GNPI1_MOUSE
ID GNPI1_MOUSE Reviewed; 289 AA.
AC O88958; Q91WJ4; Q9R188;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Glucosamine-6-phosphate isomerase 1;
DE EC=3.5.99.6 {ECO:0000250|UniProtKB:P46926};
DE AltName: Full=Glucosamine-6-phosphate deaminase 1;
DE Short=GNPDA 1;
DE Short=GlcN6P deaminase 1;
DE AltName: Full=Oscillin;
GN Name=Gnpda1; Synonyms=Gnpi;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=10481053; DOI=10.1016/s0014-5793(99)01141-2;
RA Montag M., van der Ven K., Doerbecker C., van der Ven H.;
RT "Characterization of testicular mouse glucosamine 6-phosphate deaminase
RT (GNPDA).";
RL FEBS Lett. 458:141-144(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=10862010;
RX DOI=10.1002/1098-2795(200007)56:3<424::aid-mrd13>3.0.co;2-t;
RA Amireault P., Dube F.;
RT "Cloning, sequencing, and expression analysis of mouse glucosamine-6-
RT phosphate deaminase (GNPDA/oscillin).";
RL Mol. Reprod. Dev. 56:424-435(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161, 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).
CC -!- FUNCTION: Catalyzes the reversible conversion of alpha-D-glucosamine 6-
CC phosphate (GlcN-6P) into beta-D-fructose 6-phosphate (Fru-6P) and
CC ammonium ion, a regulatory reaction step in de novo uridine
CC diphosphate-N-acetyl-alpha-D-glucosamine (UDP-GlcNAc) biosynthesis via
CC hexosamine pathway. Deamination is coupled to aldo-keto isomerization
CC mediating the metabolic flux from UDP-GlcNAc toward Fru-6P. At high
CC ammonium level can drive amination and isomerization of Fru-6P toward
CC hexosamines and UDP-GlcNAc synthesis (By similarity). Has a role in
CC fine tuning the metabolic fluctuations of cytosolic UDP-GlcNAc and
CC their effects on hyaluronan synthesis that occur during tissue
CC remodeling (By similarity). Seems to trigger calcium oscillations in
CC mammalian eggs. These oscillations serve as the essential trigger for
CC egg activation and early development of the embryo (By similarity).
CC {ECO:0000250|UniProtKB:P46926, ECO:0000250|UniProtKB:Q64422}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-
CC phosphate + NH4(+); Xref=Rhea:RHEA:12172, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:57634, ChEBI:CHEBI:75989; EC=3.5.99.6;
CC Evidence={ECO:0000250|UniProtKB:P46926};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12173;
CC Evidence={ECO:0000250|UniProtKB:P46926};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12174;
CC Evidence={ECO:0000250|UniProtKB:P46926};
CC -!- ACTIVITY REGULATION: Allosterically activated by N-acetylglucosamine-6-
CC phosphate (GlcNAc6P). {ECO:0000250|UniProtKB:P46926}.
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:P46926}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:P46926}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10481053}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Detected in brain, liver, kidney,
CC muscle, ovary, testis, spermatids and spermatozoa. In spermatids,
CC located close to the developing acrosome vesicle. In spermatozoa, found
CC close to the acrosomal region. {ECO:0000269|PubMed:10481053}.
CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate
CC isomerase family. {ECO:0000305}.
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DR EMBL; AF088903; AAC36739.1; -; mRNA.
DR EMBL; AF160355; AAD42233.1; -; mRNA.
DR EMBL; AC134576; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC152450; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466528; EDL10078.1; -; Genomic_DNA.
DR EMBL; BC014800; AAH14800.1; -; mRNA.
DR CCDS; CCDS29201.1; -.
DR RefSeq; NP_036067.2; NM_011937.2.
DR AlphaFoldDB; O88958; -.
DR SMR; O88958; -.
DR BioGRID; 204942; 12.
DR STRING; 10090.ENSMUSP00000069081; -.
DR iPTMnet; O88958; -.
DR PhosphoSitePlus; O88958; -.
DR EPD; O88958; -.
DR jPOST; O88958; -.
DR PaxDb; O88958; -.
DR PeptideAtlas; O88958; -.
DR PRIDE; O88958; -.
