GNPI2_MOUSE
ID GNPI2_MOUSE Reviewed; 276 AA.
AC Q9CRC9; Q3TH02; Q9D457;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Glucosamine-6-phosphate isomerase 2;
DE EC=3.5.99.6 {ECO:0000250|UniProtKB:Q8TDQ7};
DE AltName: Full=Glucosamine-6-phosphate deaminase 2;
DE Short=GNPDA 2;
DE Short=GlcN6P deaminase 2;
GN Name=Gnpda2; Synonyms=Kiaa4008;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Kidney, Spinal cord, and 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, 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. Has a role in fine tuning the
CC metabolic fluctuations of cytosolic UDP-GlcNAc and their effects on
CC hyaluronan synthesis that occur during tissue remodeling.
CC {ECO:0000250|UniProtKB:Q8TDQ7}.
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:Q8TDQ7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12173;
CC Evidence={ECO:0000250|UniProtKB:Q8TDQ7};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12174;
CC Evidence={ECO:0000250|UniProtKB:Q8TDQ7};
CC -!- ACTIVITY REGULATION: Allosterically activated by N-acetylglucosamine-6-
CC phosphate (GlcNAc6P). {ECO:0000250|UniProtKB:Q8TDQ7}.
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:Q8TDQ7}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CRC9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CRC9-2; Sequence=VSP_034581;
CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate
CC isomerase family. {ECO:0000305}.
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DR EMBL; AK015527; BAB29883.1; -; mRNA.
DR EMBL; AK016785; BAB30428.1; -; mRNA.
DR EMBL; AK017588; BAB30824.1; -; mRNA.
DR EMBL; AK141408; BAE24675.1; -; mRNA.
DR EMBL; AK166601; BAE38886.1; -; mRNA.
DR EMBL; AK168516; BAE40396.1; -; mRNA.
DR EMBL; AK171299; BAE42378.1; -; mRNA.
DR EMBL; BC004084; AAH04084.1; -; mRNA.
DR CCDS; CCDS19324.1; -. [Q9CRC9-1]
DR CCDS; CCDS84888.1; -. [Q9CRC9-2]
DR RefSeq; NP_001033104.1; NM_001038015.1. [Q9CRC9-1]
DR RefSeq; NP_001334292.1; NM_001347363.1. [Q9CRC9-2]
DR AlphaFoldDB; Q9CRC9; -.
DR SMR; Q9CRC9; -.
DR STRING; 10090.ENSMUSP00000031117; -.
DR iPTMnet; Q9CRC9; -.
DR PhosphoSitePlus; Q9CRC9; -.
DR REPRODUCTION-2DPAGE; Q3TH02; -.
DR REPRODUCTION-2DPAGE; Q9CRC9; -.
DR EPD; Q9CRC9; -.
DR jPOST; Q9CRC9; -.
DR MaxQB; Q9CRC9; -.
DR PaxDb; Q9CRC9; -.
DR PeptideAtlas; Q9CRC9; -.
DR PRIDE; Q9CRC9; -.
DR ProteomicsDB; 263384; -. [Q9CRC9-1]
DR ProteomicsDB; 263385; -. [Q9CRC9-2]
DR Antibodypedia; 23728; 133 antibodies from 28 providers.
DR DNASU; 67980; -.
DR Ensembl; ENSMUST00000031117; ENSMUSP00000031117; ENSMUSG00000029209. [Q9CRC9-1]
DR Ensembl; ENSMUST00000139632; ENSMUSP00000121014; ENSMUSG00000029209. [Q9CRC9-1]
DR Ensembl; ENSMUST00000166298; ENSMUSP00000128233; ENSMUSG00000029209. [Q9CRC9-2]
DR Ensembl; ENSMUST00000173927; ENSMUSP00000133490; ENSMUSG00000029209. [Q9CRC9-2]
DR GeneID; 67980; -.
DR KEGG; mmu:67980; -.
DR UCSC; uc008xqq.1; mouse. [Q9CRC9-1]
DR CTD; 132789; -.
DR MGI; MGI:1915230; Gnpda2.
DR VEuPathDB; HostDB:ENSMUSG00000029209; -.
DR eggNOG; KOG3148; Eukaryota.
DR GeneTree; ENSGT00390000014316; -.
DR HOGENOM; CLU_049611_0_1_1; -.
DR InParanoid; Q9CRC9; -.
DR OMA; GENTHIA; -.
DR OrthoDB; 1425290at2759; -.
DR PhylomeDB; Q9CRC9; -.
DR TreeFam; TF300841; -.
DR Reactome; R-MMU-70171; Glycolysis.
DR UniPathway; UPA00113; UER00528.
DR BioGRID-ORCS; 67980; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Gnpda2; mouse.
DR PRO; PR:Q9CRC9; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9CRC9; protein.
DR Bgee; ENSMUSG00000029209; Expressed in spermatid and 243 other tissues.
DR ExpressionAtlas; Q9CRC9; baseline and differential.
DR Genevisible; Q9CRC9; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006043; P:glucosamine catabolic process; IBA:GO_Central.
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 Alternative splicing; Carbohydrate metabolism; Coiled coil; Cytoplasm;
KW Hydrolase; Isomerase; Phosphoprotein; Reference proteome.
FT CHAIN 1..276
FT /note="Glucosamine-6-phosphate isomerase 2"
FT /id="PRO_0000343206"
FT COILED 103..131
FT /evidence="ECO:0000255"
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:0000250|UniProtKB:O88958"
FT VAR_SEQ 137..138
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034581"
FT CONFLICT 101
FT /note="P -> T (in Ref. 1; BAE40396)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 276 AA; 31084 MW; 01202806EE88FCB2 CRC64;
MRLVILDNYD LASEWAAKYI CNRIIKFKPG QDRYFSLGLP TGSTPLGCYK KLIEYHKSGN
LSFKYVKTFN MDEYVGLPRN HPESYHSYMW NNFFKHIDID PNNAHILDGN AADLQAECDA
FEEKIKEAGG IDLFVGGIGP DGHIAFNEPG SSLVSRTRLK TLAMDTILAN AKYFDGDLSK
VPTMALTVGV GTVMDAREVM ILITGAHKAF ALYKAMEEGV NHMWTVSAFQ QHPRTIFVCD
EDATLELRVK TVKYFKGLMH VHNKLVDPLY SMKEGN
