AG10B_MOUSE
ID AG10B_MOUSE Reviewed; 474 AA.
AC Q3UGP8; Q3TLS4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Putative Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase {ECO:0000250|UniProtKB:P50076};
DE EC=2.4.1.256 {ECO:0000250|UniProtKB:P50076};
DE AltName: Full=Alpha-1,2-glucosyltransferase ALG10-A;
DE AltName: Full=Alpha-2-glucosyltransferase ALG10-B;
DE AltName: Full=Asparagine-linked glycosylation protein 10 homolog B;
GN Name=Alg10b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP FUNCTION, AND MUTAGENESIS OF LEU-389.
RX PubMed=24303013; DOI=10.1371/journal.pone.0080408;
RA Probst F.J., Corrigan R.R., Del Gaudio D., Salinger A.P., Lorenzo I.,
RA Gao S.S., Chiu I., Xia A., Oghalai J.S., Justice M.J.;
RT "A point mutation in the gene for asparagine-linked glycosylation 10B
RT (Alg10b) causes nonsyndromic hearing impairment in mice (Mus musculus).";
RL PLoS ONE 8:E80408-E80408(2013).
CC -!- FUNCTION: Putative alpha-1,2-glucosyltransferase, which adds the third
CC glucose residue to the lipid-linked oligosaccharide precursor for N-
CC linked glycosylation. Transfers glucose from dolichyl phosphate glucose
CC (Dol-P-Glc) onto the lipid-linked oligosaccharide
CC Glc(2)Man(9)GlcNAc(2)-PP-Dol (By similarity). When coupled to KCNH2 may
CC reduce KCNH2 sensitivity to classic proarrhythmic drug blockade,
CC possibly by mediating glycosylation of KCNH2 (By similarity). Has a
CC role in maintenance of cochlear outer hair cell function
CC (PubMed:24303013). {ECO:0000250|UniProtKB:O88788,
CC ECO:0000250|UniProtKB:P50076, ECO:0000269|PubMed:24303013}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-
CC alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-
CC GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate
CC + alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-
CC Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-
CC Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-
CC diphosphodolichol + H(+); Xref=Rhea:RHEA:29543, Rhea:RHEA-COMP:9517,
CC Rhea:RHEA-COMP:9528, Rhea:RHEA-COMP:12633, Rhea:RHEA-COMP:12634,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57525, ChEBI:CHEBI:57683,
CC ChEBI:CHEBI:132522, ChEBI:CHEBI:132523; EC=2.4.1.256;
CC Evidence={ECO:0000250|UniProtKB:P50076};
CC -!- SUBUNIT: Interacts with KCNH1 and KCNH2.
CC {ECO:0000250|UniProtKB:O88788}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O88788};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:O88788}.
CC -!- SIMILARITY: Belongs to the ALG10 glucosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AK147821; BAE28159.1; -; mRNA.
DR EMBL; AK166344; BAE38718.1; -; mRNA.
DR CCDS; CCDS27757.1; -.
DR RefSeq; NP_001028613.1; NM_001033441.3.
DR AlphaFoldDB; Q3UGP8; -.
DR STRING; 10090.ENSMUSP00000097882; -.
DR CAZy; GT59; Glycosyltransferase Family 59.
DR iPTMnet; Q3UGP8; -.
DR PhosphoSitePlus; Q3UGP8; -.
DR EPD; Q3UGP8; -.
DR MaxQB; Q3UGP8; -.
DR PaxDb; Q3UGP8; -.
DR PeptideAtlas; Q3UGP8; -.
DR PRIDE; Q3UGP8; -.
DR ProteomicsDB; 285561; -.
DR DNASU; 380959; -.
DR Ensembl; ENSMUST00000100309; ENSMUSP00000097882; ENSMUSG00000075470.
DR GeneID; 380959; -.
DR KEGG; mmu:380959; -.
DR UCSC; uc007xhj.1; mouse.
DR CTD; 144245; -.
DR MGI; MGI:2146159; Alg10b.
DR VEuPathDB; HostDB:ENSMUSG00000075470; -.
DR eggNOG; KOG2642; Eukaryota.
DR GeneTree; ENSGT00390000012906; -.
DR HOGENOM; CLU_017053_1_0_1; -.
DR InParanoid; Q3UGP8; -.
DR OMA; FNCGNLY; -.
DR OrthoDB; 476469at2759; -.
DR PhylomeDB; Q3UGP8; -.
DR TreeFam; TF300150; -.
DR BioGRID-ORCS; 380959; 10 hits in 75 CRISPR screens.
DR PRO; PR:Q3UGP8; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q3UGP8; protein.
DR Bgee; ENSMUSG00000075470; Expressed in manus and 227 other tissues.
DR ExpressionAtlas; Q3UGP8; baseline and differential.
DR Genevisible; Q3UGP8; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0106073; F:dolichyl pyrophosphate Glc2Man9GlcNAc2 alpha-1,2-glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0016740; F:transferase activity; ISO:MGI.
DR GO; GO:0060117; P:auditory receptor cell development; IMP:MGI.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:InterPro.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISO:MGI.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR InterPro; IPR016900; Alg10.
DR PANTHER; PTHR12989; PTHR12989; 1.
DR Pfam; PF04922; DIE2_ALG10; 1.
DR PIRSF; PIRSF028810; Alpha1_2_glucosyltferase_Alg10; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycosyltransferase; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..474
FT /note="Putative Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol
FT alpha-1,2-glucosyltransferase"
FT /id="PRO_0000320064"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..64
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..126
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..175
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..256
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 278..283
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..317
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 339..365
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 387..392
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 414..436
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 437..457
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 458..473
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MUTAGEN 389
FT /note="L->S: Significant hearing impairment, associated
FT with loss or degeneration of cochlear outer hair cells."
FT /evidence="ECO:0000269|PubMed:24303013"
FT CONFLICT 211
FT /note="I -> T (in Ref. 1; BAE38718)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="L -> F (in Ref. 1; BAE38718)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="V -> L (in Ref. 1; BAE38718)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 474 AA; 55465 MW; 8D18F21134AC089F CRC64;
MAQLEGYYFS AALSCTFLVS CLLFSAFSRA LREPYMDEIF HLPQAQRYCE GRFSLSQWDP
MITTLPGLYL VSVGVVKPAS WLLGWSEHVI CSIGVLRFVN LLFSVGNFYL LYLLFRKVQP
RNKASSSIQR ILSTLTLAVF PTLYFFNFLY YTEAGSVFFT LFAYLMCLYG NHRTSALLGF
CGFMFRQTNI IWAAFCAGHL IAQKCSEAWK IELQKKKEER LAPTKGPLSE LRRVLQFLLV
YAMSLKNLRM LFLLTWPYVL LLLAFFAFVV VNGGIVVGDR SSHEACLHFP QLFYFFSFTA
FFSFPHLLSL TKVKTFLSLV WKRRVQFSVV TLVSILLVWK FTYVHKYLLA DNRHYTFYVW
KRVFQRHEVV KYLLVPAYIF AGWAIADSLK AKSIFWNLMF FVCLVASTVP QKLLEFRYFI
LPYIIYRLNI PLPPISRLVC ELGCYTVVNF VTFYIFLNKT FQWPNSQDIQ RFMW
