GFPT1_MOUSE
ID GFPT1_MOUSE Reviewed; 697 AA.
AC P47856; Q91XG9; Q99LP7; Q99MJ4;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1;
DE EC=2.6.1.16 {ECO:0000250|UniProtKB:P82808};
DE AltName: Full=D-fructose-6-phosphate amidotransferase 1;
DE AltName: Full=Glutamine:fructose-6-phosphate amidotransferase 1;
DE Short=GFAT 1;
DE Short=GFAT1;
DE AltName: Full=Hexosephosphate aminotransferase 1;
GN Name=Gfpt1; Synonyms=Gfpt;
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 [MRNA] (ISOFORM 2).
RC STRAIN=SWR/J;
RX PubMed=8144040; DOI=10.1016/0378-1119(94)90560-6;
RA Sayeski P.P., Paterson A.J., Kudlow J.E.;
RT "The murine glutamine:fructose-6-phosphate amidotransferase-encoding cDNA
RT sequence.";
RL Gene 140:289-290(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Skeletal muscle;
RX PubMed=11679416; DOI=10.2337/diabetes.50.11.2419;
RA DeHaven J.E., Robinson K.A., Nelson B.A., Buse M.G.;
RT "A novel variant of glutamine:fructose-6-phosphate amidotransferase-1
RT (GFAT1) mRNA is selectively expressed in striated muscle.";
RL Diabetes 50:2419-2424(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Mammary gland, Salivary gland, and 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).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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).
RN [8]
RP FUNCTION, AND INDUCTION.
RX PubMed=23395176; DOI=10.1016/j.cmet.2012.12.015;
RA Li M.D., Ruan H.B., Hughes M.E., Lee J.S., Singh J.P., Jones S.P.,
RA Nitabach M.N., Yang X.;
RT "O-GlcNAc signaling entrains the circadian clock by inhibiting BMAL1/CLOCK
RT ubiquitination.";
RL Cell Metab. 17:303-310(2013).
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. Regulates the circadian
CC expression of clock genes ARNTL/BMAL1 and CRY1 (PubMed:23395176). Has a
CC role in fine tuning the metabolic fluctuations of cytosolic UDP-GlcNAc
CC and its effects on hyaluronan synthesis that occur during tissue
CC remodeling (By similarity). {ECO:0000250|UniProtKB:Q06210,
CC ECO:0000269|PubMed:23395176}.
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}.
CC -!- SUBUNIT: Homotetramer, may also exist as homodimers. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=GFAT1m;
CC IsoId=P47856-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P47856-2; Sequence=VSP_007498;
CC -!- TISSUE SPECIFICITY: Isoform 1 is predominantly expressed in hindlimb
CC muscle and is also expressed weakly in the heart. Seems to be
CC selectively expressed in striated muscle.
CC {ECO:0000269|PubMed:11679416}.
CC -!- INDUCTION: Expression in the liver oscillates in an ultradian manner
CC (with a 12 hour period/cycle). {ECO:0000269|PubMed:23395176}.
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DR EMBL; U00932; AAC27348.1; -; mRNA.
DR EMBL; AF334736; AAK15341.1; -; mRNA.
DR EMBL; AK019852; BAB31882.1; -; mRNA.
DR EMBL; BC002283; AAH02283.1; -; mRNA.
DR EMBL; BC010516; AAH10516.1; -; mRNA.
DR EMBL; BC050762; AAH50762.1; -; mRNA.
DR CCDS; CCDS39545.1; -. [P47856-2]
DR PIR; I53743; I53743.
DR RefSeq; NP_038556.1; NM_013528.3. [P47856-2]
DR AlphaFoldDB; P47856; -.
DR SMR; P47856; -.
DR BioGRID; 199902; 8.
DR IntAct; P47856; 1.
DR STRING; 10090.ENSMUSP00000109288; -.
DR MEROPS; C44.970; -.
DR iPTMnet; P47856; -.
DR PhosphoSitePlus; P47856; -.
DR SwissPalm; P47856; -.
DR EPD; P47856; -.
DR jPOST; P47856; -.
DR MaxQB; P47856; -.
DR PaxDb; P47856; -.
DR PeptideAtlas; P47856; -.
DR PRIDE; P47856; -.
DR ProteomicsDB; 266795; -. [P47856-1]
DR ProteomicsDB; 266796; -. [P47856-2]
DR Antibodypedia; 47446; 235 antibodies from 33 providers.
DR DNASU; 14583; -.
