PMM1_MOUSE
ID PMM1_MOUSE Reviewed; 262 AA.
AC O35621;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Phosphomannomutase 1;
DE Short=PMM 1;
DE EC=5.4.2.8;
GN Name=Pmm1;
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 Janoueix-Lerosey I., Goud B.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=16847318; DOI=10.1128/mcb.02357-05;
RA Cromphout K., Vleugels W., Heykants L., Schollen E., Keldermans L.,
RA Sciot R., D'Hooge R., De Deyn P.P., von Figura K., Hartmann D., Korner C.,
RA Matthijs G.;
RT "The normal phenotype of Pmm1-deficient mice suggests that Pmm1 is not
RT essential for normal mouse development.";
RL Mol. Cell. Biol. 26:5621-5635(2006).
RN [3]
RP FUNCTION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18927083; DOI=10.1074/jbc.m805224200;
RA Veiga-da-Cunha M., Vleugels W., Maliekal P., Matthijs G.,
RA Van Schaftingen E.;
RT "Mammalian phosphomannomutase PMM1 is the brain IMP-sensitive glucose-1,6-
RT bisphosphatase.";
RL J. Biol. Chem. 283:33988-33993(2008).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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: Involved in the synthesis of the GDP-mannose and dolichol-
CC phosphate-mannose required for a number of critical mannosyl transfer
CC reactions. In addition, may be responsible for the degradation of
CC glucose-1,6-bisphosphate in ischemic brain.
CC {ECO:0000269|PubMed:18927083}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: IMP, a metabolite whose concentration is elevated
CC in anoxia, inhibits phosphomannomutase and phosphoglucomutase
CC activities and strongly enhances glucose-1,6-bisphosphatase activity.
CC {ECO:0000269|PubMed:18927083}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=17 uM for glucose-1,6-bisphosphate in the presence of 1 uM IMP
CC {ECO:0000269|PubMed:18927083};
CC KM=40 uM for glucose-1,6-bisphosphate in the presence of 20 uM IMP
CC {ECO:0000269|PubMed:18927083};
CC Vmax=2.1 umol/min/mg enzyme with glucose-1,6-bisphosphate as
CC substrate {ECO:0000269|PubMed:18927083};
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:0000269|PubMed:16847318}.
CC -!- TISSUE SPECIFICITY: Present in brain, where it is restricted to
CC neuronal cell bodies. Present at lower levels in pancreas, liver, lung,
CC gonads, uterus, adrenal glands and pituitary (at protein level).
CC Undetectable in intestine. {ECO:0000269|PubMed:16847318}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed at 17 dpc in most organs (at
CC protein level). {ECO:0000269|PubMed:16847318}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and fertile and develop normally.
CC {ECO:0000269|PubMed:16847318}.
CC -!- SIMILARITY: Belongs to the eukaryotic PMM family. {ECO:0000305}.
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DR EMBL; AF007267; AAB62943.1; -; mRNA.
DR CCDS; CCDS27678.1; -.
DR RefSeq; NP_038900.1; NM_013872.4.
DR AlphaFoldDB; O35621; -.
DR SMR; O35621; -.
DR IntAct; O35621; 2.
DR MINT; O35621; -.
DR STRING; 10090.ENSMUSP00000023112; -.
DR iPTMnet; O35621; -.
DR PhosphoSitePlus; O35621; -.
DR EPD; O35621; -.
DR PaxDb; O35621; -.
DR PeptideAtlas; O35621; -.
DR PRIDE; O35621; -.
DR ProteomicsDB; 289551; -.
DR Antibodypedia; 26980; 99 antibodies from 20 providers.
DR DNASU; 29858; -.
DR Ensembl; ENSMUST00000023112; ENSMUSP00000023112; ENSMUSG00000022474.
DR GeneID; 29858; -.
DR KEGG; mmu:29858; -.
DR UCSC; uc007wxt.3; mouse.
DR CTD; 5372; -.
DR MGI; MGI:1353418; Pmm1.
DR VEuPathDB; HostDB:ENSMUSG00000022474; -.
DR eggNOG; KOG3189; Eukaryota.
DR GeneTree; ENSGT00390000002918; -.
DR HOGENOM; CLU_065642_0_1_1; -.
DR InParanoid; O35621; -.
DR OMA; VYSPEHT; -.
DR OrthoDB; 1038583at2759; -.
DR PhylomeDB; O35621; -.
DR TreeFam; TF300874; -.
DR Reactome; R-MMU-446205; Synthesis of GDP-mannose.
DR SABIO-RK; O35621; -.
DR UniPathway; UPA00126; UER00424.
DR BioGRID-ORCS; 29858; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Pmm1; mouse.
DR PRO; PR:O35621; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; O35621; protein.
DR Bgee; ENSMUSG00000022474; Expressed in morula and 254 other tissues.
DR ExpressionAtlas; O35621; baseline and differential.
DR Genevisible; O35621; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004615; F:phosphomannomutase activity; ISS:UniProtKB.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006013; P:mannose metabolic process; ISS:UniProtKB.
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 Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT CHAIN 2..262
FT /note="Phosphomannomutase 1"
FT /id="PRO_0000199693"
FT ACT_SITE 19
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT ACT_SITE 21
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 19
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 21
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 28
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 132
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 143
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 150
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 186
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 188
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 190
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 218
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P31353"
FT BINDING 232
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 235
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 262 AA; 29775 MW; 2967154C0FF292B0 CRC64;
MAVAVEGARR KERILCLFDV DGTLTPARQK IDPEVSAFLQ KLRSRVQIGV VGGSDYSKIA
EQLGEGDEVI EKFDYVFAEN GTVQYKHGRL LSKQTIQNHL GEELLQDLIN FCLSYMALLR
LPKKRGTFIE FRNGMLNVSP IGRSCTLEER IEFSELDKKE KIREKFVEAL KTEFAGKGLR
FSRGGMISFD VFPEGWDKRY CLDSLDEDSF DIIHFFGNET SPGGNDFEIY ADPRTVGHSV
VSPQDTVQRC RELFFPETAH EA
