ID AG10B_HUMAN Reviewed; 473 AA. AC Q5I7T1; B2RPF4; DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 2. DT 24-JAN-2024, entry version 143. 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; DE AltName: Full=Potassium channel regulator 1; GN Name=ALG10B; Synonyms=KCR1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND VARIANT RP GLY-84. RX PubMed=14525949; DOI=10.1096/fj.02-1057fje; RA Kupershmidt S., Yang I.C.-H., Hayashi K., Wei J., Chanthaphaychith S., RA Petersen C.I., Johns D.C., George A.L. Jr., Roden D.M., Balser J.R.; RT "The IKr drug response is modulated by KCR1 in transfected cardiac and RT noncardiac cell lines."; RL FASEB J. 17:2263-2265(2003). RN [2] RP SEQUENCE REVISION. RA George A.L. Jr.; RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLY-84. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-84. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP VARIANT VAL-446. RX PubMed=15280551; DOI=10.1073/pnas.0306005101; RA Petersen C.I., McFarland T.R., Stepanovic S.Z., Yang P., Reiner D.J., RA Hayashi K., George A.L. Jr., Roden D.M., Thomas J.H., Balser J.R.; RT "In vivo identification of genes that modify ether-a-go-go-related gene RT activity in Caenorhabditis elegans may also affect human cardiac RT arrhythmia."; RL Proc. Natl. Acad. Sci. U.S.A. 101:11773-11778(2004). 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 (PubMed:14525949). Has a CC role in maintenance of cochlear outer hair cell function (By CC similarity). {ECO:0000250|UniProtKB:P50076, CC ECO:0000250|UniProtKB:Q3UGP8, ECO:0000269|PubMed:14525949}. 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 -!- PATHWAY: Protein modification; protein glycosylation. CC -!- SUBUNIT: Interacts with KCNH1 and KCNH2. CC {ECO:0000250|UniProtKB:O88788}. CC -!- INTERACTION: CC Q5I7T1; P11912: CD79A; NbExp=3; IntAct=EBI-18075734, EBI-7797864; CC Q5I7T1; Q3SXP7: SHISAL1; NbExp=3; IntAct=EBI-18075734, EBI-18037857; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O88788}; CC Multi-pass membrane protein {ECO:0000250|UniProtKB:O88788}. CC -!- TISSUE SPECIFICITY: Highly expressed in heart, placenta, liver, kidney CC and pancreas. Weakly expressed in lung, skeletal muscle and brain. CC {ECO:0000269|PubMed:14525949}. CC -!- SIMILARITY: Belongs to the ALG10 glucosyltransferase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY845858; AAW31756.1; -; mRNA. DR EMBL; AC117372; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471111; EAW57795.1; -; Genomic_DNA. DR EMBL; BC137413; AAI37414.1; -; mRNA. DR EMBL; BC137414; AAI37415.1; -; mRNA. DR CCDS; CCDS31772.1; -. DR RefSeq; NP_001013642.1; NM_001013620.3. DR AlphaFoldDB; Q5I7T1; -. DR BioGRID; 126840; 47. DR IntAct; Q5I7T1; 5. DR STRING; 9606.ENSP00000310120; -. DR GlyGen; Q5I7T1; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q5I7T1; -. DR PhosphoSitePlus; Q5I7T1; -. DR SwissPalm; Q5I7T1; -. DR BioMuta; ALG10B; -. DR DMDM; 296434391; -. DR EPD; Q5I7T1; -. DR jPOST; Q5I7T1; -. DR MassIVE; Q5I7T1; -. DR MaxQB; Q5I7T1; -. DR PaxDb; 9606-ENSP00000310120; -. DR PeptideAtlas; Q5I7T1; -. DR ProteomicsDB; 62974; -. DR Pumba; Q5I7T1; -. DR Antibodypedia; 55463; 80 antibodies from 14 providers. DR DNASU; 144245; -. DR Ensembl; ENST00000308742.9; ENSP00000310120.4; ENSG00000175548.9. DR GeneID; 144245; -. DR KEGG; hsa:144245; -. DR