Reviewed, UniProtKB/Swiss-Prot P49088 (ASNS_RAT)

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)

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	561 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)

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
Gene Ontology (GO)
Biological process	asparagine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW response to amino acid stimulus Inferred from expression pattern. Source: RGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW asparagine synthase (glutamine-hydrolyzing) activity Ref.1 Inferred from direct assay. Source: RGD cofactor binding Inferred from direct assay. Source: RGD protein homodimerization activity Inferred from direct assay. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 561	560	Asparagine synthetase [glutamine-hydrolyzing]		PRO_0000056914
Regions
	Domain	2 – 191	190	Glutamine amidotransferase type-2
	Domain	213 – 536	324	Asparagine synthetase
Sites
	Active site	2	1	For GATase activity 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)
	P49088-1 [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: 7818476] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U07202 mRNA. Translation: AAA77672.1. U07201 mRNA. Translation: AAA77671.1. BC081719 mRNA. Translation: AAH81719.1.
IPI	IPI00471908.
PIR	S53447.
RefSeq	NP_037211.2.
UniGene	Rn.11172
3D structure databases
HSSP	HSSP built from PDB template 1CT9 based on UniProtKB P22106.
ModBase	Search...
Protein-protein interaction databases
STRING	P49088.
Protein family/group databases
MEROPS	C44.974.
Genome annotation databases
Ensembl	ENSRNOT00000010079; ENSRNOP00000010079; ENSRNOG00000007546; Rattus norvegicus. [Genome view] ENSRNOT00000060851; ENSRNOP00000057574; ENSRNOG00000007546; Rattus norvegicus. [Genome view]
GeneID	25612.
KEGG	rno:25612.
NMPDR	fig|10116.3.peg.20825.
UCSC	NM_013079. rat.
Organism-specific databases
CTD	25612.
RGD	2162. Asns.
Phylogenomic databases
HOVERGEN	P49088.
OMA	NKSLAAW.
Enzyme and pathway databases
BioCyc	MetaCyc:MON-13063.
BRENDA	6.3.5.4. 248.
Gene expression databases
ArrayExpress	P49088.
Genevestigator	P49088.
GermOnline	ENSRNOG00000007546. Rattus norvegicus.
Family and domain databases
InterPro	IPR006426. Asn_synth_AEB. IPR001962. Asn_synthase. IPR000583. GATase_2. IPR017932. GATase_II. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
Pfam	PF00733. Asn_synthase. 1 hit. PF00310. GATase_2. 1 hit. [Graphical view]
TIGRFAMs	TIGR01536. asn_synth_AEB. 1 hit.
PROSITE	PS51278. GATASE_TYPE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
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:	November 3, 2009
This is version 72 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)