PGAM2_MOUSE
ID PGAM2_MOUSE Reviewed; 253 AA.
AC O70250;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Phosphoglycerate mutase 2;
DE EC=5.4.2.11 {ECO:0000250|UniProtKB:P18669};
DE EC=5.4.2.4 {ECO:0000250|UniProtKB:P18669};
DE AltName: Full=BPG-dependent PGAM 2;
DE AltName: Full=Muscle-specific phosphoglycerate mutase;
DE AltName: Full=Phosphoglycerate mutase isozyme M;
DE Short=PGAM-M;
GN Name=Pgam2;
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].
RA Wu G., Yu L., Tu Q., Jiang Y., Fan Y., Zhao S.;
RT "Cloning and expression analysis of a mouse gene coding phosphoglycerate
RT mutase muscle-specific subunit.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11250083; DOI=10.1016/s0378-1119(00)00597-7;
RA Zhang J., Yu L., Fu Q., Gao J., Xie Y., Chen J., Zhang P., Liu Q., Zhao S.;
RT "Mouse phosphoglycerate mutase M and B isozymes: cDNA cloning, enzyme
RT activity assay and mapping.";
RL Gene 264:273-279(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, 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 [5]
RP INTERACTION WITH ENO1, AND TISSUE SPECIFICITY.
RX PubMed=23446454; DOI=10.1095/biolreprod.112.107128;
RA Nakamura N., Dai Q., Williams J., Goulding E.H., Willis W.D., Brown P.R.,
RA Eddy E.M.;
RT "Disruption of a spermatogenic cell-specific mouse enolase 4 (eno4) gene
RT causes sperm structural defects and male infertility.";
RL Biol. Reprod. 88:90-90(2013).
CC -!- FUNCTION: Interconversion of 3- and 2-phosphoglycerate with 2,3-
CC bisphosphoglycerate as the primer of the reaction. Can also catalyze
CC the reaction of EC 5.4.2.4 (synthase), but with a reduced activity.
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:P18669};
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:P18669};
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with ENO1
CC (PubMed:23446454). {ECO:0000250|UniProtKB:P18669,
CC ECO:0000269|PubMed:23446454}.
CC -!- TISSUE SPECIFICITY: Testis. {ECO:0000269|PubMed:23446454}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000305}.
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DR EMBL; AF029843; AAC13263.1; -; mRNA.
DR EMBL; AF317587; AAK06662.1; -; Genomic_DNA.
DR EMBL; BC010750; AAH10750.1; -; mRNA.
DR CCDS; CCDS24404.1; -.
DR RefSeq; NP_061358.1; NM_018870.3.
DR AlphaFoldDB; O70250; -.
DR SMR; O70250; -.
DR BioGRID; 207767; 22.
DR IntAct; O70250; 1.
DR STRING; 10090.ENSMUSP00000020768; -.
DR iPTMnet; O70250; -.
DR PhosphoSitePlus; O70250; -.
DR SwissPalm; O70250; -.
DR SWISS-2DPAGE; O70250; -.
DR CPTAC; non-CPTAC-3727; -.
DR jPOST; O70250; -.
DR PaxDb; O70250; -.
DR PeptideAtlas; O70250; -.
DR PRIDE; O70250; -.
DR ProteomicsDB; 288103; -.
DR Antibodypedia; 26984; 373 antibodies from 27 providers.
DR DNASU; 56012; -.
DR Ensembl; ENSMUST00000020768; ENSMUSP00000020768; ENSMUSG00000020475.
DR GeneID; 56012; -.
DR KEGG; mmu:56012; -.
DR UCSC; uc007hxe.2; mouse.
DR CTD; 5224; -.
DR MGI; MGI:1933118; Pgam2.
DR VEuPathDB; HostDB:ENSMUSG00000020475; -.
DR eggNOG; KOG0235; Eukaryota.
DR GeneTree; ENSGT00950000182926; -.
DR HOGENOM; CLU_033323_1_1_1; -.
DR InParanoid; O70250; -.
DR OMA; MATHRVV; -.
DR OrthoDB; 804949at2759; -.
DR PhylomeDB; O70250; -.
DR TreeFam; TF300007; -.
DR BRENDA; 5.4.2.11; 3474.
DR Reactome; R-MMU-70171; Glycolysis.
DR Reactome; R-MMU-70263; Gluconeogenesis.
DR BioGRID-ORCS; 56012; 7 hits in 74 CRISPR screens.
DR PRO; PR:O70250; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O70250; protein.
DR Bgee; ENSMUSG00000020475; Expressed in triceps brachii and 192 other tissues.
DR ExpressionAtlas; O70250; baseline and differential.
DR Genevisible; O70250; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; ISO:MGI.
DR GO; GO:0004082; F:bisphosphoglycerate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004619; F:phosphoglycerate mutase activity; IDA:MGI.
DR GO; GO:0061621; P:canonical glycolysis; IDA:MGI.
DR GO; GO:0006094; P:gluconeogenesis; ISO:MGI.
DR GO; GO:0006096; P:glycolytic process; IDA:MGI.
DR GO; GO:0007219; P:Notch signaling pathway; IDA:MGI.
DR GO; GO:0010035; P:response to inorganic substance; ISO:MGI.
DR GO; GO:0046689; P:response to mercury ion; ISO:MGI.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0006941; P:striated muscle contraction; ISO: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; 1.
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 Glycolysis; Hydrolase; Isomerase; Phosphoprotein; Reference proteome.
FT CHAIN 1..253
FT /note="Phosphoglycerate mutase 2"
FT /id="PRO_0000179830"
FT ACT_SITE 11
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P18669"
FT ACT_SITE 89
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P18669"
FT BINDING 10..17
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 23..24
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 89..92
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 116..117
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 187..188
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT SITE 186
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT MOD_RES 3
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P16290"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16290"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 121
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P16290"
FT MOD_RES 132
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P16290"
FT MOD_RES 133
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P16290"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16290"
FT MOD_RES 152
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P16290"
SQ SEQUENCE 253 AA; 28827 MW; 477AF9EC59A15B86 CRC64;
MTTHRLVMVR HGESLWNQEN RFCGWFDAEL SEKGAEEAKR GATAIKDAKI EFDICYTSVL
KRAIRTLWTI LDVTDQMWVP VVRTWRLNER HYGGLTGLNK AETAAKHGEE QVKIWRRSFD
TPPPPMDEKH NYYTSISKDR RYAGLKPEEL PTCESLKDTI ARALPFWNEE IAPKIKAGQR
VLIAAHGNSL RGIVKHLEGM SDQAIMELNL PTGIPIVYEL DQNLKPTKPM RFLGDEETVR
KAMEAVAAQG KAK
