Reviewed, UniProtKB/Swiss-Prot P11163 (ASPG2_YEAST)

Names and origin

Protein names

Recommended name:
    L-asparaginase 2
    EC=3.5.1.1
Alternative name(s):
    L-asparaginase II
    L-asparagine amidohydrolase II
      Short name=ASP II

Gene names

Name:	ASP3-1
Ordered Locus Names:	YLR155C
ORF Names:	L9632.6
AND
Name:	ASP3-2
Ordered Locus Names:	YLR157C
ORF Names:	L9632.7
AND
Name:	ASP3-3
Ordered Locus Names:	YLR158C
ORF Names:	L9632.8
AND
Name:	ASP3-4
Ordered Locus Names:	YLR160C
ORF Names:	L9632.9

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	362 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)

Catalytic activity	L-asparagine + H2O = L-aspartate + NH3.
Subcellular location	Secreted › cell wall.
Induction	Subject to nitrogen catabolite repression (NCR). Not found in cells grown on rich nitrogen sources like ammonia, glutamine or glutamate, but is found in cells that have been subjected to nitrogen starvation or have been grown on a poor nitrogen source such as proline. Ref.5
Miscellaneous	Yeast contains 2 L-asparaginase isoenzymes: cytoplasmic L-asparaginase I, and cell wall L-asparaginase II. The 4 copies are arranged in tandem repeats.
Sequence similarities	Belongs to the asparaginase 1 family.
Biophysicochemical properties	Kinetic parameters: Does not act on isoasparagine, L-aspartate diamide, beta-alanine amide and L-glutamine. KM=0.27 mM for L-asparagine KM=0.27 mM for D-asparagine KM=0.27 mM for N-acetyl-L-asparagine KM=0.07 mM for N-carbamyl-L-asparagine KM=0.06 mM for N-isoleucyl-L-asparagine KM=0.06 mM for N-glycyl-L-asparagine KM=0.06 mM for N-valyl-L-asparagine KM=0.2 mM for N-methionyl-L-asparagine KM=0.4 mM for N-glycyl-D-asparagine Vmax=42 µmol/min/mg enzyme for L-asparagine Vmax=60 µmol/min/mg enzyme for D-asparagine Vmax=167 µmol/min/mg enzyme for N-acetyl-L-asparagine Vmax=79 µmol/min/mg enzyme for N-carbamyl-L-asparagine Vmax=67 µmol/min/mg enzyme for N-isoleucyl-L-asparagine Vmax=135 µmol/min/mg enzyme for N-glycyl-L-asparagine Vmax=56 µmol/min/mg enzyme for N-valyl-L-asparagine Vmax=92 µmol/min/mg enzyme for N-methionyl-L-asparagine Vmax=8 µmol/min/mg enzyme for N-glycyl-D-asparagine pH dependence: Optimum pH is 6.8. Active from pH 5.5 to pH 7.5. Stable from pH 3.5 to pH 10.5.
Sequence caution	The sequence AAA34438.1 differs from that shown. Reason: Frameshift at position 243.

