PMGE_MOUSE
ID PMGE_MOUSE Reviewed; 259 AA.
AC P15327; Q543Z6;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Bisphosphoglycerate mutase;
DE Short=BPGM;
DE EC=5.4.2.4 {ECO:0000250|UniProtKB:P07738};
DE AltName: Full=2,3-bisphosphoglycerate mutase, erythrocyte;
DE AltName: Full=2,3-bisphosphoglycerate synthase;
DE EC=5.4.2.11 {ECO:0000250|UniProtKB:P07738};
DE AltName: Full=BPG-dependent PGAM;
GN Name=Bpgm;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Spleen;
RX PubMed=2847721; DOI=10.1016/s0006-291x(88)80925-2;
RA le Boulch P., Joulin V., Garel M.-C., Rosa J., Cohen-Solal M.;
RT "Molecular cloning and nucleotide sequence of murine 2,3-
RT bisphosphoglycerate mutase cDNA.";
RL Biochem. Biophys. Res. Commun. 156:874-881(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Medulla oblongata;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 TISSUE SPECIFICITY.
RX PubMed=19733906; DOI=10.1016/j.placenta.2009.08.005;
RA Gu M., Pritlove D.C., Boyd C.A., Vatish M.;
RT "Placental expression of 2,3 bisphosphoglycerate mutase in IGF-II knock out
RT mouse: correlation of circulating maternal 2,3 bisphosphoglycerate and
RT fetal growth.";
RL Placenta 30:919-922(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC 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: Plays a major role in regulating hemoglobin oxygen affinity
CC by controlling the levels of its allosteric effector 2,3-
CC bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 5.4.2.11)
CC activity. {ECO:0000250|UniProtKB:P07738}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phospho-glyceroyl phosphate = (2R)-2,3-
CC bisphosphoglycerate + H(+); Xref=Rhea:RHEA:17765, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58248; EC=5.4.2.4;
CC Evidence={ECO:0000250|UniProtKB:P07738};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC EC=5.4.2.11; Evidence={ECO:0000250|UniProtKB:P07738};
CC -!- ACTIVITY REGULATION: At alkaline pH BPGM favors the synthase reaction;
CC however, at lower pH the phosphatase reaction is dominant. Inhibited by
CC citrate. {ECO:0000250|UniProtKB:P07738}.
CC -!- SUBUNIT: Homodimer.
CC -!- TISSUE SPECIFICITY: Expressed in red blood cells. Expressed in placenta
CC (labyrinthine trophoblasts). {ECO:0000269|PubMed:19733906,
CC ECO:0000269|PubMed:2847721}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000305}.
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DR EMBL; X13586; CAA31927.1; -; mRNA.
DR EMBL; AK043412; BAC31541.1; -; mRNA.
DR EMBL; AK078119; BAC37133.1; -; mRNA.
DR EMBL; BC004589; AAH04589.1; -; mRNA.
DR CCDS; CCDS19994.1; -.
DR PIR; A31585; PMMSBM.
DR RefSeq; NP_031589.1; NM_007563.4.
DR AlphaFoldDB; P15327; -.
DR SMR; P15327; -.
DR BioGRID; 198382; 1.
DR STRING; 10090.ENSMUSP00000047393; -.
DR iPTMnet; P15327; -.
DR PhosphoSitePlus; P15327; -.
DR SwissPalm; P15327; -.
DR REPRODUCTION-2DPAGE; P15327; -.
DR CPTAC; non-CPTAC-3373; -.
DR EPD; P15327; -.
DR jPOST; P15327; -.
DR MaxQB; P15327; -.
DR PaxDb; P15327; -.
DR PeptideAtlas; P15327; -.
DR PRIDE; P15327; -.
DR ProteomicsDB; 291764; -.
DR Antibodypedia; 2975; 265 antibodies from 28 providers.
DR DNASU; 12183; -.
DR Ensembl; ENSMUST00000045372; ENSMUSP00000047393; ENSMUSG00000038871.
DR GeneID; 12183; -.
DR KEGG; mmu:12183; -.
DR UCSC; uc009bhf.1; mouse.
DR CTD; 669; -.
DR MGI; MGI:1098242; Bpgm.
DR VEuPathDB; HostDB:ENSMUSG00000038871; -.
DR eggNOG; KOG0235; Eukaryota.
DR GeneTree; ENSGT00950000182926; -.
DR HOGENOM; CLU_033323_1_1_1; -.
DR InParanoid; P15327; -.
DR OMA; ITESHPY; -.
DR OrthoDB; 1112626at2759; -.
DR PhylomeDB; P15327; -.
DR TreeFam; TF300007; -.
DR Reactome; R-MMU-70171; Glycolysis.
DR BioGRID-ORCS; 12183; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Bpgm; mouse.
DR PRO; PR:P15327; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P15327; protein.
DR Bgee; ENSMUSG00000038871; Expressed in blood and 262 other tissues.
DR ExpressionAtlas; P15327; baseline and differential.
DR Genevisible; P15327; MM.
DR GO; GO:0004082; F:bisphosphoglycerate mutase activity; IMP:MGI.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0004619; F:phosphoglycerate mutase activity; IEA:InterPro.
DR GO; GO:0042832; P:defense response to protozoan; IMP:MGI.
DR GO; GO:0048821; P:erythrocyte development; IMP:MGI.
DR GO; GO:0060856; P:establishment of blood-brain barrier; IMP:MGI.
DR GO; GO:0006096; P:glycolytic process; IMP:MGI.
DR GO; GO:0150076; P:neuroinflammatory response; IMP:MGI.
DR GO; GO:0006753; P:nucleoside phosphate metabolic process; IMP:MGI.
DR GO; GO:0015671; P:oxygen transport; IMP:MGI.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR HAMAP; MF_01039; PGAM_GpmA; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR InterPro; IPR005952; Phosphogly_mut1.
DR PANTHER; PTHR11931; PTHR11931; 1.
DR Pfam; PF00300; His_Phos_1; 2.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR TIGRFAMs; TIGR01258; pgm_1; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Glycolysis; Hydrolase; Isomerase; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT CHAIN 2..259
FT /note="Bisphosphoglycerate mutase"
FT /id="PRO_0000179835"
FT ACT_SITE 11
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT ACT_SITE 89
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT BINDING 10..17
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT BINDING 23..24
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT BINDING 89..92
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT BINDING 116..117
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT BINDING 189..190
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT SITE 188
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT MOD_RES 122
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07738"
SQ SEQUENCE 259 AA; 29978 MW; 6C2674005B41A0C5 CRC64;
MSKHKLIILR HGEGQWNKEN RFCSWVDQKL NNDGLEEARN CGRQLKALNF EFDLVFTSIL
NRSIHTAWLI LEELGQEWVP VESSWRLNER HYGALIGLNR EKMALNHGEE QVRLWRRSYN
VTPPPIEESH PYFHEIYSDR RYKVCDVPLD QLPRSESLKD VLERLLPYWK ERIAPEILKG
KSILISAHGN SSRALLKHLE GISDEDIINI TLPTGVPILL ELDENLRAVG PHQFLGNQEA
IQAAIKKVDD QGKVKQGKQ
