ASNS_RAT
ID ASNS_RAT Reviewed; 561 AA.
AC P49088; Q66HR8;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Asparagine synthetase [glutamine-hydrolyzing];
DE EC=6.3.5.4;
DE AltName: Full=Glutamine-dependent asparagine synthetase;
GN Name=Asns;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7818476; DOI=10.1042/bj3040745;
RA Hutson R.G., Kilberg M.S.;
RT "Cloning of rat asparagine synthetase and specificity of the amino acid-
RT dependent control of its mRNA content.";
RL Biochem. J. 304:745-750(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-aspartate + L-glutamine = AMP + diphosphate +
CC H(+) + L-asparagine + L-glutamate; Xref=Rhea:RHEA:12228,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58048, ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.4;
CC -!- PATHWAY: Amino-acid biosynthesis; L-asparagine biosynthesis; L-
CC asparagine from L-aspartate (L-Gln route): step 1/1.
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DR EMBL; U07202; AAA77672.1; -; mRNA.
DR EMBL; U07201; AAA77671.1; -; mRNA.
DR EMBL; BC081719; AAH81719.1; -; mRNA.
DR PIR; S53447; S53447.
DR RefSeq; NP_037211.2; NM_013079.2.
DR RefSeq; XP_006236151.1; XM_006236089.3.
DR AlphaFoldDB; P49088; -.
DR SMR; P49088; -.
DR BioGRID; 247641; 1.
DR STRING; 10116.ENSRNOP00000010079; -.
DR ChEMBL; CHEMBL2303; -.
DR MEROPS; C44.974; -.
DR iPTMnet; P49088; -.
DR PhosphoSitePlus; P49088; -.
DR jPOST; P49088; -.
DR PaxDb; P49088; -.
DR PRIDE; P49088; -.
DR Ensembl; ENSRNOT00000010079; ENSRNOP00000010079; ENSRNOG00000007546.
DR GeneID; 25612; -.
DR KEGG; rno:25612; -.
DR UCSC; RGD:2162; rat.
DR CTD; 440; -.
DR RGD; 2162; Asns.
DR eggNOG; KOG0571; Eukaryota.
DR GeneTree; ENSGT00390000001994; -.
DR HOGENOM; CLU_014658_2_1_1; -.
DR InParanoid; P49088; -.
DR OMA; DWSGIYS; -.
DR OrthoDB; 782607at2759; -.
DR PhylomeDB; P49088; -.
DR TreeFam; TF300603; -.
DR BioCyc; MetaCyc:MON-13063; -.
DR Reactome; R-RNO-8963693; Aspartate and asparagine metabolism.
DR UniPathway; UPA00134; UER00195.
DR PRO; PR:P49088; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000007546; Expressed in pancreas and 20 other tissues.
DR Genevisible; P49088; RN.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004066; F:asparagine synthase (glutamine-hydrolyzing) activity; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0006529; P:asparagine biosynthetic process; IDA:RGD.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IEP:RGD.
DR GO; GO:0042149; P:cellular response to glucose starvation; IEP:RGD.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IEP:RGD.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0070981; P:L-asparagine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0001889; P:liver development; IEP:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISO:RGD.
DR GO; GO:0043200; P:response to amino acid; IEP:RGD.
DR GO; GO:0032354; P:response to follicle-stimulating hormone; IEP:RGD.
DR GO; GO:0009416; P:response to light stimulus; IEP:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0009636; P:response to toxic substance; IEP:RGD.
DR CDD; cd01991; Asn_Synthase_B_C; 1.
DR CDD; cd00712; AsnB; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR006426; Asn_synth_AEB.
DR InterPro; IPR001962; Asn_synthase.
DR InterPro; IPR033738; AsnB_N.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00733; Asn_synthase; 2.
DR Pfam; PF13537; GATase_7; 1.
DR PIRSF; PIRSF001589; Asn_synthetase_glu-h; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR01536; asn_synth_AEB; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Amino-acid biosynthesis; Asparagine biosynthesis; ATP-binding;
KW Glutamine amidotransferase; Ligase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..561
FT /note="Asparagine synthetase [glutamine-hydrolyzing]"
FT /id="PRO_0000056914"
FT DOMAIN 2..191
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT DOMAIN 213..536
FT /note="Asparagine synthetase"
FT ACT_SITE 2
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT BINDING 49..53
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250"
FT BINDING 75..77
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 288
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 363..364
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 365
FT /note="Important for beta-aspartyl-AMP intermediate
FT formation"
FT /evidence="ECO:0000250"
FT MOD_RES 385
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08243"
FT MOD_RES 545
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08243"
FT MOD_RES 557
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08243"
FT CONFLICT 330
FT /note="S -> P (in Ref. 1; AAA77672/AAA77671)"
FT /evidence="ECO:0000305"
FT CONFLICT 491
FT /note="H -> Y (in Ref. 1; AAA77672/AAA77671)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 561 AA; 64247 MW; 6C8C6438F424326F CRC64;
MCGIWALFGS DDCLSVQCLS AMKIAHRGPD AFRFENVNGY TNCCFGFHRL AVVDPLFGMQ
PIRVRKYPYL WLCYNGEIYN HKALQQRFEF EYQTNVDGEI ILHLYDKGGI EKTICMLDGV
FAFILLDTAN KKVFLGRDTY GVRPLFKALT EDGFLAVCSE AKGLVSLKHS TTPFLKVEPF
LPGHYEVLDL KPNGKVASVE MVKYHHCTDE PLHAIYDSVE KLFPGFEIET VKNNLRILFN
NAIKKRLMTD RRIGCLLSGG LDSSLVAASL LKQLKEAQVP YALQTFAIGM EDSPDLLAAR
KVANYIGSEH HEVLFNSEEG IQSLDEVIFS LETYDITTVR ASVGMYLISK YIRKNTDSVV
IFSGEGSDEL TQGYIYFHKA PSPEKAEEES ERLLKELYLF DVLRADRTTA AHGLELRVPF
LDHRFSSYYL SLPPEMRIPK DGIEKHLLRE TFEDSNLLPK EILWRPKEAF SDGITSVKNS
WFKILQDFVE HQVDDAMMSE ASQKFPFNTP QTKEGYYYRQ IFEHHYPGRA DWLTHYWMPK
WINATDPSAR TLTHYKSTAK A