DR ProteomicsDB; 271008; -.
DR Antibodypedia; 606; 255 antibodies from 32 providers.
DR DNASU; 26384; -.
DR Ensembl; ENSMUST00000063814; ENSMUSP00000069081; ENSMUSG00000052102.
DR GeneID; 26384; -.
DR KEGG; mmu:26384; -.
DR UCSC; uc008esi.2; mouse.
DR CTD; 10007; -.
DR MGI; MGI:1347054; Gnpda1.
DR VEuPathDB; HostDB:ENSMUSG00000052102; -.
DR eggNOG; KOG3148; Eukaryota.
DR GeneTree; ENSGT00390000014316; -.
DR HOGENOM; CLU_049611_0_1_1; -.
DR InParanoid; O88958; -.
DR OMA; INHMWTL; -.
DR OrthoDB; 1425290at2759; -.
DR PhylomeDB; O88958; -.
DR TreeFam; TF300841; -.
DR Reactome; R-MMU-70171; Glycolysis.
DR UniPathway; UPA00113; UER00528.
DR BioGRID-ORCS; 26384; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Gnpda1; mouse.
DR PRO; PR:O88958; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; O88958; protein.
DR Bgee; ENSMUSG00000052102; Expressed in yolk sac and 63 other tissues.
DR ExpressionAtlas; O88958; baseline and differential.
DR Genevisible; O88958; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0004342; F:glucosamine-6-phosphate deaminase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0007340; P:acrosome reaction; TAS:MGI.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; ISO:MGI.
DR GO; GO:0046370; P:fructose biosynthetic process; ISO:MGI.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; ISS:UniProtKB.
DR GO; GO:0006043; P:glucosamine catabolic process; ISS:UniProtKB.
DR GO; GO:0006041; P:glucosamine metabolic process; ISO:MGI.
DR GO; GO:0006046; P:N-acetylglucosamine catabolic process; IBA:GO_Central.
DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; IBA:GO_Central.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; ISS:UniProtKB.
DR CDD; cd01399; GlcN6P_deaminase; 1.
DR HAMAP; MF_01241; GlcN6P_deamin; 1.
DR InterPro; IPR006148; Glc/Gal-6P_isomerase.
DR InterPro; IPR004547; Glucosamine6P_isomerase.
DR InterPro; IPR018321; Glucosamine6P_isomerase_CS.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR PANTHER; PTHR11280; PTHR11280; 1.
DR Pfam; PF01182; Glucosamine_iso; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
DR TIGRFAMs; TIGR00502; nagB; 1.
DR PROSITE; PS01161; GLC_GALNAC_ISOMERASE; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cytoplasm; Hydrolase; Isomerase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..289
FT /note="Glucosamine-6-phosphate isomerase 1"
FT /id="PRO_0000160124"
FT ACT_SITE 72
FT /note="Proton acceptor; for enolization step"
FT /evidence="ECO:0000250"
FT ACT_SITE 141
FT /note="For ring-opening step"
FT /evidence="ECO:0000250"
FT ACT_SITE 143
FT /note="Proton acceptor; for ring-opening step"
FT /evidence="ECO:0000250"
FT ACT_SITE 148
FT /note="For ring-opening step"
FT /evidence="ECO:0000250"
FT MOD_RES 161
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 87
FT /note="S -> F (in Ref. 1; AAC36739)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="N -> D (in Ref. 1; AAC36739)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="A -> G (in Ref. 1; AAC36739)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 289 AA; 32549 MW; 4778C0E0D74EBBB8 CRC64;
MKLIILEHYS QASEWAAKYI RNRIIQFNPG PDKYFTLGLP TGSTPLGCYQ KLIEYYKNGD
LSFQYVKTFN MDEYVGLPRD HPESYHSFMW NNFFKHIDIH PENTHILDGN AADLQAECDA
FEEKIQAAGG IELFVGGIGP DGHIAFNEPG SSLVSRTRVK TLAMDTILAN ARFFDGDLAK
VPTMALTVGV GTVMDAKEVM ILITGAHKAF ALYKAIEEGV NHMWTVSAFQ QHPRTVFVCD
EDATLELKVK TVKYFKGLML VHNKLVDPLY SIKEKEIQKS QSAKKPYSD
