Reviewed, UniProtKB/Swiss-Prot P30919 (ASPG_RAT)

Names and origin

Protein names

Recommended name:
    N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase
    EC=3.5.1.26
Alternative name(s):
    Glycosylasparaginase
    Aspartylglucosaminidase
      Short name=AGA
    N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase
Cleaved into the following 2 chains:
    1- Recommended name:
            Glycosylasparaginase alpha chain
    2- Recommended name:
            Glycosylasparaginase beta chain

Gene names

Name:

Aga

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	345 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins.
Catalytic activity	N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O = N-acetyl-beta-D-glucosaminylamine + L-aspartate.
Subunit structure	Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers.
Subcellular location	Lysosome.
Sequence similarities	Belongs to the Ntn-hydrolase family.

Ontologies

Keywords
Cellular component	Lysosome
Domain	Signal
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Cellular component	lysosome Inferred from direct assay. Source: RGD
Molecular function	N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity Ref.2 Inferred from direct assay. Source: RGD protein self-association Ref.2 Inferred from direct assay. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Ref.2
	Chain	24 – 204	181	Glycosylasparaginase alpha chain		PRO_0000044571
	Chain	205 – 345	141	Glycosylasparaginase beta chain		PRO_0000044572
Sites
	Active site	205	1	Nucleophile By similarity
Amino acid modifications
	Glycosylation	38	1	N-linked (GlcNAc...) Potential
	Glycosylation	149	1	N-linked (GlcNAc...) Potential
	Glycosylation	307	1	N-linked (GlcNAc...) Potential
	Disulfide bond	64 ↔ 69		By similarity
	Disulfide bond	163 ↔ 179		By similarity
	Disulfide bond	285 ↔ 305		By similarity
	Disulfide bond	316 ↔ 344		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P30919-1 [UniParc]. Last modified December 6, 2005. Version 2. Checksum: BC809F2116B65871	FASTA	345	37,167
	10 20 30 40 50 60 MARKWNLPFL LLPLVLGIPL VRGSNPLPLV VNTWPFKNAT EAAWWTLVSG GSALDAVEKG 70 80 90 100 110 120 CAMCEKEQCG GTVGFGGSPD EVGETTLDAM IMDGTAMDVG AVGGLRRIKN AIGVARKVLE 130 140 150 160 170 180 HTTHTLLVGD SATKFAVSMG FTSEDLSTNT SRALHSDWLS RNCQPNYWRN VIPDPSKYCG 190 200 210 220 230 240 PYKPPDFLEQ NNRAHKEVDI HSHDTIGMVV IHKTGHTAAG TSTNGLKFKI PGRVGDSPIP 250 260 270 280 290 300 GAGAYADDMA GAAAATGDGD TLLRFLPSYQ AVEYMRGGDD PARACQKVIS RIQKYYPKFF 310 320 330 340 GAVICANVTG SYGAACNRLP TFTQFSFMVY NSLHNQAIEE KVDCM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Spleen.
[2]	"Purification and characterization of rat liver glycosylasparaginase." Tollersrud O.-K., Aronson N.N. Jr. Biochem. J. 260:101-108(1989) [PubMed: 2775174] [Abstract] Cited for: PROTEIN SEQUENCE OF 24-41 AND 205-226. Tissue: Liver.
[3]	"Comparison of liver glycosylasparaginases from six vertebrates." Tollersrud O.-K., Aronson N.N. Jr. Biochem. J. 282:891-897(1992) [PubMed: 1554372] [Abstract] Cited for: SEQUENCE REVISION. Tissue: Liver.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BC098718 mRNA. Translation: AAH98718.1.
IPI	IPI00213615.
PIR	S04228. S04229. S57865.
RefSeq	NP_001026811.1.
UniGene	Rn.104649
3D structure databases
HSSP	HSSP built from PDB template 1APY based on UniProtKB P20933.
SMR	P30919. Positions 25-185, 205-345.
ModBase	Search...
Protein family/group databases
MEROPS	T02.001.
Genome annotation databases
Ensembl	ENSRNOG00000000108. Rattus norvegicus. [Contig view]
GeneID	290923.
KEGG	rno:290923.
Organism-specific databases
RGD	1309646. Aga.
Phylogenomic databases
HOVERGEN	P30919.
OMA	P30919. PLVLNTW.
Enzyme and pathway databases
BRENDA	3.5.1.26. 248.
Gene expression databases
ArrayExpress	P30919.
GermOnline	ENSRNOG00000000108. Rattus norvegicus.
Family and domain databases
InterPro	IPR000246. Peptidase_T2. [Graphical view]
PANTHER	PTHR10188. Peptidase_T2. 1 hit.
Pfam	PF01112. Asparaginase_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	631851.

Entry information

Entry name

ASPG_RAT

Accession

Primary (citable) accession number: P30919
Secondary accession number(s): Q4G065

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	December 6, 2005
Last modified:	June 16, 2009
This is version 67 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)