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O70152 (DPM1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dolichol-phosphate mannosyltransferase subunit 1

EC=2.4.1.83
Alternative name(s):
Dolichol-phosphate mannose synthase subunit 1
Short name=DPM synthase subunit 1
Dolichyl-phosphate beta-D-mannosyltransferase subunit 1
Mannose-P-dolichol synthase subunit 1
Short name=MPD synthase
Gene names
Name:Dpm1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length260 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 subunit of the dolichol-phosphate mannose (DPM) synthase complex By similarity.

Catalytic activity

GDP-mannose + dolichyl phosphate = GDP + dolichyl D-mannosyl phosphate.

Pathway

Protein modification; protein glycosylation.

Subunit structure

Component of the dolichol-phosphate mannose (DPM) synthase complex composed of DPM1, DPM2 and DPM3; in the complex interacts directly with DPM3 By similarity.

Subcellular location

Endoplasmic reticulum.

Sequence similarities

Belongs to the glycosyltransferase 2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 260259Dolichol-phosphate mannosyltransferase subunit 1
PRO_0000059171

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue91Phosphoserine By similarity

Experimental info

Sequence conflict761E → G in BAB25735. Ref.2
Sequence conflict1221S → Y in BAB25735. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O70152 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 8CB1BCDF1977EBA6

FASTA26029,175
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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.

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.
CCDSCCDS17109.1.
RefSeqNP_034202.1. NM_010072.3.
UniGeneMm.422657.

3D structure databases

ProteinModelPortalO70152.
SMRO70152. Positions 26-120.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO70152. 2 interactions.
MINTMINT-4093451.

Protein family/group databases

CAZyGT2. Glycosyltransferase Family 2.

PTM databases

PhosphoSiteO70152.

Proteomic databases

MaxQBO70152.
PaxDbO70152.
PRIDEO70152.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000138667; ENSMUSP00000139070; ENSMUSG00000093752.
ENSMUST00000154111; ENSMUSP00000118776; ENSMUSG00000078919.
GeneID13480.
KEGGmmu:13480.
UCSCuc008oas.1. mouse.

Organism-specific databases

CTD8813.
MGIMGI:1330239. Dpm1.

Phylogenomic databases

eggNOGCOG0463.
GeneTreeENSGT00550000075000.
HOVERGENHBG018967.
InParanoidO70152.
KOK00721.
OMAHGIKHAT.
OrthoDBEOG7W41CN.
PhylomeDBO70152.
TreeFamTF105617.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

BgeeO70152.
CleanExMM_DPM1.
GenevestigatorO70152.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
InterProIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamPF00535. Glycos_transf_2. 1 hit.
[Graphical view]
SUPFAMSSF53448. SSF53448. 1 hit.
ProtoNetSearch...

Other

NextBio283971.
PROO70152.
SOURCESearch...

Entry information

Entry nameDPM1_MOUSE
AccessionPrimary (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: July 9, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot