PGM2_MOUSE
ID PGM2_MOUSE Reviewed; 620 AA.
AC Q7TSV4; Q8K0P7; Q9CRS8;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Phosphopentomutase {ECO:0000305};
DE EC=5.4.2.7 {ECO:0000250|UniProtKB:Q96G03};
DE AltName: Full=Glucose phosphomutase 2;
DE AltName: Full=Phosphodeoxyribomutase;
DE AltName: Full=Phosphoglucomutase-1;
DE AltName: Full=Phosphoglucomutase-2 {ECO:0000305};
DE Short=PGM 2;
DE EC=5.4.2.2 {ECO:0000250|UniProtKB:Q96G03};
GN Name=Pgm2 {ECO:0000312|MGI:MGI:97564}; Synonyms=Pgm1;
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].
RC STRAIN=FVB/N; TISSUE=Colon, and Limb;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-620.
RC STRAIN=C57BL/6J; TISSUE=Head;
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=17804405; DOI=10.1074/jbc.m706818200;
RA Maliekal P., Sokolova T., Vertommen D., Veiga-da-Cunha M.,
RA Van Schaftingen E.;
RT "Molecular identification of mammalian phosphopentomutase and glucose-1,6-
RT bisphosphate synthase, two members of the alpha-D-phosphohexomutase
RT family.";
RL J. Biol. Chem. 282:31844-31851(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, 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 conversion of the nucleoside breakdown products
CC ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-
CC phosphopentoses. Catalyzes the interconversion of glucose-1-phosphate
CC into glucose-6-phosphate but with a lower catalytic efficiency. In
CC vitro, has also a low glucose 1,6-bisphosphate synthase activity which
CC is most probably not physiologically relevant.
CC {ECO:0000250|UniProtKB:Q96G03}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-ribose 1-phosphate = D-ribose 5-phosphate;
CC Xref=Rhea:RHEA:18793, ChEBI:CHEBI:57720, ChEBI:CHEBI:78346;
CC EC=5.4.2.7; Evidence={ECO:0000250|UniProtKB:Q96G03};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-deoxy-alpha-D-ribose 1-phosphate = 2-deoxy-D-ribose 5-
CC phosphate; Xref=Rhea:RHEA:27658, ChEBI:CHEBI:57259,
CC ChEBI:CHEBI:62877; EC=5.4.2.7;
CC Evidence={ECO:0000250|UniProtKB:Q96G03};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate;
CC Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601;
CC EC=5.4.2.2; Evidence={ECO:0000250|UniProtKB:Q96G03};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P00949};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P00949};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q96G03}.
CC -!- TISSUE SPECIFICITY: Highly expressed in lung, spleen and thymus.
CC Expressed at lower levels in liver, brain, kidney, skeletal muscle,
CC testis and heart. {ECO:0000269|PubMed:17804405}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
CC -!- CAUTION: There is a known reversal of the Pgm1 and Pgm2 nomenclature
CC applied to mouse versus other vertebrates. The official name of this
CC gene in mouse is Pgm1 but it is the ortholog of other vertebrate PGM2
CC genes. {ECO:0000305}.
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DR EMBL; BC030869; AAH30869.1; -; mRNA.
DR EMBL; BC052762; AAH52762.1; -; mRNA.
DR EMBL; AK014332; BAB29278.1; -; mRNA.
DR CCDS; CCDS19300.1; -.
DR RefSeq; NP_079976.1; NM_025700.2.
DR AlphaFoldDB; Q7TSV4; -.
DR SMR; Q7TSV4; -.
DR BioGRID; 211641; 1.
DR STRING; 10090.ENSMUSP00000084582; -.
DR iPTMnet; Q7TSV4; -.
DR PhosphoSitePlus; Q7TSV4; -.
DR SwissPalm; Q7TSV4; -.
DR EPD; Q7TSV4; -.
DR jPOST; Q7TSV4; -.
DR MaxQB; Q7TSV4; -.
DR PaxDb; Q7TSV4; -.
DR PeptideAtlas; Q7TSV4; -.
DR PRIDE; Q7TSV4; -.
