Q8VI04 (ASGL1_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
L-asparaginase
EC=3.5.1.1

Alternative name(s):
Asparaginase-like protein 1
Asparaginase-like sperm autoantigen
Glial asparaginase
L-asparagine amidohydrolase

Gene names

Name:	Asrgl1
Synonyms:	Alp, Gliap, Hiob

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	333 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts in asparagine catabolism. May be involved in astroglial production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions. Ref.2
Catalytic activity	L-asparagine + H2O = L-aspartate + NH3. Ref.2
Subcellular location	Cytoplasm. Note: Midpiece of sperm tail. Ref.1 Ref.2
Tissue specificity	Present in testis, brain, liver, kidney, heart and skeletal muscle. In brain, specifically present in the astrocytic lineage. Present in sperm (at protein level). Ref.1 Ref.2
Miscellaneous	Does not have aspartylglucosaminidase activity. In vasectomized rats, autoantibodies against Asrgl1 are present.
Sequence similarities	Belongs to the Ntn-hydrolase family.
Biophysicochemical properties	Kinetic parameters: KM=2.4 mM for L-aspartic acid beta-(7-amido-4-methylcoumarin) Ref.2

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	asparagine catabolic process via L-aspartate Inferred from direct assay Ref.2. Source: UniProtKB protein maturation Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular component	cytoplasm Inferred from direct assay Ref.2. Source: MGI
Molecular function	N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity Inferred from direct assay Ref.2. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 333	333	L-asparaginase		PRO_0000305207
Sites
	Active site	191	1	Nucleophile By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8VI04 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: FD0BF38DAC6F905D	FASTA	333	34,410
	10 20 30 40 50 60 MATARPSSCG RDSVPATPRA SIDVSLVVVV HGGGASNISP GRKELVSEGI AKAATEGYNI 70 80 90 100 110 120 LKAGGSAVDA VEGAVTMLEN DPEFNAGYGS VLNADGDIEM DASIMDGKDL SAGAVSAVRC 130 140 150 160 170 180 IANPVKLARL VMEKTPHCFL TGRGAEKFAA DMGIPQTPAE KLITERTKKH LEKEKLEKGA 190 200 210 220 230 240 QKADCPKNSG TVGAVALDCK GNLAYATSTG GIVNKMVGRV GDSPCIGAGG YADNNLGAVS 250 260 270 280 290 300 TTGHGESILK VNLARLALFH VEQGKTVDEA ATLALDYMKS KLKGLGGLIL INKTGDWVAK 310 320 330 WTSASMPWAA VKNGKLQAGI DLCETKTRNL PTC

References

[1]	"A novel asparaginase-like protein is a sperm autoantigen in rats." Bush L.A., Herr J.C., Wolkowicz M., Sherman N.E., Shore A., Flickinger C.J. Mol. Reprod. Dev. 62:233-247(2002) [PubMed: 11984834] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. Strain: Lewis. Tissue: Testis.
[2]	"Gliap -- a novel untypical L-asparaginase localized to rat brain astrocytes." Dieterich D.C., Landwehr M., Reissner C., Smalla K.-H., Richter K., Wolf G., Boeckers T.M., Gundelfinger E.D., Kreutz M.R. J. Neurochem. 85:1117-1125(2003) [PubMed: 12753071] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. Strain: Wistar. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF329099 mRNA. Translation: AAL41029.1. AJ427914 mRNA. Translation: CAD20833.1. AJ427915 mRNA. Translation: CAD20834.1.
IPI	IPI00207252.
RefSeq	NP_659557.1. NM_145089.4.
UniGene	Rn.22774.
3D structure databases
HSSP	HSSP built from PDB template 1K2X based on UniProtKB P37595.
ProteinModelPortal	Q8VI04.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8VI04. 1 interaction.
STRING	Q8VI04.
Protein family/group databases
MEROPS	T02.002.
Proteomic databases
PRIDE	Q8VI04.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000027459; ENSRNOP00000027459; ENSRNOG00000020202.
GeneID	246307.
KEGG	rno:246307.
Organism-specific databases
CTD	80150.
RGD	708526. Asrgl1.
Phylogenomic databases
eggNOG	roNOG10540.
GeneTree	ENSGT00530000063034.
HOVERGEN	HBG101662.
InParanoid	Q8VI04.
OMA	ATGHGEF.
OrthoDB	EOG4ZS93Q.
PhylomeDB	Q8VI04.
Gene expression databases
ArrayExpress	Q8VI04.
Genevestigator	Q8VI04.
Family and domain databases
InterPro	IPR000246. Peptidase_T2. [Graphical view]
KO	K13051.
PANTHER	PTHR10188. Peptidase_T2. 1 hit.
Pfam	PF01112. Asparaginase_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	623728.

Entry information

Entry name

ASGL1_RAT

Accession

Primary (citable) accession number: Q8VI04
Secondary accession number(s): Q8CG44

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 2, 2007
Last sequence update:	March 1, 2002
Last modified:	November 16, 2011
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program