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O88788 (AG10B_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
Potassium channel regulator 1
Gene names
Name:Alg10b
Synonyms:Kcr1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length474 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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. Ref.1 Ref.2

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. Ref.1 Ref.2

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.2.

Tissue specificity

Highly expressed in brain, skeletal muscle, uterus, small intestine and liver. Moderately expressed in lung and kidney. Weakly expressed in heart and stomach. Ref.1

Sequence similarities

Belongs to the ALG10 glucosyltransferase family.

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_0000215449

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

Sequences

Sequence LengthMass (Da)Tools
O88788 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 0901C1DEA9C7B9E9

FASTA47455,574
        10         20         30         40         50         60 
MAQLEGYYFS AALSCTFLVS CLLFSAFSRA LREPYMDEIF HLPQAQRYCE GRFSLSQWDP 

        70         80         90        100        110        120 
MITTLPGLYL VSVGVVKPAS WILGWSEHVV CSIGMLRFVN LLFSVGNFYL LYLLFRKIQP 

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

       190        200        210        220        230        240 
CGFMFRQTNI IWAAFCAGHI IAQKCSEAWK TELQKKKEER LPPAKGPLSE LRRVLQFLLM 

       250        260        270        280        290        300 
YSMSLKNLSM LFLLTWPYML LLLAFFVFVV VNGGIVVGDR SSHEACLHFP QLFYFFSFTA 

       310        320        330        340        350        360 
FFSFPHLLSP TKVKTFLSLV WKRRVQFSVI TLVSVFLVWK FTYVHKYLLA DNRHYTFYVW 

       370        380        390        400        410        420 
KRVFQRHEIV KYLLVPAYMF AGWAVADSLK SKSIFWNLMF FVCLVASTVP QKLLEFRYFI 

       430        440        450        460        470 
LPYIIYRLNM PLPPISRLVC ELGCYAVVNF LTFYIFLNKT FQWSDSHDIQ RFMW

« Hide

References

[1]"KCR1, a membrane protein that facilitates functional expression of non-inactivating K+ currents associates with rat EAG voltage-dependent K+ channels."
Hoshi N., Takahashi H., Shahidullah M., Yokoyama S., Higashida H.
J. Biol. Chem. 273:23080-23085(1998) [PubMed: 9722534] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH KCNH1, TISSUE SPECIFICITY.
Strain: Wistar.
Tissue: Cerebellum.
[2]"The IKr drug response is modulated by KCR1 in transfected cardiac and noncardiac cell lines."
Kupershmidt S., Yang I.C.-H., Hayashi K., Wei J., Chanthaphaychith S., Petersen C.I., Johns D.C., George A.L. Jr., Roden D.M., Balser J.R.
FASEB J. 17:2263-2265(2003) [PubMed: 14525949] [Abstract]
Cited for: FUNCTION, INTERACTION WITH KCNH2, SUBCELLULAR LOCATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U78090 mRNA. Translation: AAC34249.1.
IPIIPI00212583.
RefSeqNP_620801.1. NM_139101.2.
UniGeneRn.3635.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGO88788.

Protein family/group databases

CAZyGT59. Glycosyltransferase Family 59.

Proteomic databases

PRIDEO88788.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000019672; ENSRNOP00000019672; ENSRNOG00000014511.
GeneID245960.
KEGGrno:245960.
UCSCNM_139101. rat.

Organism-specific databases

CTD84920.
RGD708500. Alg10b.

Phylogenomic databases

eggNOGroNOG09525.
GeneTreeENSGT00390000012906.
HOVERGENHBG053222.
InParanoidO88788.
OMALLTWPYI.
OrthoDBEOG4THVSZ.
PhylomeDBO88788.

Gene expression databases

GenevestigatorO88788.

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

NextBio623217.

Entry information

Entry nameAG10B_RAT
AccessionPrimary (citable) accession number: O88788
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 1, 1998
Last modified: November 16, 2011
This is version 65 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

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