MANE-Select; ENST00000308742.9; ENSP00000310120.4; NM_001013620.4; NP_001013642.2. DR UCSC; uc001rln.5; human. DR AGR; HGNC:31088; -. DR CTD; 144245; -. DR DisGeNET; 144245; -. DR GeneCards; ALG10B; -. DR HGNC; HGNC:31088; ALG10B. DR HPA; ENSG00000175548; Low tissue specificity. DR MalaCards; ALG10B; -. DR MIM; 603313; gene. DR neXtProt; NX_Q5I7T1; -. DR OpenTargets; ENSG00000175548; -. DR PharmGKB; PA134936082; -. DR VEuPathDB; HostDB:ENSG00000175548; -. DR eggNOG; KOG2642; Eukaryota. DR GeneTree; ENSGT00390000012906; -. DR HOGENOM; CLU_017053_1_0_1; -. DR InParanoid; Q5I7T1; -. DR OMA; INKTFQW; -. DR OrthoDB; 50992at2759; -. DR PhylomeDB; Q5I7T1; -. DR TreeFam; TF300150; -. DR PathwayCommons; Q5I7T1; -. DR Reactome; R-HSA-446193; Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein. DR SignaLink; Q5I7T1; -. DR UniPathway; UPA00378; -. DR BioGRID-ORCS; 144245; 116 hits in 1082 CRISPR screens. DR ChiTaRS; ALG10B; human. DR GenomeRNAi; 144245; -. DR Pharos; Q5I7T1; Tbio. DR PRO; PR:Q5I7T1; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q5I7T1; Protein. DR Bgee; ENSG00000175548; Expressed in calcaneal tendon and 159 other cell types or tissues. DR ExpressionAtlas; Q5I7T1; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. 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; IDA:UniProtKB. DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:InterPro. DR GO; GO:1901980; P:positive regulation of inward rectifier potassium channel activity; IMP:UniProtKB. DR GO; GO:0060050; P:positive regulation of protein glycosylation; IMP:UniProtKB. DR GO; GO:0006486; P:protein glycosylation; IMP:UniProtKB. DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central. DR InterPro; IPR016900; Alg10. DR PANTHER; PTHR12989; ALPHA-1,2-GLUCOSYLTRANSFERASE ALG10; 1. DR PANTHER; PTHR12989:SF12; DOL-P-GLC:GLC(2)MAN(9)GLCNAC(2)-PP-DOL ALPHA-1,2-GLUCOSYLTRANSFERASE-RELATED; 1. DR Pfam; PF04922; DIE2_ALG10; 1. DR PIRSF; PIRSF028810; Alpha1_2_glucosyltferase_Alg10; 1. DR Genevisible; Q5I7T1; HS. PE 1: Evidence at protein level; KW Cell membrane; Glycosyltransferase; Membrane; Reference proteome; KW Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1..473 FT /note="Putative Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol FT alpha-1,2-glucosyltransferase" FT /id="PRO_0000215448" 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 VARIANT 84 FT /note="A -> G (in dbSNP:rs6582584)" FT /evidence="ECO:0000269|PubMed:14525949, FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.4" FT /id="VAR_048217" FT VARIANT 383 FT /note="S -> N (in dbSNP:rs57963306)" FT /id="VAR_061002" FT VARIANT 446 FT /note="I -> V (in dbSNP:rs61730283)" FT /evidence="ECO:0000269|PubMed:15280551" FT /id="VAR_023753" SQ SEQUENCE 473 AA; 55448 MW; 47D0CF7B6C84B8EC CRC64; MAQLEGYCFS AALSCTFLVS CLLFSAFSRA LREPYMDEIF HLPQAQRYCE GHFSLSQWDP MITTLPGLYL VSVGVVKPAI WIFAWSEHVV CSIGMLRFVN LLFSVGNFYL LYLLFHKVQP RNKAASSIQR VLSTLTLAVF PTLYFFNFLY YTEAGSMFFT LFAYLMCLYG NHKTSAFLGF CGFMFRQTNI IWAVFCAGNV IAQKLTEAWK TELQKKEDRL PPIKGPFAEF RKILQFLLAY SMSFKNLSML FCLTWPYILL GFLFCAFVVV NGGIVIGDRS SHEACLHFPQ LFYFFSFTLF FSFPHLLSPS KIKTFLSLVW KHGILFLVVT LVSVFLVWKF TYAHKYLLAD NRHYTFYVWK RVFQRYAILK YLLVPAYIFA GWSIADSLKS KPIFWNLMFF ICLFIVIVPQ KLLEFRYFIL PYVIYRLNIT LPPTSRLVCE LSCYAIVNFI TFYIFLNKTF QWPNSQDIQR FMW //