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Q3UGP8 (AG10B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase
EC=2.4.1.256
Alternative name(s):
Alpha-1,2-glucosyltransferase ALG10-A
Alpha-2-glucosyltransferase ALG10-B
Asparagine-linked glycosylation protein 10 homolog B
Gene names
Name:Alg10b
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length474 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Putative alpha-1,2-glucosyltransferase, which adds the third 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 Glc2Man9GlcNAc(2)-PP-Dol. When coupled to KCNH2 may reduce KCNH2 sensitivity to classic proarrhythmic drug blockade, possibly by mediating glycosylation of KCNH2 By similarity.

Catalytic activity

Dolichyl beta-D-glucosyl phosphate + D-Glc-alpha-(1->3)-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 = D-Glc-alpha-(1->2)-D-Glc-alpha-(1->3)-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.

Subunit structure

Interacts with KCNH1 and KCNH2 By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the ALG10 glucosyltransferase family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiontransferase activity, transferring hexosyl groups

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 474474Putative Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase
PRO_0000320064

Regions

Topological domain1 – 66Cytoplasmic Potential
Transmembrane7 – 2721Helical; Potential
Topological domain28 – 6437Extracellular Potential
Transmembrane65 – 8521Helical; Potential
Topological domain86 – 9712Cytoplasmic Potential
Transmembrane98 – 11821Helical; Potential
Topological domain119 – 1268Extracellular Potential
Transmembrane127 – 14721Helical; Potential
Topological domain148 – 1503Cytoplasmic Potential
Transmembrane151 – 17121Helical; Potential
Topological domain172 – 1754Extracellular Potential
Transmembrane176 – 19621Helical; Potential
Topological domain197 – 25660Cytoplasmic Potential
Transmembrane257 – 27721Helical; Potential
Topological domain278 – 2836Extracellular Potential
Transmembrane284 – 30421Helical; Potential
Topological domain305 – 31713Cytoplasmic Potential
Transmembrane318 – 33821Helical; Potential
Topological domain339 – 36527Extracellular Potential
Transmembrane366 – 38621Helical; Potential
Topological domain387 – 3926Cytoplasmic Potential
Transmembrane393 – 41321Helical; Potential
Topological domain414 – 43623Extracellular Potential
Transmembrane437 – 45721Helical; Potential
Topological domain458 – 47316Cytoplasmic Potential

Experimental info

Sequence conflict2111I → T in BAE38718. Ref.1
Sequence conflict2211L → F in BAE38718. Ref.1
Sequence conflict2401V → L in BAE38718. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q3UGP8 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: 8D18F21134AC089F

FASTA47455,465
        10         20         30         40         50         60 
MAQLEGYYFS AALSCTFLVS CLLFSAFSRA LREPYMDEIF HLPQAQRYCE GRFSLSQWDP 

        70         80         90        100        110        120 
MITTLPGLYL VSVGVVKPAS WLLGWSEHVI CSIGVLRFVN LLFSVGNFYL LYLLFRKVQP 

       130        140        150        160        170        180 
RNKASSSIQR ILSTLTLAVF PTLYFFNFLY YTEAGSVFFT LFAYLMCLYG NHRTSALLGF 

       190        200        210        220        230        240 
CGFMFRQTNI IWAAFCAGHL IAQKCSEAWK IELQKKKEER LAPTKGPLSE LRRVLQFLLV 

       250        260        270        280        290        300 
YAMSLKNLRM LFLLTWPYVL LLLAFFAFVV VNGGIVVGDR SSHEACLHFP QLFYFFSFTA 

       310        320        330        340        350        360 
FFSFPHLLSL TKVKTFLSLV WKRRVQFSVV TLVSILLVWK FTYVHKYLLA DNRHYTFYVW 

       370        380        390        400        410        420 
KRVFQRHEVV KYLLVPAYIF AGWAIADSLK AKSIFWNLMF FVCLVASTVP QKLLEFRYFI 

       430        440        450        460        470 
LPYIIYRLNI PLPPISRLVC ELGCYTVVNF VTFYIFLNKT FQWPNSQDIQ RFMW

« 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: C57BL/6J.
Tissue: Mammary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK147821 mRNA. Translation: BAE28159.1.
AK166344 mRNA. Translation: BAE38718.1.
IPIIPI00381144.
RefSeqNP_001028613.1. NM_001033441.3.
UniGeneMm.17853.

3D structure databases

ProteinModelPortalQ3UGP8.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3UGP8.

Protein family/group databases

CAZyGT59. Glycosyltransferase Family 59.

Proteomic databases

PRIDEQ3UGP8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000100309; ENSMUSP00000097882; ENSMUSG00000075470.
GeneID380959.
KEGGmmu:380959.
UCSCuc007xhj.1. mouse.

Organism-specific databases

CTD144245.
MGIMGI:2146159. Alg10b.

Phylogenomic databases

HOGENOMHBG714502.
HOVERGENHBG053222.
InParanoidQ3UGP8.
OMALLTWPYI.
OrthoDBEOG4THVSZ.

Gene expression databases

ArrayExpressQ3UGP8.
BgeeQ3UGP8.
GenevestigatorQ3UGP8.

Family and domain databases

InterProIPR016900. Alpha1_2_glucosyltferase_Alg10.
IPR007006. Glycosyltransferase_ALG10.
[Graphical view]
KOK03850.
PANTHERPTHR12989. DIE2_ALG10. 1 hit.
PfamPF04922. DIE2_ALG10. 1 hit.
[Graphical view]
PIRSFPIRSF028810. Alpha1_2_glucosyltferase_Alg10. 1 hit.
ProtoNetSearch...

Other

NextBio401419.
SOURCESearch...

Entry information

Entry nameAG10B_MOUSE
AccessionPrimary (citable) accession number: Q3UGP8
Secondary accession number(s): Q3TLS4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: October 11, 2005
Last modified: November 16, 2011
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents