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Q3TAE8 (ALG6_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 68. 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:
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 names
Name:Alg6
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length507 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Catalytic activity

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.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Potential.

Sequence similarities

Belongs to the ALG6/ALG8 glucosyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 507507Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
PRO_0000284132

Regions

Transmembrane4 – 2421Helical; Potential
Transmembrane115 – 13521Helical; Potential
Transmembrane144 – 16421Helical; Potential
Transmembrane173 – 19321Helical; Potential
Transmembrane227 – 24721Helical; Potential
Transmembrane298 – 31821Helical; Potential
Transmembrane324 – 34421Helical; Potential
Transmembrane362 – 38221Helical; Potential
Transmembrane388 – 40821Helical; Potential
Transmembrane438 – 45821Helical; Potential
Transmembrane473 – 49321Helical; Potential

Experimental info

Sequence conflict4421L → F in BAE34254. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q3TAE8 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: 55D661178739A2CF

FASTA50757,874
        10         20         30         40         50         60 
MESWPWMAVV VLLGLTVRWT VSLSSYSGAG KPPMFGDYEA QRHWQEITLN LPVKQWYFNS 

        70         80         90        100        110        120 
SDNNLLYWGL DYPPLTAYHS LLCAYVAKFI NPDWVALHTS RGYESQAHKL FMRATVLAAD 

       130        140        150        160        170        180 
LLIYVPAVLL YCYSLKEISP KRKIASALCI LLYPGLILID YGHFQYNSVS LGFALWGVLG 

       190        200        210        220        230        240 
VSWDWDLLGS LAFCLALNYK QMELYHSLPF FCFLLGKCFK KGLKGKGLAL FIRIACTVLA 

       250        260        270        280        290        300 
SFLLCWLPFL TEREHALQVV RRLFPVDRGL FEDKVANIWC SVNVFLKIKD TLPRHIQIAI 

       310        320        330        340        350        360 
SFCFTLLSLL PACIKLTVRP SCKGFRFTLV SCALSFFLFS FQVHEKSILL VSLPVCLVLT 

       370        380        390        400        410        420 
EIPFMSTWFL LVSTFSMLPL LLKDELLLPS VVTVMAFVIA CGTFFPMLEN TSEEQLQLKS 

       430        440        450        460        470        480 
FAVSVRRHLP GFTFLPRIMQ CLFLSSVITM VLLTILSVTL DPPQKLPDLF PVLICFVSCV 

       490        500 
NFVFFLVYFN IVIMWDSKNG RNRKKIE 

« Hide

References

[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. 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: NOD.
Tissue: Spleen.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK157903 mRNA. Translation: BAE34254.1.
AK171887 mRNA. Translation: BAE42720.1.
BX005053 Genomic DNA. Translation: CAM22176.1.
BC050854 mRNA. Translation: AAH50854.1.
RefSeqNP_001074733.1. NM_001081264.1.
UniGeneMm.32408.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000095574.

Protein family/group databases

CAZyGT57. Glycosyltransferase Family 57.

PTM databases

PhosphoSiteQ3TAE8.

Proteomic databases

PRIDEQ3TAE8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000097961; ENSMUSP00000095574; ENSMUSG00000073792.
GeneID320438.
KEGGmmu:320438.
UCSCuc008tuw.1. mouse.

Organism-specific databases

CTD29929.
MGIMGI:2444031. Alg6.

Phylogenomic databases

eggNOGNOG287760.
GeneTreeENSGT00550000075073.
HOGENOMHOG000195048.
HOVERGENHBG024331.
InParanoidQ3TAE8.
KOK03848.
OMAMELTIHL.
OrthoDBEOG70088D.
TreeFamTF314522.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ3TAE8.
BgeeQ3TAE8.
GenevestigatorQ3TAE8.

Family and domain databases

InterProIPR004856. Glyco_trans_ALG6/ALG8.
[Graphical view]
PANTHERPTHR12413. PTHR12413. 1 hit.
PfamPF03155. Alg6_Alg8. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio396728.
PROQ3TAE8.
SOURCESearch...

Entry information

Entry nameALG6_MOUSE
AccessionPrimary (citable) accession number: Q3TAE8
Secondary accession number(s): Q3TZF4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: October 11, 2005
Last modified: February 19, 2014
This is version 68 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