O35621 (PMM1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphomannomutase 1
Short name=PMM 1
EC=5.4.2.8

Gene names

Name:

Pmm1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	262 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions. In addition, may be responsible for the degradation of glucose-1,6-bisphosphate in ischemic brain. Ref.3
Catalytic activity	Alpha-D-mannose 1-phosphate = D-mannose 6-phosphate.
Cofactor	Magnesium By similarity.
Enzyme regulation	IMP, a metabolite whose concentration is elevated in anoxia, inhibits phosphomannomutase and phosphoglucomutase activities and strongly enhances glucose-1,6-bisphosphatase activity. Ref.3
Pathway	Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm Ref.2.
Tissue specificity	Present in brain, where it is restricted to neuronal cell bodies. Present at lower levels in pancreas, liver, lung, gonads, uterus, adrenal glands and pituitary (at protein level). Undetectable in intestine. Ref.2
Developmental stage	Highly expressed at E17 in most organs (at protein level). Ref.2
Disruption phenotype	Mice are viable and fertile and develop normally. Ref.2
Sequence similarities	Belongs to the eukaryotic PMM family.
Biophysicochemical properties	Kinetic parameters: KM=17 µM for glucose-1,6-bisphosphate in the presence of 1 µM IMP Ref.3 KM=40 µM for glucose-1,6-bisphosphate in the presence of 20 µM IMP Vmax=2.1 µmol/min/mg enzyme with glucose-1,6-bisphosphate as substrate

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Isomerase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	GDP-mannose biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway mannose biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from direct assay PubMed 16115222. Source: MGI neuronal cell body Inferred from direct assay PubMed 16115222. Source: MGI
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphomannomutase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 262	262	Phosphomannomutase 1		PRO_0000199693
Sites
	Active site	19	1	Nucleophile By similarity
	Active site	21	1	By similarity
	Active site	54	1	By similarity
	Active site	198	1	By similarity
	Metal binding	218	1	Magnesium By similarity
	Binding site	28	1	Substrate By similarity
	Binding site	132	1	Substrate By similarity
	Binding site	143	1	Substrate By similarity
	Binding site	150	1	Substrate By similarity
	Binding site	186	1	Substrate By similarity
	Binding site	188	1	Substrate By similarity
	Binding site	190	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	O35621 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 2967154C0FF292B0	FASTA	262	29,775
	10 20 30 40 50 60 MAVAVEGARR KERILCLFDV DGTLTPARQK IDPEVSAFLQ KLRSRVQIGV VGGSDYSKIA 70 80 90 100 110 120 EQLGEGDEVI EKFDYVFAEN GTVQYKHGRL LSKQTIQNHL GEELLQDLIN FCLSYMALLR 130 140 150 160 170 180 LPKKRGTFIE FRNGMLNVSP IGRSCTLEER IEFSELDKKE KIREKFVEAL KTEFAGKGLR 190 200 210 220 230 240 FSRGGMISFD VFPEGWDKRY CLDSLDEDSF DIIHFFGNET SPGGNDFEIY ADPRTVGHSV 250 260 VSPQDTVQRC RELFFPETAH EA

References

[1]	Janoueix-Lerosey I., Goud B. Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The normal phenotype of Pmm1-deficient mice suggests that Pmm1 is not essential for normal mouse development." Cromphout K., Vleugels W., Heykants L., Schollen E., Keldermans L., Sciot R., D'Hooge R., De Deyn P.P., von Figura K., Hartmann D., Korner C., Matthijs G. Mol. Cell. Biol. 26:5621-5635(2006) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
[3]	"Mammalian phosphomannomutase PMM1 is the brain IMP-sensitive glucose-1,6-bisphosphatase." Veiga-da-Cunha M., Vleugels W., Maliekal P., Matthijs G., Van Schaftingen E. J. Biol. Chem. 283:33988-33993(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF007267 mRNA. Translation: AAB62943.1.
IPI	IPI00132682.
RefSeq	NP_038900.1. NM_013872.3.
UniGene	Mm.18939.
3D structure databases
ProteinModelPortal	O35621.
SMR	O35621. Positions 13-258.
ModBase	Search...
PTM databases
PhosphoSite	O35621.
Proteomic databases
PaxDb	O35621.
PRIDE	O35621.
Protocols and materials databases
DNASU	29858.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000023112; ENSMUSP00000023112; ENSMUSG00000022474.
GeneID	29858.
KEGG	mmu:29858.
Organism-specific databases
CTD	5372.
MGI	MGI:1353418. Pmm1.
Phylogenomic databases
eggNOG	COG0561.
HOGENOM	HOG000181843.
HOVERGEN	HBG009971.
InParanoid	O35621.
KO	K01840.
OMA	NDYEIYD.
OrthoDB	EOG4894NB.
Enzyme and pathway databases
UniPathway	UPA00126; UER00424.
Gene expression databases
ArrayExpress	O35621.
Bgee	O35621.
CleanEx	MM_PMM1.
Genevestigator	O35621.
GermOnline	ENSMUSG00000022474. Mus musculus.
Family and domain databases
Gene3D	3.40.50.1000. 2 hits.
InterPro	IPR023214. HAD-like_dom. IPR006379. HAD-SF_hydro_IIB. IPR005002. PMM. [Graphical view]
PANTHER	PTHR10466. PTHR10466. 1 hit.
Pfam	PF03332. PMM. 1 hit. [Graphical view]
SUPFAM	SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01484. HAD-SF-IIB. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	PMM1. mouse.
NextBio	307058.
SOURCE	Search...

Entry information

Entry name

PMM1_MOUSE

Accession

Primary (citable) accession number: O35621

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	January 1, 1998
Last modified:	April 3, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program