Ontologies

Keywords
Cellular component	Cell wall Secreted
Domain	Signal
Molecular function	Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	asparagine metabolic process Inferred from electronic annotation. Source: InterPro cellular response to nitrogen starvation Traceable author statement. Source: SGD
Cellular component	cell wall Inferred from electronic annotation. Source: UniProtKB-SubCell cell wall-bounded periplasmic space Traceable author statement. Source: SGD endoplasmic reticulum Inferred from direct assay. Source: SGD extracellular region Inferred from electronic annotation. Source: UniProtKB-KW nuclear envelope Inferred from direct assay. Source: SGD
Molecular function	asparaginase activity Ref.1 Traceable author statement. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 25	25	Ref.1
	Chain	26 – 362	337	L-asparaginase 2		PRO_0000002362
Sites
	Active site	43	1	By similarity
	Active site	122	1	By similarity
	Active site	123	1	By similarity
	Active site	195	1	By similarity
Amino acid modifications
	Glycosylation	29	1	N-linked (GlcNAc...) Potential
	Glycosylation	93	1	N-linked (GlcNAc...) Potential
	Glycosylation	239	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	26 – 55	30	Missing
Experimental info
	Sequence conflict	31	1	S → P in AAS56283. Ref.3
	Sequence conflict	243	1	P → L in AAS56284. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P11163-1 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 1DE5DC8692BF0461	FASTA	362	38,687
	10 20 30 40 50 60 MRSLNTLLLS LFVAMSSGAP LLKIREEKNS SLPSIKIFGT GGTIASKGST SATTAGYSVG 70 80 90 100 110 120 LTVNDLIEAV PSLAEKANLD YLQVSNVGSN SLNYTHLIPL YHGISEALAS DDYAGAVVTH 130 140 150 160 170 180 GTDTMEETAF FLDLTINSEK PVCIAGAMRP ATATSADGPM NLYQAVSIAA SEKSLGRGTM 190 200 210 220 230 240 ITLNDRIASG FWTTKMNANS LDTFRADEQG YLGYFSNDDV EFYYPPVKPN GWQFFDISNL 250 260 270 280 290 300 TDPSEIPEVI ILYSYQGLNP ELIVKAVKDL GAKGIVLAGS GAGSWTATGS IVNEQLYEEY 310 320 330 340 350 360 GIPIVHSRRT ADGTVPPDDA PEYAIGSGYL NPQKSRILLQ LCLYSGYGMD QIRSVFSGVY GG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Asparaginase II of Saccharomyces cerevisiae. Characterization of the ASP3 gene." Kim K.-W., Kamerud J.Q., Livingston D.M., Roon R.J. J. Biol. Chem. 263:11948-11953(1988) [PubMed: 3042786] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 26-41 AND 56-71, VARIANT 26-GLU--ALA-55 DEL.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D. Nature 387:87-90(1997) [PubMed: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ASP3-1; ASP3-2; ASP3-3 AND ASP3-4). Strain: ATCC 204511 / S288c / AB972.
[3]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ASP3-1 AND ASP3-2). Strain: ATCC 204508 / S288c.
[4]	"Characterization of two forms of asparaginase in Saccharomyces cerevisiae." Dunlop P.C., Meyer G.M., Ban D., Roon R.J. J. Biol. Chem. 253:1297-1304(1978) [PubMed: 342521] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
[5]	"Nitrogen catabolite repression of asparaginase II in Saccharomyces cerevisiae." Dunlop P.C., Meyer G.M., Roon R.J. J. Bacteriol. 143:422-426(1980) [PubMed: 6995441] [Abstract] Cited for: INDUCTION.
[6]	"Reactions of asparaginase II of Saccharomyces cerevisiae. A mechanistic analysis of hydrolysis and hydroxylaminolysis." Dunlop P.C., Meyer G.M., Roon R.J. J. Biol. Chem. 255:1542-1546(1980) [PubMed: 6986375] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	J03926 Genomic DNA. Translation: AAA34438.1. Frameshift. U51921 Genomic DNA. Translation: AAB67479.1. U51921 Genomic DNA. Translation: AAB67481.1. U51921 Genomic DNA. Translation: AAB67482.1. U51921 Genomic DNA. Translation: AAB67484.1. AY557957 Genomic DNA. Translation: AAS56283.1. AY557958 Genomic DNA. Translation: AAS56284.1.
PIR	S68471.
RefSeq	NP_013256.1. NP_013258.1. NP_013259.1. NP_013261.1.
3D structure databases
HSSP	HSSP built from PDB template 1HFW based on UniProtKB P06608.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:3807N.
IntAct	P11163. 18 interactions.
STRING	P11163.
Genome annotation databases
Ensembl	YLR155C; YLR155C; YLR155C; Saccharomyces cerevisiae. [Genome view] YLR157C; YLR157C; YLR157C; Saccharomyces cerevisiae. [Genome view] YLR158C; YLR158C; YLR158C; Saccharomyces cerevisiae. [Genome view] YLR160C; YLR160C; YLR160C; Saccharomyces cerevisiae. [Genome view]
GeneID	850850. 850852. 850855. 850857.
KEGG	sce:YLR155C. sce:YLR157C. sce:YLR158C. sce:YLR160C.
Organism-specific databases
CYGD	YLR155c. YLR157c. YLR158c. YLR160c.
SGD	S000004145. ASP3-1. S000004147. ASP3-2. S000004148. ASP3-3. S000004150. ASP3-4.
Phylogenomic databases
HOGENOM	P11163.
OMA	TIAGCAN.
Enzyme and pathway databases
BRENDA	3.5.1.1. 250.
Gene expression databases
Genevestigator	P11163.
GermOnline	YLR155C. Saccharomyces cerevisiae. YLR157C. Saccharomyces cerevisiae. YLR158C. Saccharomyces cerevisiae. YLR160C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR004550. AsnASE_II. IPR006034. Asp/Glutamnse. [Graphical view]
PANTHER	PTHR11707. Asp/Glutamnse. 1 hit.
Pfam	PF00710. Asparaginase. 1 hit. [Graphical view]
PRINTS	PR00139. ASNGLNASE.
ProDom	PD003221. Asp/Glutamnse. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00520. asnASE_II. 1 hit.
PROSITE	PS00144. ASN_GLN_ASE_1. 1 hit. PS00917. ASN_GLN_ASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	967149.

Entry information

Entry name

ASPG2_YEAST

Accession

Primary (citable) accession number: P11163
Secondary accession number(s): Q12268, Q6Q5K8, Q6Q5K9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	November 1, 1997
Last modified:	November 3, 2009
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)