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Reviewed, UniProtKB/Swiss-Prot Q3UGP8 (AG10B_MOUSE)

Last modified December 15, 2009. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

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Names and origin

Protein namesRecommended name:
    Putative alpha-1,2-glucosyltransferase ALG10-B
      Short name=Alpha-2-glucosyltransferase ALG10-B
    EC=2.4.1.-
Alternative name(s):
    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

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Protein attributes

Sequence length474 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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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.

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.

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Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
   Molecular functionGlycosyltransferase
Transferase
Gene Ontology (GO)
   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functiontransferase activity, transferring hexosyl groups

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 474474Putative alpha-1,2-glucosyltransferase ALG10-B
PRO_0000320064

Regions

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

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Sequences

Sequence LengthMass (Da)Tools
Q3UGP8-1 [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

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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.

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Cross-references

Sequence databases

AK147821 mRNA. Translation: BAE28159.1.
AK166344 mRNA. Translation: BAE38718.1.
IPIIPI00381144.
RefSeqNP_001028613.1.
UniGeneMm.17853

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ3UGP8.

Protein family/group databases

CAZyGT59. Glycosyltransferase Family 59.

Proteomic databases

PRIDEQ3UGP8.

Genome annotation databases

EnsemblENSMUST00000100309; ENSMUSP00000097882; ENSMUSG00000075470; Mus musculus. [Genome view]
GeneID380959.
KEGGmmu:380959.
UCSCuc007xhk.1. mouse.

Organism-specific databases

CTD380959.
MGIMGI:2146159. Alg10b.

Phylogenomic databases

HOGENOMHBG714502.
HOVERGENQ3UGP8.
InParanoidQ3UGP8.
OMALLTWPYI.
OrthoDBEOG9XKXSM.

Gene expression databases

ArrayExpressQ3UGP8.
BgeeQ3UGP8.
GenevestigatorQ3UGP8.

Family and domain databases

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

Other Resources

NextBio401419.
SOURCESearch...

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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: December 15, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

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

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