Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Probable dolichol-phosphate mannosyltransferase

Gene

CG10166

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

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.By similarity

Catalytic activityi

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

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT2. Glycosyltransferase Family 2.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable dolichol-phosphate mannosyltransferase (EC:2.4.1.83)
Short name:
DPM synthase
Short name:
Dolichol-phosphate mannose synthase
Alternative name(s):
Dolichyl-phosphate beta-D-mannosyltransferase
Mannose-P-dolichol synthase
Short name:
MPD synthase
Gene namesi
ORF Names:CG10166
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0032799. CG10166.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 241241Probable dolichol-phosphate mannosyltransferasePRO_0000059172Add
BLAST

Proteomic databases

PaxDbiQ9VIU7.
PRIDEiQ9VIU7.

Expressioni

Gene expression databases

BgeeiQ9VIU7.
ExpressionAtlasiQ9VIU7. differential.
GenevisibleiQ9VIU7. DM.

Interactioni

Protein-protein interaction databases

DIPiDIP-17174N.
MINTiMINT-980632.
STRINGi7227.FBpp0080817.

Structurei

3D structure databases

ProteinModelPortaliQ9VIU7.
SMRiQ9VIU7. Positions 5-113.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 2 family.Curated

Phylogenomic databases

eggNOGiKOG2978. Eukaryota.
COG0463. LUCA.
GeneTreeiENSGT00550000075000.
InParanoidiQ9VIU7.
KOiK00721.
OMAiTAYIHGF.
OrthoDBiEOG7W41CN.
PhylomeDBiQ9VIU7.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF00535. Glycos_transf_2. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9VIU7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPTNGHKYSI LMPTYNEKDN LPIIIWLIVK YMKASGLEYE VIVIDDGSPD
60 70 80 90 100
GTLDVAKDLQ KIYGEDKIVL RPRGSKLGLG TAYIHGIKHA TGDFIVIIDA
110 120 130 140 150
DLSHHPKFIP EFIKLQQEGN YDIVSGTRYA GNGGVFGWDF KRKLISRGAN
160 170 180 190 200
FLSQVLLRPN ASDLTGSFRL YKKDVLEKCI ASCVSKGYVF QMEMLVRARQ
210 220 230 240
HGYTIAEVPI TFVDRIYGTS KLGGTEIIQF AKNLLYLFAT T
Length:241
Mass (Da):27,002
Last modified:May 1, 2000 - v1
Checksum:i45ECC64EF96B0C38
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA. Translation: AAF53817.1.
RefSeqiNP_609980.1. NM_136136.3.

Genome annotation databases

EnsemblMetazoaiFBtr0081279; FBpp0080817; FBgn0032799.
GeneIDi35240.
KEGGidme:Dmel_CG10166.
UCSCiCG10166-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA. Translation: AAF53817.1.
RefSeqiNP_609980.1. NM_136136.3.

3D structure databases

ProteinModelPortaliQ9VIU7.
SMRiQ9VIU7. Positions 5-113.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-17174N.
MINTiMINT-980632.
STRINGi7227.FBpp0080817.

Protein family/group databases

CAZyiGT2. Glycosyltransferase Family 2.

Proteomic databases

PaxDbiQ9VIU7.
PRIDEiQ9VIU7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0081279; FBpp0080817; FBgn0032799.
GeneIDi35240.
KEGGidme:Dmel_CG10166.
UCSCiCG10166-RA. d. melanogaster.

Organism-specific databases

FlyBaseiFBgn0032799. CG10166.

Phylogenomic databases

eggNOGiKOG2978. Eukaryota.
COG0463. LUCA.
GeneTreeiENSGT00550000075000.
InParanoidiQ9VIU7.
KOiK00721.
OMAiTAYIHGF.
OrthoDBiEOG7W41CN.
PhylomeDBiQ9VIU7.

Enzyme and pathway databases

UniPathwayiUPA00378.

Miscellaneous databases

GenomeRNAii35240.
NextBioi792550.
PROiQ9VIU7.

Gene expression databases

BgeeiQ9VIU7.
ExpressionAtlasiQ9VIU7. differential.
GenevisibleiQ9VIU7. DM.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF00535. Glycos_transf_2. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.

Entry informationi

Entry nameiDPM1_DROME
AccessioniPrimary (citable) accession number: Q9VIU7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: May 1, 2000
Last modified: May 11, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.