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Protein

Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase

Gene

Alg6

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Adds the first glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Man9GlcNAc(2)-PP-Dol (By similarity).By similarity

Catalytic activityi

Dolichyl beta-D-glucosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->6))-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = D-Glc-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->6))-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate.

Pathwayi

GO - Molecular functioni

  1. dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase activity Source: GO_Central
  2. glucosyltransferase activity Source: MGI

GO - Biological processi

  1. oligosaccharide-lipid intermediate biosynthetic process Source: GO_Central
  2. protein N-linked glycosylation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

ReactomeiREACT_262413. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT57. Glycosyltransferase Family 57.

Names & Taxonomyi

Protein namesi
Recommended name:
Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase (EC:2.4.1.267)
Alternative name(s):
Asparagine-linked glycosylation protein 6 homolog
Dol-P-Glc:Man(9)GlcNAc(2)-PP-Dol alpha-1,3-glucosyltransferase
Dolichyl-P-Glc:Man9GlcNAc2-PP-dolichyl glucosyltransferase
Gene namesi
Name:Alg6
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:2444031. Alg6.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei4 – 2421HelicalSequence AnalysisAdd
BLAST
Transmembranei115 – 13521HelicalSequence AnalysisAdd
BLAST
Transmembranei144 – 16421HelicalSequence AnalysisAdd
BLAST
Transmembranei173 – 19321HelicalSequence AnalysisAdd
BLAST
Transmembranei227 – 24721HelicalSequence AnalysisAdd
BLAST
Transmembranei298 – 31821HelicalSequence AnalysisAdd
BLAST
Transmembranei324 – 34421HelicalSequence AnalysisAdd
BLAST
Transmembranei362 – 38221HelicalSequence AnalysisAdd
BLAST
Transmembranei388 – 40821HelicalSequence AnalysisAdd
BLAST
Transmembranei438 – 45821HelicalSequence AnalysisAdd
BLAST
Transmembranei473 – 49321HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: GO_Central
  2. integral component of membrane Source: UniProtKB-KW
  3. membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 507507Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferasePRO_0000284132Add
BLAST

Proteomic databases

MaxQBiQ3TAE8.
PRIDEiQ3TAE8.

PTM databases

PhosphoSiteiQ3TAE8.

Expressioni

Gene expression databases

BgeeiQ3TAE8.
ExpressionAtlasiQ3TAE8. baseline and differential.
GenevestigatoriQ3TAE8.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000095574.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG287760.
GeneTreeiENSGT00550000075073.
HOGENOMiHOG000195048.
HOVERGENiHBG024331.
InParanoidiQ3TAE8.
KOiK03848.
OMAiMELTIHL.
OrthoDBiEOG70088D.
PhylomeDBiQ3TAE8.
TreeFamiTF314522.

Family and domain databases

InterProiIPR004856. Glyco_trans_ALG6/ALG8.
[Graphical view]
PANTHERiPTHR12413. PTHR12413. 1 hit.
PfamiPF03155. Alg6_Alg8. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q3TAE8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESWPWMAVV VLLGLTVRWT VSLSSYSGAG KPPMFGDYEA QRHWQEITLN
60 70 80 90 100
LPVKQWYFNS SDNNLLYWGL DYPPLTAYHS LLCAYVAKFI NPDWVALHTS
110 120 130 140 150
RGYESQAHKL FMRATVLAAD LLIYVPAVLL YCYSLKEISP KRKIASALCI
160 170 180 190 200
LLYPGLILID YGHFQYNSVS LGFALWGVLG VSWDWDLLGS LAFCLALNYK
210 220 230 240 250
QMELYHSLPF FCFLLGKCFK KGLKGKGLAL FIRIACTVLA SFLLCWLPFL
260 270 280 290 300
TEREHALQVV RRLFPVDRGL FEDKVANIWC SVNVFLKIKD TLPRHIQIAI
310 320 330 340 350
SFCFTLLSLL PACIKLTVRP SCKGFRFTLV SCALSFFLFS FQVHEKSILL
360 370 380 390 400
VSLPVCLVLT EIPFMSTWFL LVSTFSMLPL LLKDELLLPS VVTVMAFVIA
410 420 430 440 450
CGTFFPMLEN TSEEQLQLKS FAVSVRRHLP GFTFLPRIMQ CLFLSSVITM
460 470 480 490 500
VLLTILSVTL DPPQKLPDLF PVLICFVSCV NFVFFLVYFN IVIMWDSKNG

RNRKKIE
Length:507
Mass (Da):57,874
Last modified:October 11, 2005 - v1
Checksum:i55D661178739A2CF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti442 – 4421L → F in BAE34254 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK157903 mRNA. Translation: BAE34254.1.
AK171887 mRNA. Translation: BAE42720.1.
BX005053 Genomic DNA. Translation: CAM22176.1.
BC050854 mRNA. Translation: AAH50854.1.
CCDSiCCDS38818.1.
RefSeqiNP_001074733.1. NM_001081264.1.
UniGeneiMm.32408.

Genome annotation databases

EnsembliENSMUST00000097961; ENSMUSP00000095574; ENSMUSG00000073792.
GeneIDi320438.
KEGGimmu:320438.
UCSCiuc008tuw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK157903 mRNA. Translation: BAE34254.1.
AK171887 mRNA. Translation: BAE42720.1.
BX005053 Genomic DNA. Translation: CAM22176.1.
BC050854 mRNA. Translation: AAH50854.1.
CCDSiCCDS38818.1.
RefSeqiNP_001074733.1. NM_001081264.1.
UniGeneiMm.32408.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000095574.

Protein family/group databases

CAZyiGT57. Glycosyltransferase Family 57.

PTM databases

PhosphoSiteiQ3TAE8.

Proteomic databases

MaxQBiQ3TAE8.
PRIDEiQ3TAE8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000097961; ENSMUSP00000095574; ENSMUSG00000073792.
GeneIDi320438.
KEGGimmu:320438.
UCSCiuc008tuw.1. mouse.

Organism-specific databases

CTDi29929.
MGIiMGI:2444031. Alg6.

Phylogenomic databases

eggNOGiNOG287760.
GeneTreeiENSGT00550000075073.
HOGENOMiHOG000195048.
HOVERGENiHBG024331.
InParanoidiQ3TAE8.
KOiK03848.
OMAiMELTIHL.
OrthoDBiEOG70088D.
PhylomeDBiQ3TAE8.
TreeFamiTF314522.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiREACT_262413. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.

Miscellaneous databases

NextBioi396728.
PROiQ3TAE8.
SOURCEiSearch...

Gene expression databases

BgeeiQ3TAE8.
ExpressionAtlasiQ3TAE8. baseline and differential.
GenevestigatoriQ3TAE8.

Family and domain databases

InterProiIPR004856. Glyco_trans_ALG6/ALG8.
[Graphical view]
PANTHERiPTHR12413. PTHR12413. 1 hit.
PfamiPF03155. Alg6_Alg8. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "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: NOD.
    Tissue: Spleen.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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: Embryo.

Entry informationi

Entry nameiALG6_MOUSE
AccessioniPrimary (citable) accession number: Q3TAE8
Secondary accession number(s): Q3TZF4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: October 11, 2005
Last modified: February 4, 2015
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.