ9R1T5 baseline and differential
GenevisibleiQ9R1T5 RN

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-15617537,EBI-15617537

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

DIPiDIP-60794N
STRINGi10116.ENSRNOP00000050760

Structurei

Secondary structure

1312
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 7Combined sources3
Beta strandi13 – 17Combined sources5
Helixi24 – 35Combined sources12
Helixi38 – 40Combined sources3
Beta strandi48 – 52Combined sources5
Helixi54 – 59Combined sources6
Beta strandi64 – 66Combined sources3
Helixi68 – 70Combined sources3
Helixi74 – 77Combined sources4
Helixi87 – 99Combined sources13
Beta strandi109 – 116Combined sources8
Beta strandi118 – 120Combined sources3
Beta strandi123 – 128Combined sources6
Helixi133 – 146Combined sources14
Beta strandi151 – 155Combined sources5
Helixi160 – 163Combined sources4
Helixi166 – 169Combined sources4
Beta strandi170 – 178Combined sources9
Helixi188 – 209Combined sources22
Beta strandi217 – 228Combined sources12
Beta strandi236 – 238Combined sources3
Beta strandi240 – 242Combined sources3
Turni244 – 248Combined sources5
Beta strandi258 – 262Combined sources5
Beta strandi268 – 270Combined sources3
Beta strandi273 – 275Combined sources3
Beta strandi277 – 281Combined sources5
Helixi285 – 287Combined sources3
Turni288 – 291Combined sources4
Beta strandi293 – 304Combined sources12
Beta strandi307 – 309Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9R1T5

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni69 – 70Substrate bindingBy similarity2
Regioni163 – 167Substrate bindingBy similarity5

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410IERR Eukaryota
COG2988 LUCA
GeneTreeiENSGT00390000001189
HOGENOMiHOG000232489
HOVERGENiHBG004172
InParanoidiQ9R1T5
KOiK01437
OrthoDBiEOG091G0BL6

Family and domain databases

CDDicd06909 M14_ASPA, 1 hit
HAMAPiMF_00704 Aspartoacylase, 1 hit
InterProiView protein in InterPro
IPR016708 Aspartoacylase
IPR007036 Aste_AspA
PfamiView protein in Pfam
PF04952 AstE_AspA, 1 hit
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)DescriptionActionsGraphical viewLength
Sequence conflicti103N → D in BAA82801 (Ref. 1) Curated1
Sequence conflicti113D → V in BAA82801 (Ref. 1) Curated1
Sequence conflicti182P → H in BAA82801 (Ref. 1) Curated1
Sequence conflicti247Q → QLQ in BAA82801 (Ref. 1) Curated1

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_006246815.3
UniGeneiRn.21677

Genome annotation databases

EnsembliENSRNOT00000084432; ENSRNOP00000072876; ENSRNOG00000019659
ENSRNOT00000093230; ENSRNOP00000076091; ENSRNOG00000019659
GeneIDi79251
KEGGirno:79251

Similar proteinsi

Entry informationi

Entry nameiACY2_RAT
AccessioniPrimary (citable) accession number: Q9R1T5
Secondary accession number(s): Q6AZ03
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: January 9, 2007
Last modified: May 23, 2018
This is version 107 of the entry and version 2 of the sequence. See 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

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