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Reviewed, UniProtKB/Swiss-Prot Q3TAE8 (ALG6_MOUSE)

Last modified December 15, 2009. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
    EC=2.4.1.-
Alternative name(s):
    Dolichyl-P-Glc:Man9GlcNAc2-PP-dolichyl glucosyltransferase
    Asparagine-linked glycosylation protein 6
Gene names
Name: Alg6
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length507 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Potential.

Sequence similarities

Belongs to the ALG6/ALG8 glucosyltransferase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

Regions

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

Experimental info

Sequence conflict4421L → F in BAE34254. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q3TAE8-1 [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: 16141072] [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: 19468303] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

AK157903 mRNA. Translation: BAE34254.1.
AK171887 mRNA. Translation: BAE42720.1.
BX005053 Genomic DNA. Translation: CAM22176.1.
BC050854 mRNA. Translation: AAH50854.1.
IPIIPI00221535.
RefSeqNP_001074733.1.
UniGeneMm.32408

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ3TAE8.

Protein family/group databases

CAZyGT57. Glycosyltransferase Family 57.

Proteomic databases

PRIDEQ3TAE8.

Genome annotation databases

EnsemblENSMUST00000097961; ENSMUSP00000095574; ENSMUSG00000073792; Mus musculus. [Genome view]
ENSMUST00000107007; ENSMUSP00000102620; ENSMUSG00000073792; Mus musculus. [Genome view]
GeneID320438.
KEGGmmu:320438.
NMPDRfig|10090.3.peg.9953.
UCSCuc008tuw.1. mouse.

Organism-specific databases

CTD320438.
MGIMGI:2444031. Alg6.

Phylogenomic databases

HOGENOMHBG621987.
HOVERGENQ3TAE8.
InParanoidQ3TAE8.
OMAIMWDSRN.

Gene expression databases

ArrayExpressQ3TAE8.
BgeeQ3TAE8.
GenevestigatorQ3TAE8.

Family and domain databases

InterProIPR004856. Glycosyltransferase_ALG6/ALG8.
[Graphical view]
PANTHERPTHR12413. Alg6_Alg8. 1 hit.
PfamPF03155. Alg6_Alg8. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio396728.
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: December 15, 2009
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents