PMM2_MOUSE
ID PMM2_MOUSE Reviewed; 242 AA.
AC Q9Z2M7;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Phosphomannomutase 2;
DE Short=PMM 2;
DE EC=5.4.2.8;
GN Name=Pmm2;
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].
RC STRAIN=C57BL/6J;
RX PubMed=11404002; DOI=10.1016/s0378-1119(01)00481-4;
RA Heykants L., Schollen E., Grunewald S., Matthijs G.;
RT "Identification and localization of two mouse phosphomannomutase genes,
RT Pmm1 and Pmm2.";
RL Gene 270:53-59(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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, 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).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-145, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Involved in the synthesis of the GDP-mannose and dolichol-
CC phosphate-mannose required for a number of critical mannosyl transfer
CC reactions. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate;
CC Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735;
CC EC=5.4.2.8;
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate:
CC step 2/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the eukaryotic PMM family. {ECO:0000305}.
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DR EMBL; AF043514; AAD02276.1; -; mRNA.
DR EMBL; BC046325; AAH46325.1; -; mRNA.
DR CCDS; CCDS27941.1; -.
DR RefSeq; NP_058577.1; NM_016881.2.
DR AlphaFoldDB; Q9Z2M7; -.
DR SMR; Q9Z2M7; -.
DR BioGRID; 207568; 1.
DR STRING; 10090.ENSMUSP00000023396; -.
DR iPTMnet; Q9Z2M7; -.
DR PhosphoSitePlus; Q9Z2M7; -.
DR REPRODUCTION-2DPAGE; Q9Z2M7; -.
DR EPD; Q9Z2M7; -.
DR jPOST; Q9Z2M7; -.
DR MaxQB; Q9Z2M7; -.
DR PaxDb; Q9Z2M7; -.
DR PRIDE; Q9Z2M7; -.
DR ProteomicsDB; 289552; -.
DR Antibodypedia; 24552; 226 antibodies from 30 providers.
DR DNASU; 54128; -.
DR Ensembl; ENSMUST00000023396; ENSMUSP00000023396; ENSMUSG00000022711.
DR Ensembl; ENSMUST00000230828; ENSMUSP00000155554; ENSMUSG00000022711.
DR GeneID; 54128; -.
DR KEGG; mmu:54128; -.
DR UCSC; uc007ycr.1; mouse.
DR CTD; 5373; -.
DR MGI; MGI:1859214; Pmm2.
DR VEuPathDB; HostDB:ENSMUSG00000022711; -.
DR eggNOG; KOG3189; Eukaryota.
DR GeneTree; ENSGT00390000002918; -.
DR HOGENOM; CLU_065642_0_0_1; -.
DR InParanoid; Q9Z2M7; -.
DR OMA; VCPIGRQ; -.
DR OrthoDB; 1038583at2759; -.
DR PhylomeDB; Q9Z2M7; -.
DR TreeFam; TF300874; -.
DR Reactome; R-MMU-446205; Synthesis of GDP-mannose.
DR UniPathway; UPA00126; UER00424.
DR BioGRID-ORCS; 54128; 12 hits in 74 CRISPR screens.
DR ChiTaRS; Pmm2; mouse.
DR PRO; PR:Q9Z2M7; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9Z2M7; protein.
DR Bgee; ENSMUSG00000022711; Expressed in seminal vesicle and 259 other tissues.
DR ExpressionAtlas; Q9Z2M7; baseline and differential.
DR Genevisible; Q9Z2M7; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004615; F:phosphomannomutase activity; IBA:GO_Central.
DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006013; P:mannose metabolic process; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR CDD; cd02585; HAD_PMM; 1.
DR Gene3D; 3.30.1240.20; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006379; HAD-SF_hydro_IIB.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR005002; PMM.
DR InterPro; IPR043169; PMM_cap.
DR PANTHER; PTHR10466; PTHR10466; 1.
DR Pfam; PF03332; PMM; 1.
DR SFLD; SFLDF00445; alpha-phosphomannomutase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01484; HAD-SF-IIB; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Isomerase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..242
FT /note="Phosphomannomutase 2"
FT /id="PRO_0000199696"
FT ACT_SITE 8
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT ACT_SITE 10
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 17
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 119
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 130
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 137
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 175
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 177
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 205
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P31353"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 219
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 222
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT MOD_RES 145
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
SQ SEQUENCE 242 AA; 27657 MW; 065CD3C322AE724C CRC64;
MATLCLFDMD GTLTAPRQKI TEEMDGFLQK LRQKTKIGVV GGSDFEKLQE QLGNDVVEKY
DYVFPENGLV AYKDGKLLCK QNIQGHLGED VIQDLINYCL SYIANIKLPK KRGTFIEFRN
GMLNVSPIGR SCSQEERIEF YELDKKEHIR QKFVADLRKE FAGKGLTFSI GGQISIDVFP
EGWDKRYCLR HLEHAGYKTI YFFGDKTMPG GNDHEIFTDP RTVGYTVTAP EDTRRICEGL
FP