DR ProteomicsDB; 288183; -.
DR Antibodypedia; 23314; 102 antibodies from 25 providers.
DR Ensembl; ENSMUST00000087324; ENSMUSP00000084582; ENSMUSG00000029171.
DR GeneID; 66681; -.
DR KEGG; mmu:66681; -.
DR UCSC; uc008xmi.1; mouse.
DR CTD; 55276; -.
DR MGI; MGI:97564; Pgm2.
DR VEuPathDB; HostDB:ENSMUSG00000029171; -.
DR eggNOG; KOG1220; Eukaryota.
DR GeneTree; ENSGT00940000156247; -.
DR HOGENOM; CLU_016950_0_1_1; -.
DR InParanoid; Q7TSV4; -.
DR OMA; YKAYWEE; -.
DR OrthoDB; 1041556at2759; -.
DR PhylomeDB; Q7TSV4; -.
DR TreeFam; TF300692; -.
DR Reactome; R-MMU-3322077; Glycogen synthesis.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-70221; Glycogen breakdown (glycogenolysis).
DR Reactome; R-MMU-70370; Galactose catabolism.
DR Reactome; R-MMU-71336; Pentose phosphate pathway.
DR BioGRID-ORCS; 66681; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Pgm2; mouse.
DR PRO; PR:Q7TSV4; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q7TSV4; protein.
DR Bgee; ENSMUSG00000029171; Expressed in small intestine Peyer's patch and 248 other tissues.
DR ExpressionAtlas; Q7TSV4; baseline and differential.
DR Genevisible; Q7TSV4; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IDA:MGI.
DR GO; GO:0008973; F:phosphopentomutase activity; ISS:UniProtKB.
DR GO; GO:0006006; P:glucose metabolic process; IDA:MGI.
DR GO; GO:0005980; P:glycogen catabolic process; IMP:MGI.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IBA:GO_Central.
DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR InterPro; IPR005843; A-D-PHexomutase_C.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR Pfam; PF00408; PGM_PMM_IV; 1.
DR SUPFAM; SSF53738; SSF53738; 3.
DR SUPFAM; SSF55957; SSF55957; 1.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cytoplasm; Glucose metabolism; Isomerase;
KW Magnesium; Metal-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..620
FT /note="Phosphopentomutase"
FT /id="PRO_0000147782"
FT ACT_SITE 173
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 71
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 173
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 173
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 330
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 332
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 334
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 334
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 335
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 408
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 432
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 446
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
SQ SEQUENCE 620 AA; 68748 MW; F2535A3F700EFD50 CRC64;
MAAATPTETP APEGSGLGMD ARLDQETAQW LRWDQNPLTS ESVKQLIAGG NKEELRKCFG
ARMEFGTAGL RAPMGAGISR MNDLTIIQTT QGFCRYLEKQ FSDLKQRGVV ISFDARAHPA
SGGSSRRFAR LAATAFITQG VPVYLFSDIT PTPFVPYTVS HLKLCAGIMI TASHNPKQDN
GYKVYWDNGA QIISPHDRGI SQAIEENLEP WPQAWEESLV DSSPLLHNPS ASIGNDYFED
LKKYCFHRTV NKESKVKFVH TSVHGVGHEF VQLAFKAFDL APPEAVPQQK DPDPEFPTVK
YPNPEEGKGV LTLSFALADK IKAKIVLAND PDADRLAVAE KQDSGEWRVF SGNELGALLG
WWLFTSWKEK NQDQSNLKDT YMLSSTVSSK ILRAIALKEG FHFEETLTGF KWMGNRAQQL
GDQGKTVLFA FEEAIGYMCC PFVLDKDGVS AAVICAELAS FLATKNLSLS QQLNAIYVEY
GYHITTASYF ICHDQGTIQN LFGNLRNYDG KNNYPKMCGK FEISAIRDLT TGYDDSQPDK
KAVLPTSKSS QMITFTFANG GVATMRTSGT EPKIKYYAEL CAPPGNSDPE HLKKELDELV
GAIEEHFFQP QKYNLQPKAE
