Q8MR45 (ASPG1_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase CG1827
EC=3.5.1.26

Alternative name(s):
Aspartylglucosaminidase
Short name=AGA
Glycosylasparaginase
N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase

Cleaved into the following 2 chains:

1. Glycosylasparaginase alpha chain
2. Glycosylasparaginase beta chain

Gene names

ORF Names:

CG1827

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	393 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins By similarity. UniProtKB P20933
Catalytic activity	N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O = N-acetyl-beta-D-glucosaminylamine + L-aspartate. UniProtKB P20933
Subunit structure	Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers By similarity. UniProtKB P20933
Post-translational modification	Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity By similarity.
Sequence similarities	Belongs to the Ntn-hydrolase family.
Sequence caution	The sequence AAF58918.4 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Domain	Signal
Molecular function	Hydrolase Protease
PTM	Autocatalytic cleavage Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein deglycosylation Inferred from sequence or structural similarity. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	lysosome Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity Inferred from sequence or structural similarity. Source: UniProtKB peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform C Ref.1 (identifier: Q8MR45-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: No experimental confirmation available.

Isoform B Ref.1 (identifier: Q8MR45-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-57: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 242	219	Glycosylasparaginase alpha chain UniProtKB P20933		PRO_0000384129
	Chain	243 – 393	151	Glycosylasparaginase beta chain UniProtKB P20933		PRO_0000384130
Regions
	Region	271 – 274	4	Substrate binding By similarity
	Region	294 – 297	4	Substrate binding By similarity
Sites
	Active site	243	1	Nucleophile By similarity UniProtKB P20933
Amino acid modifications
	Glycosylation	49	1	N-linked (GlcNAc...) Potential
	Glycosylation	64	1	N-linked (GlcNAc...) Potential
	Disulfide bond	97 ↔ 102		By similarity UniProtKB P20933
	Disulfide bond	196 ↔ 212		By similarity UniProtKB P20933
	Disulfide bond	354 ↔ 381		By similarity UniProtKB P20933
Natural variations
	Alternative sequence	1 – 57	57	Missing in isoform B. Ref.1		VSP_053149
Experimental info
	Sequence conflict	370	1	A → G in AAR96196. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform C [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 993979A39BF9129C	FASTA	393	42,240
	10 20 30 40 50 60 MRRHLRASLW ILCLATMAFS ILAAVNTSPK PTLTSAFSGK AGTTAVKANK TTGELLPMVI 70 80 90 100 110 120 NTWNFTAANV LAWRILKQSK GGLRQTRNAV VEGCSKCEKL QCDRTVGYGG SPDELGETTL 130 140 150 160 170 180 DAMVMDGATM DVGAVAGLRR IKDAIKVARH VLEHTQHTML VGDAASAFAN AMGFESESLV 190 200 210 220 230 240 TPESKDMWLQ WTAENCQPNF WKNVHPDPKV SCGPYKPRPT PLTRWKEDRA RNEYEIGRKN 250 260 270 280 290 300 HDTIGMIAID VESNIHAGTS TNGARHKIPG RVGDSPIPGA GAYADNEVGA AVATGDGDVM 310 320 330 340 350 360 MRFLPSLLAV ETMRAGKPPA EAAQEGLRRI LKHHKDFMGA LIAVDRLGNY GAACYGLAEF 370 380 390 PFMVSSPAGA DGPTRLETVK CIGGQDKVNI VAL
	Isoform B [UniParc]. Checksum: C93688857E75FAD9	FASTA	336	36,242
	10 20 30 40 50 60 MVINTWNFTA ANVLAWRILK QSKGGLRQTR NAVVEGCSKC EKLQCDRTVG YGGSPDELGE 70 80 90 100 110 120 TTLDAMVMDG ATMDVGAVAG LRRIKDAIKV ARHVLEHTQH TMLVGDAASA FANAMGFESE 130 140 150 160 170 180 SLVTPESKDM WLQWTAENCQ PNFWKNVHPD PKVSCGPYKP RPTPLTRWKE DRARNEYEIG 190 200 210 220 230 240 RKNHDTIGMI AIDVESNIHA GTSTNGARHK IPGRVGDSPI PGAGAYADNE VGAAVATGDG 250 260 270 280 290 300 DVMMRFLPSL LAVETMRAGK PPAEAAQEGL RRILKHHKDF MGALIAVDRL GNYGAACYGL 310 320 330 AEFPFMVSSP AGADGPTRLE TVKCIGGQDK VNIVAL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[2]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING. Strain: Berkeley.
[3]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C). Strain: Berkeley. Tissue: Head.
[4]	Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B). Strain: Berkeley. Tissue: Testis.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE013599 Genomic DNA. Translation: AAF58918.4. Different initiation. AE013599 Genomic DNA. Translation: AAM71075.1. AY122133 mRNA. Translation: AAM52645.1. BT011404 mRNA. Translation: AAR96196.1.
RefSeq	NP_610504.3. NM_136660.2. NP_724808.1. NM_165684.2.
UniGene	Dm.11231.
3D structure databases
HSSP	HSSP built from PDB template 1APY based on UniProtKB P20933.
ProteinModelPortal	Q8MR45.
SMR	Q8MR45. Positions 56-382.
ModBase	Search...
Protein-protein interaction databases
STRING	7227.FBpp0271751.
Protein family/group databases
MEROPS	T02.001.
Proteomic databases
PaxDb	Q8MR45.
PRIDE	Q8MR45.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	35989.
KEGG	dme:Dmel_CG1827.
UCSC	CG1827-RC. d. melanogaster.
Organism-specific databases
FlyBase	FBgn0033431. CG1827.
Phylogenomic databases
eggNOG	COG1446.
InParanoid	Q8MR45.
KO	K01444.
OrthoDB	EOG44MW7V.
Gene expression databases
Bgee	Q8MR45.
Family and domain databases
InterPro	IPR000246. Peptidase_T2. [Graphical view]
PANTHER	PTHR10188. PTHR10188. 1 hit.
Pfam	PF01112. Asparaginase_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	35989.
NextBio	796207.

Entry information

Entry name

ASPG1_DROME

Accession

Primary (citable) accession number: Q8MR45
Secondary accession number(s): A1Z7W5, A1Z7W6, Q6NN89

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 22, 2009
Last sequence update:	October 1, 2002
Last modified:	May 1, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project