O70152 (DPM1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dolichol-phosphate mannosyltransferase
EC=2.4.1.83

Alternative name(s):
Dolichol-phosphate mannose synthase
Short name=DPM synthase
Dolichyl-phosphate beta-D-mannosyltransferase
Mannose-P-dolichol synthase
Short name=MPD synthase

Gene names

Name:

Dpm1

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	260 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

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.
Catalytic activity	GDP-mannose + dolichyl phosphate = GDP + dolichyl D-mannosyl phosphate.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Endoplasmic reticulum.
Sequence similarities	Belongs to the glycosyltransferase 2 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Molecular function	Glycosyltransferase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	GDP-mannose metabolic process Inferred from electronic annotation. Source: Compara GPI anchor biosynthetic process Inferred from sequence or structural similarity. Source: HGNC dolichol metabolic process Inferred from mutant phenotype Ref.1. Source: MGI protein O-linked mannosylation Inferred from sequence or structural similarity. Source: HGNC
Cellular_component	dolichol-phosphate-mannose synthase complex Inferred from electronic annotation. Source: Compara endoplasmic reticulum membrane Inferred from sequence or structural similarity. Source: HGNC
Molecular_function	alcohol binding Inferred from electronic annotation. Source: Compara dolichyl-phosphate beta-D-mannosyltransferase activity Inferred from sequence or structural similarity. Source: HGNC dolichyl-phosphate-mannose-protein mannosyltransferase activity Inferred from sequence or structural similarity. Source: HGNC mannose binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 260	259	Dolichol-phosphate mannosyltransferase		PRO_0000059171
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
	Modified residue	9	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	76	1	E → G in BAB25735. Ref.2
	Sequence conflict	122	1	S → Y in BAB25735. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O70152 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 8CB1BCDF1977EBA6	FASTA	260	29,175
	10 20 30 40 50 60 MASTGASRSL AASPRPPQGR SSRQDKYSVL LPTYNERENL PLIVWLLVKS FSESAINYEI 70 80 90 100 110 120 IIIDDGSPDG TREVAEQLAE IYGPDRILLR PREKKLGLGT AYIHGIKHAT GNYVIIMDAD 130 140 150 160 170 180 LSHHPKFIPE FIRKQKEGNF DIVSGTRYKG NGGVYGWDLK RKIISRGANF ITQILLRPGA 190 200 210 220 230 240 SDLTGSFRLY RKEVLQKLIE KCVSKGYVFQ MEMIVRARQM NYTIGEVPIS FVDRVYGESK 250 260 LGGNEIVSFL KGLLTLFATT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A homologue of Saccharomyces cerevisiae Dpm1p is not sufficient for synthesis of dolichol-phosphate-mannose in mammalian cells." Tomita S., Inoue N., Maeda Y., Ohishi K., Takeda J., Kinoshita T. J. Biol. Chem. 273:9249-9254(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Cerebellum, Lung and Small intestine.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB004789 mRNA. Translation: BAA25759.1. AK005268 mRNA. Translation: BAB23920.1. AK004834 mRNA. Translation: BAB23602.1. AK008548 mRNA. Translation: BAB25735.1. BC061151 mRNA. Translation: AAH61151.1.
IPI	IPI00115668.
RefSeq	NP_034202.1. NM_010072.3.
UniGene	Mm.422657.
3D structure databases
ProteinModelPortal	O70152.
SMR	O70152. Positions 26-120.
ModBase	Search...
Protein-protein interaction databases
IntAct	O70152. 1 interaction.
Protein family/group databases
CAZy	GT2. Glycosyltransferase Family 2.
PTM databases
PhosphoSite	O70152.
Proteomic databases
PaxDb	O70152.
PRIDE	O70152.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000154111; ENSMUSP00000118776; ENSMUSG00000078919.
GeneID	13480.
KEGG	mmu:13480.
Organism-specific databases
CTD	8813.
MGI	MGI:1330239. Dpm1.
Phylogenomic databases
eggNOG	COG0463.
GeneTree	ENSGT00550000075000.
HOVERGEN	HBG018967.
InParanoid	O70152.
KO	K00721.
OMA	HPKFIPQ.
Enzyme and pathway databases
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	O70152.
Bgee	O70152.
CleanEx	MM_DPM1.
Genevestigator	O70152.
GermOnline	ENSMUSG00000051149. Mus musculus.
Family and domain databases
InterPro	IPR001173. Glyco_trans_2. [Graphical view]
Pfam	PF00535. Glycos_transf_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	283971.
SOURCE	Search...

Entry information

Entry name

DPM1_MOUSE

Accession

Primary (citable) accession number: O70152
Secondary accession number(s): Q9D829

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	August 1, 1998
Last modified:	May 1, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program