GFPT2_MOUSE
ID GFPT2_MOUSE Reviewed; 682 AA.
AC Q9Z2Z9; Q5NCL2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 2;
DE EC=2.6.1.16 {ECO:0000250|UniProtKB:P82808};
DE AltName: Full=D-fructose-6-phosphate amidotransferase 2;
DE AltName: Full=Glutamine:fructose-6-phosphate amidotransferase 2;
DE Short=GFAT 2;
DE Short=GFAT2;
DE AltName: Full=Hexosephosphate aminotransferase 2;
GN Name=Gfpt2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=C57BL/6J, and Swiss Webster;
RX PubMed=10198162; DOI=10.1006/geno.1999.5785;
RA Oki T., Yamazaki K., Kuromitsu J., Okada M., Tanaka I.;
RT "cDNA cloning and mapping of a novel subtype of glutamine:fructose-6-
RT phosphate amidotransferase (GFAT2) in human and mouse.";
RL Genomics 57:227-234(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Controls the flux of glucose into the hexosamine pathway.
CC Most likely involved in regulating the availability of precursors for
CC N- and O-linked glycosylation of proteins.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-
CC phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16;
CC Evidence={ECO:0000250|UniProtKB:P82808};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-
CC fructose 6-phosphate: step 1/1. {ECO:0000250|UniProtKB:P82808}.
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DR EMBL; AB016778; BAA74727.1; -; Genomic_DNA.
DR EMBL; AB016780; BAA74729.1; -; mRNA.
DR EMBL; AL606479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031928; AAH31928.1; -; mRNA.
DR CCDS; CCDS24622.1; -.
DR RefSeq; NP_038557.1; NM_013529.3.
DR AlphaFoldDB; Q9Z2Z9; -.
DR SMR; Q9Z2Z9; -.
DR BioGRID; 199903; 3.
DR STRING; 10090.ENSMUSP00000020629; -.
DR MEROPS; C44.975; -.
DR iPTMnet; Q9Z2Z9; -.
DR PhosphoSitePlus; Q9Z2Z9; -.
DR jPOST; Q9Z2Z9; -.
DR MaxQB; Q9Z2Z9; -.
DR PaxDb; Q9Z2Z9; -.
DR PeptideAtlas; Q9Z2Z9; -.
DR PRIDE; Q9Z2Z9; -.
DR ProteomicsDB; 267430; -.
DR Antibodypedia; 29588; 198 antibodies from 27 providers.
DR DNASU; 14584; -.
DR Ensembl; ENSMUST00000020629; ENSMUSP00000020629; ENSMUSG00000020363.
DR GeneID; 14584; -.
DR KEGG; mmu:14584; -.
DR UCSC; uc011xud.1; mouse.
DR CTD; 9945; -.
DR MGI; MGI:1338883; Gfpt2.
DR VEuPathDB; HostDB:ENSMUSG00000020363; -.
DR eggNOG; KOG1268; Eukaryota.
DR GeneTree; ENSGT00940000156413; -.
DR HOGENOM; CLU_012520_5_2_1; -.
DR InParanoid; Q9Z2Z9; -.
DR OMA; TSYYSGC; -.
DR OrthoDB; 262871at2759; -.
DR PhylomeDB; Q9Z2Z9; -.
DR TreeFam; TF300864; -.
DR Reactome; R-MMU-446210; Synthesis of UDP-N-acetyl-glucosamine.
DR UniPathway; UPA00113; UER00528.
DR BioGRID-ORCS; 14584; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Gfpt2; mouse.
DR PRO; PR:Q9Z2Z9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9Z2Z9; protein.
DR Bgee; ENSMUSG00000020363; Expressed in tarsal region and 233 other tissues.
DR Genevisible; Q9Z2Z9; MM.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IBA:GO_Central.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006541; P:glutamine metabolic process; TAS:MGI.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IBA:GO_Central.
DR CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR035466; GlmS/AgaS_SIS.
DR InterPro; IPR035490; GlmS/FrlB_SIS.
DR InterPro; IPR005855; GlmS_trans.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR Pfam; PF01380; SIS; 2.
DR SUPFAM; SSF53697; SSF53697; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR01135; glmS; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
DR PROSITE; PS51464; SIS; 2.
PE 1: Evidence at protein level;
KW Aminotransferase; Glutamine amidotransferase; Phosphoprotein;
KW Reference proteome; Repeat; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..682
FT /note="Glutamine--fructose-6-phosphate aminotransferase
FT [isomerizing] 2"
FT /id="PRO_0000135284"
FT DOMAIN 2..288
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT DOMAIN 360..499
FT /note="SIS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT DOMAIN 531..672
FT /note="SIS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT ACT_SITE 2
FT /note="For GATase activity"
FT /evidence="ECO:0000250|UniProtKB:P14742"
FT BINDING 377..378
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06210"
FT BINDING 422..424
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06210"
FT BINDING 427
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06210"
FT BINDING 578
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06210"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 682 AA; 77009 MW; D5F2DA9FA48932B5 CRC64;
MCGIFAYMNY RVPKTRKEIF ETLIRGLQRL EYRGYDSAGV AIDGNNHEVK ERHIHLVKKR
GKVKALDEEL YKQDSMDLKV EFETHFGIAH TRWATHGVPN AVNSHPQRSD KDNEFVVIHN
GIITNYKDLR KFLESKGYEF ESETDTETIA KLIKYVFDNR ETEDITFSTL VERVIQQLEG
AFALVFKSIH YPGEAVATRR GSPLLIGVRS KYKLSTEQIP VLYPTCNIEN VKNICKTRMK
RLDSSTCLHA VGDKAVEFFF ASDASAIIEH TNRVIFLEDD DIAAVADGKL SIHRVKRSAT
DDPSRAIQTL QMELQQIMKG NFSAFMQKEI FEQPESVFNT MRGRVNFETN TVLLGGLKDH
LKEIRRCRRL IVIGCGTSYH AAVATRQVLE ELTELPVMVE LASDFLDRNT PVFRDDVCFF
ISQSGETADT LLALRYCKDR GALTVGITNT VGSSISRETD CGVHINAGPE IGVASTKAYT
SQFISLVMFG LMMSEDRISL QNRRQEIIRG LRSLPELIKE VLSLDEKIHD LALELYTQRS
LLVMGRGYNY ATCLEGALKI KEITYMHSEG ILAGELKHGP LALVDKQMPV IMVIMKDPCF
AKCQNALQQV TARQGRPIIL CSKDDTESSK FAYKTIELPH TVDCLQGILS VIPLQLLSFH
LAVLRGYDVD FPRNLAKSVT VE