DR Ensembl; ENSMUST00000032057; ENSMUSP00000032057; ENSMUSG00000029992. [P47856-1]
DR Ensembl; ENSMUST00000113658; ENSMUSP00000109288; ENSMUSG00000029992. [P47856-2]
DR GeneID; 14583; -.
DR KEGG; mmu:14583; -.
DR UCSC; uc009csz.2; mouse. [P47856-2]
DR UCSC; uc009cta.2; mouse. [P47856-1]
DR CTD; 2673; -.
DR MGI; MGI:95698; Gfpt1.
DR VEuPathDB; HostDB:ENSMUSG00000029992; -.
DR eggNOG; KOG1268; Eukaryota.
DR GeneTree; ENSGT00940000158488; -.
DR HOGENOM; CLU_012520_5_2_1; -.
DR InParanoid; P47856; -.
DR OMA; ASEYRYA; -.
DR OrthoDB; 262871at2759; -.
DR PhylomeDB; P47856; -.
DR TreeFam; TF300864; -.
DR Reactome; R-MMU-446210; Synthesis of UDP-N-acetyl-glucosamine.
DR UniPathway; UPA00113; UER00528.
DR BioGRID-ORCS; 14583; 24 hits in 72 CRISPR screens.
DR ChiTaRS; Gfpt1; mouse.
DR PRO; PR:P47856; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P47856; protein.
DR Bgee; ENSMUSG00000029992; Expressed in left colon and 230 other tissues.
DR ExpressionAtlas; P47856; baseline and differential.
DR Genevisible; P47856; MM.
DR GO; GO:0016597; F:amino acid binding; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; ISO:MGI.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; ISO:MGI.
DR GO; GO:0006042; P:glucosamine biosynthetic process; ISO:MGI.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0045719; P:negative regulation of glycogen biosynthetic process; ISO:MGI.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; ISO:MGI.
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 Alternative splicing; Aminotransferase; Biological rhythms;
KW Glutamine amidotransferase; Phosphoprotein; Reference proteome; Repeat;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..697
FT /note="Glutamine--fructose-6-phosphate aminotransferase
FT [isomerizing] 1"
FT /id="PRO_0000135281"
FT DOMAIN 2..303
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT DOMAIN 375..514
FT /note="SIS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT DOMAIN 546..687
FT /note="SIS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT REGION 311..678
FT /note="Isomerase"
FT /evidence="ECO:0000250"
FT ACT_SITE 2
FT /note="For GATase activity"
FT /evidence="ECO:0000250|UniProtKB:P14742"
FT BINDING 392..393
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06210"
FT BINDING 437..439
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06210"
FT BINDING 442
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06210"
FT BINDING 593
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06210"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:21183079"
FT VAR_SEQ 229..244
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:8144040"
FT /id="VSP_007498"
FT CONFLICT 99
FT /note="H -> T (in Ref. 4; AAH10516)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 697 AA; 78539 MW; B7B01F6CD4CEB655 CRC64;
MCGIFAYLNY HVPRTRREIL ETLIKGLQRL EYRGYDSAGV GLDGGNDKDW EANACKIQLI
KKKGKVKALD EEVHKQQDMD LDIEFDVHLG IAHTRWATHG EPNPVNSHPQ RSDKNNEFIV
IHNGIITNYK DLKKFLESKG YDFESETDTE TIAKLVKYMY DNWESQDVSF TTLVERVIQQ
LEGAFALVFK SVHFPGQAVG TRRGSPLLIG VRSEHKLSTD HIPILYRTAR TQIGSTWWGS
QAERGKDKKG SCGLSRVDST TCLFPVEEKA VEYYFASDAS AVIEHTNRVI FLEDDDVAAV
VDGRLSIHRI KRTAGDHPGR AVQTLQMELQ QIMKGNFSSF MQKEIFEQPE SVVNTMRGRV
NFDDYTVNLG GLKDHIKEIQ RCRRLILIAC GTSYHAGVAT RQVLEELTEL PVMVELASDF
LDRNTPVFRD DVCFFISQSG ETADTLMGLR YCKERGALTV GITNTVGSSI SRETDCGVHI
NAGPEIGVAS TKAYTSQFVS LVMFALMMCD DRISMQERRK EIMLGLKRLP DLIKEVLSMD
DEIQKLATEL YHQKSVLIMG RGYHYATCLE GALKIKEITY MHSEGILAGE LKHGPLALVD
KLMPVIMIIM RDHTYAKCQN ALQQVVARQG RPVVICDKED TETIKNTKRT IKVPHSVDCL
QGILSVIPLQ LLAFHLAVLR GYDVDFPRNL AKSVTVE
