AG10B_HUMAN
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 03-AUG-2022, entry version 136.
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, CHARACTERIZATION OF VARIANT VAL-446, AND POSSIBLE
RP PROTECTIVE ROLE IN SUSCEPTIBILITY TO ACQUIRED LONG QT SYNDROME.
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 -!- POLYMORPHISM: Genetic variations in ALG10B may reduce susceptibility to
CC acquired long QT syndrome.
CC -!- SIMILARITY: Belongs to the ALG10 glucosyltransferase family.
CC {ECO:0000305}.
CC -!- CAUTION: PubMed:15280551 reports a Val-447 variant, however there is
CC evidence that the right variant is Val-446. {ECO:0000305}.
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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 iPTMnet; Q5I7T1; -.
DR PhosphoSitePlus; Q5I7T1; -.
DR BioMuta; ALG10B; -.
DR DMDM; 296434391; -.
DR EPD; Q5I7T1; -.
DR jPOST; Q5I7T1; -.
DR MassIVE; Q5I7T1; -.
DR MaxQB; Q5I7T1; -.
DR PaxDb; Q5I7T1; -.
DR PeptideAtlas; Q5I7T1; -.
DR PRIDE; Q5I7T1; -.
DR ProteomicsDB; 62974; -.
DR Antibodypedia; 55463; 74 antibodies from 13 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 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; 476469at2759; -.
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; 115 hits in 1010 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 157 other tissues.
DR ExpressionAtlas; Q5I7T1; baseline and differential.
DR Genevisible; Q5I7T1; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
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; 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; 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..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 some patients with drug-induced cardiac
FT repolarization defects; exerts a greater protective effect,
FT relative to wild-type, against drug blockage of KCNH2
FT potassium channel; 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
