P49088 (ASNS_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Asparagine synthetase [glutamine-hydrolyzing]
EC=6.3.5.4

Alternative name(s):
Glutamine-dependent asparagine synthetase

Gene names

Name:

Asns

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	561 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate.
Pathway	Amino-acid biosynthesis; L-asparagine biosynthesis; L-asparagine from L-aspartate (L-Gln route): step 1/1.
Sequence similarities	Contains 1 asparagine synthetase domain. Contains 1 glutamine amidotransferase type-2 domain.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Asparagine biosynthesis
Domain	Glutamine amidotransferase
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	L-asparagine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway asparagine biosynthetic process Inferred from direct assay PubMed 2887559. Source: RGD cellular response to glucose starvation Inferred from expression pattern PubMed 10085239. Source: RGD cellular response to hormone stimulus Inferred from expression pattern PubMed 1543496. Source: RGD glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW liver development Inferred from expression pattern PubMed 237754. Source: RGD negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara positive regulation of mitotic cell cycle Inferred from electronic annotation. Source: Compara response to amino acid stimulus Inferred from expression pattern PubMed 9176161. Source: RGD response to follicle-stimulating hormone stimulus Inferred from expression pattern PubMed 7915898. Source: RGD response to light stimulus Inferred from expression pattern PubMed 16885923. Source: RGD response to mechanical stimulus Inferred from expression pattern PubMed 16864689. Source: RGD response to methotrexate Inferred from expression pattern PubMed 6122150. Source: RGD response to toxin Inferred from expression pattern PubMed 18164361. Source: RGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW asparagine synthase (glutamine-hydrolyzing) activity Inferred from direct assay PubMed 6132621. Source: RGD cofactor binding Inferred from direct assay PubMed 2859838. Source: RGD protein homodimerization activity Inferred from direct assay PubMed 6132621. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 561	561	Asparagine synthetase [glutamine-hydrolyzing]		PRO_0000056914
Regions
	Domain	2 – 191	190	Glutamine amidotransferase type-2
	Domain	213 – 536	324	Asparagine synthetase
	Nucleotide binding	363 – 364	2	ATP By similarity
	Region	49 – 53	5	Glutamine binding By similarity
	Region	75 – 77	3	Glutamine binding By similarity
Sites
	Active site	2	1	For GATase activity By similarity
	Binding site	97	1	Glutamine By similarity
	Binding site	256	1	ATP; via carbonyl oxygen By similarity
	Binding site	288	1	ATP; via amide nitrogen and carbonyl oxygen By similarity
	Site	365	1	Important for beta-aspartyl-AMP intermediate formation By similarity
Amino acid modifications
	Modified residue	385	1	N6-acetyllysine By similarity
Experimental info
	Sequence conflict	330	1	S → P in AAA77672. Ref.1
	Sequence conflict	330	1	S → P in AAA77671. Ref.1
	Sequence conflict	491	1	H → Y in AAA77672. Ref.1
	Sequence conflict	491	1	H → Y in AAA77671. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P49088 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 6C8C6438F424326F	FASTA	561	64,247
	10 20 30 40 50 60 MCGIWALFGS DDCLSVQCLS AMKIAHRGPD AFRFENVNGY TNCCFGFHRL AVVDPLFGMQ 70 80 90 100 110 120 PIRVRKYPYL WLCYNGEIYN HKALQQRFEF EYQTNVDGEI ILHLYDKGGI EKTICMLDGV 130 140 150 160 170 180 FAFILLDTAN KKVFLGRDTY GVRPLFKALT EDGFLAVCSE AKGLVSLKHS TTPFLKVEPF 190 200 210 220 230 240 LPGHYEVLDL KPNGKVASVE MVKYHHCTDE PLHAIYDSVE KLFPGFEIET VKNNLRILFN 250 260 270 280 290 300 NAIKKRLMTD RRIGCLLSGG LDSSLVAASL LKQLKEAQVP YALQTFAIGM EDSPDLLAAR 310 320 330 340 350 360 KVANYIGSEH HEVLFNSEEG IQSLDEVIFS LETYDITTVR ASVGMYLISK YIRKNTDSVV 370 380 390 400 410 420 IFSGEGSDEL TQGYIYFHKA PSPEKAEEES ERLLKELYLF DVLRADRTTA AHGLELRVPF 430 440 450 460 470 480 LDHRFSSYYL SLPPEMRIPK DGIEKHLLRE TFEDSNLLPK EILWRPKEAF SDGITSVKNS 490 500 510 520 530 540 WFKILQDFVE HQVDDAMMSE ASQKFPFNTP QTKEGYYYRQ IFEHHYPGRA DWLTHYWMPK 550 560 WINATDPSAR TLTHYKSTAK A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of rat asparagine synthetase and specificity of the amino acid-dependent control of its mRNA content." Hutson R.G., Kilberg M.S. Biochem. J. 304:745-750(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U07202 mRNA. Translation: AAA77672.1. U07201 mRNA. Translation: AAA77671.1. BC081719 mRNA. Translation: AAH81719.1.
IPI	IPI00471908.
PIR	S53447.
RefSeq	NP_037211.2. NM_013079.2.
UniGene	Rn.11172.
3D structure databases
ProteinModelPortal	P49088.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000010079.
Protein family/group databases
MEROPS	C44.974.
Proteomic databases
PaxDb	P49088.
PRIDE	P49088.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000010079; ENSRNOP00000010079; ENSRNOG00000007546.
GeneID	25612.
KEGG	rno:25612.
UCSC	RGD:2162. rat.
Organism-specific databases
CTD	440.
RGD	2162. Asns.
Phylogenomic databases
eggNOG	COG0367.
GeneTree	ENSGT00390000001994.
HOGENOM	HOG000027493.
HOVERGEN	HBG003103.
InParanoid	P49088.
KO	K01953.
OMA	KEAYYFR.
OrthoDB	EOG4RV2R2.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-13063.
UniPathway	UPA00134; UER00195.
Gene expression databases
Genevestigator	P49088.
GermOnline	ENSRNOG00000007546. Rattus norvegicus.
Family and domain databases
Gene3D	3.40.50.620. 1 hit.
InterPro	IPR006426. Asn_synth_AEB. IPR001962. Asn_synthase. IPR017932. GATase_2_dom. IPR000583. GATase_dom. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Pfam	PF00733. Asn_synthase. 1 hit. PF13537. GATase_7. 1 hit. [Graphical view]
PIRSF	PIRSF001589. Asn_synthetase_glu-h. 1 hit.
TIGRFAMs	TIGR01536. asn_synth_AEB. 1 hit.
PROSITE	PS51278. GATASE_TYPE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL2303.
NextBio	607355.

Entry information

Entry name

ASNS_RAT

Accession

Primary (citable) accession number: P49088
Secondary accession number(s): Q66HR8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 100 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program