LIPID MAPS

LMPD ID

LMP007360

Gene ID

856313

Species

Saccharomyces cerevisiae S288c (Yeast (S288c))

Gene Name

dolichyl-phosphate beta-D-mannosyltransferase

Gene Symbol

DPM1

Synonyms

SED3

Chromosome

XVI

EC Number

2.4.1.83

dolichyl-phosphate beta-D-mannosyltransferase
Refseq ID	NP_015509
Protein GI	6325441
UniProt ID	P14020
mRNA ID	NM_001184280
Length	267
MSIEYSVIVPAYHEKLNIKPLTTRLFAGMSPEMAKKTELIFVDDNSQDGSVEEVDALAHQGYNVRIIVRTNERGLSSAVLKGFYEAKGQYLVCMDADLQHPPETVPKLFESLHDHAFTLGTRYAPGVGIDKDWPMYRRVISSTARMMARPLTIASDPMSGFFGLQKKYLENCNPRDINSQGFKIALELLAKLPLPRDPRVAIGEVPFTFGVRTEGESKLSGKVIIQYLQQLKELYVFKFGANNLILFITFWSILFFYVCYQLYHLVF

Entrez Gene ID

856313

Gene Name

dolichyl-phosphate beta-D-mannosyltransferase

Gene Symbol

DPM1

Species

Saccharomyces cerevisiae S288c

Gene Ontology (GO Annotations)

GO ID	Source	Type	Description
GO:0005783	IDA:SGD	C	endoplasmic reticulum
GO:0016021	IEA:UniProtKB-KW	C	integral component of membrane
GO:0042175	IDA:SGD	C	nuclear outer membrane-endoplasmic reticulum membrane network
GO:0004582	IDA:SGD	F	dolichyl-phosphate beta-D-mannosyltransferase activity
GO:0006506	IMP:SGD	P	GPI anchor biosynthetic process
GO:0097502	IDA:GOC	P	mannosylation
GO:0006487	IMP:SGD	P	protein N-linked glycosylation
GO:0006493	IMP:SGD	P	protein O-linked glycosylation

KEGG Pathway Links

KEGG Pathway ID	Description
sce01100	Metabolic pathways
ko00510	N-Glycan biosynthesis
sce00510	N-Glycan biosynthesis

BIOCYC Pathway Links

BIOCYC Pathway ID	Description
PWY3O-123	dolichyl phosphate D-mannose biosynthesis
MANNOSYL-CHITO-DOLICHOL-BIOSYNTHESIS	dolichyl-diphosphooligosaccharide biosynthesis
MANNOSYL-CHITO-DOLICHOL-BIOSYNTHESIS	dolichyl-diphosphooligosaccharide biosynthesis

InterPro Annotations

Accession	Description
IPR001173	Glycosyltransferase 2-like
IPR029044	Nucleotide-diphospho-sugar transferases

Entry Information

Gene Name

dolichyl-phosphate beta-D-mannosyltransferase

Protein Entry

DPM1_YEAST

UniProt ID

P14020

Species

Yeast (S288c)

Comments

Comment Type	Description
Biophysicochemical Properties	Kinetic parameters: KM=1.2 uM for GDP-mannose {ECO:0000269\|PubMed:15548536}; Vmax=25.1 nmol/min/mg enzyme for GDP-mannose {ECO:0000269\|PubMed:15548536}; Note=For the phosphorylated protein, the Vmax increases to 146.7 nmol/min/mg enzyme, whereas the KM stays at 1.1 uM for GDP- mannose, increasing the catalytic efficiency 6-fold.;
Biophysicochemical Properties	Kinetic parameters: KM=1.2 uM for GDP-mannose ; Vmax=25.1 nmol/min/mg enzyme for GDP-mannose ; Note=For the phosphorylated protein, the Vmax increases to 146.7 nmol/min/mg enzyme, whereas the KM stays at 1.1 uM for GDP- mannose, increasing the catalytic efficiency 6-fold.;
Catalytic Activity	GDP-mannose + dolichyl phosphate = GDP + dolichyl D-mannosyl phosphate.
Function	Transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O- mannosylation of proteins.
Miscellaneous	Present with 1885 molecules/cell in log phase SD medium
Miscellaneous	Present with 1885 molecules/cell in log phase SD medium. {ECO:0000269\|PubMed:14562106}.
Pathway	Protein modification; protein glycosylation.
Similarity	Belongs to the glycosyltransferase 2 family
Similarity	Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
Subcellular Location	Endoplasmic reticulum membrane ; Single-pass type IV membrane protein {ECO:0000269\|PubMed:14562095, ECO:0000269\|PubMed:15657391}.
Subcellular Location	Endoplasmic reticulum membrane {ECO:0000269\|PubMed:14562095, ECO:0000269\|PubMed:15657391}; Single-pass type IV membrane protein {ECO:0000269\|PubMed:14562095, ECO:0000269\|PubMed:15657391}.
Subunit	Interacts with the C-terminus of SAC1, thereby sequestering it to the endoplasmic reticulum in exponentially growing cells. Under nutrient limitation conditions, this interaction is rapidly abolished
Subunit	Interacts with the C-terminus of SAC1, thereby sequestering it to the endoplasmic reticulum in exponentially growing cells. Under nutrient limitation conditions, this interaction is rapidly abolished. {ECO:0000269\|PubMed:15657391}.