AG10A_HUMAN
ID AG10A_HUMAN Reviewed; 473 AA.
AC Q5BKT4; Q6NS98; Q96DU0; Q96SM6;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase;
DE EC=2.4.1.256;
DE AltName: Full=Alpha-1,2-glucosyltransferase ALG10-A;
DE AltName: Full=Alpha-2-glucosyltransferase ALG10-A;
DE AltName: Full=Asparagine-linked glycosylation protein 10 homolog A;
GN Name=ALG10; Synonyms=ALG10A;
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].
RC TISSUE=Embryo;
RX PubMed=12200473; DOI=10.1093/oxfordjournals.molbev.a004208;
RA Oriol R., Martinez-Duncker I., Chantret I., Mollicone R., Codogno P.;
RT "Common origin and evolution of glycosyltransferases using Dol-P-
RT monosaccharides as donor substrate.";
RL Mol. Biol. Evol. 19:1451-1463(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Lung;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 149-473.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
CC -!- FUNCTION: Adds the third glucose residue to the lipid-linked
CC oligosaccharide precursor for N-linked glycosylation. Transfers glucose
CC from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked
CC oligosaccharide Glc(2)Man(9)GlcNAc(2)-PP-Dol.
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 -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- INTERACTION:
CC Q5BKT4; P11912: CD79A; NbExp=3; IntAct=EBI-13064220, EBI-7797864;
CC Q5BKT4; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-13064220, EBI-781551;
CC Q5BKT4; P23142-4: FBLN1; NbExp=3; IntAct=EBI-13064220, EBI-11956479;
CC Q5BKT4; Q9BSE4: HERPUD2; NbExp=3; IntAct=EBI-13064220, EBI-2868124;
CC Q5BKT4; Q8N6R1: SERP2; NbExp=3; IntAct=EBI-13064220, EBI-749270;
CC Q5BKT4; Q3SXP7: SHISAL1; NbExp=3; IntAct=EBI-13064220, EBI-18037857;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein.
CC -!- SIMILARITY: Belongs to the ALG10 glucosyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB55272.1; Type=Erroneous initiation; Evidence={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; AJ312278; CAC41349.1; -; mRNA.
DR EMBL; BC070347; AAH70347.1; -; mRNA.
DR EMBL; BC090948; AAH90948.1; -; mRNA.
DR EMBL; AK027657; BAB55272.1; ALT_INIT; mRNA.
DR CCDS; CCDS41769.1; -.
DR RefSeq; NP_116223.3; NM_032834.3.
DR AlphaFoldDB; Q5BKT4; -.
DR BioGRID; 124356; 44.
DR IntAct; Q5BKT4; 20.
DR STRING; 9606.ENSP00000266483; -.
DR CAZy; GT59; Glycosyltransferase Family 59.
DR iPTMnet; Q5BKT4; -.
DR PhosphoSitePlus; Q5BKT4; -.
DR BioMuta; ALG10; -.
DR DMDM; 74736030; -.
DR EPD; Q5BKT4; -.
DR jPOST; Q5BKT4; -.
DR MassIVE; Q5BKT4; -.
DR MaxQB; Q5BKT4; -.
DR PaxDb; Q5BKT4; -.
DR PeptideAtlas; Q5BKT4; -.
DR PRIDE; Q5BKT4; -.
DR ProteomicsDB; 62698; -.
DR Antibodypedia; 55444; 90 antibodies from 18 providers.
DR DNASU; 84920; -.
DR Ensembl; ENST00000266483.7; ENSP00000266483.2; ENSG00000139133.7.
DR GeneID; 84920; -.
DR KEGG; hsa:84920; -.
DR MANE-Select; ENST00000266483.7; ENSP00000266483.2; NM_032834.4; NP_116223.3.
DR UCSC; uc001rlm.4; human.
DR CTD; 84920; -.
DR DisGeNET; 84920; -.
DR GeneCards; ALG10; -.
DR HGNC; HGNC:23162; ALG10.
DR HPA; ENSG00000139133; Low tissue specificity.
DR MIM; 618355; gene.
DR neXtProt; NX_Q5BKT4; -.
DR OpenTargets; ENSG00000139133; -.
DR PharmGKB; PA134732019; -.
DR VEuPathDB; HostDB:ENSG00000139133; -.
DR eggNOG; KOG2642; Eukaryota.
DR GeneTree; ENSGT00390000012906; -.
DR HOGENOM; CLU_017053_1_0_1; -.
DR InParanoid; Q5BKT4; -.
DR OMA; FNCGNLY; -.
DR OrthoDB; 476469at2759; -.
DR PhylomeDB; Q5BKT4; -.
DR TreeFam; TF300150; -.
DR BRENDA; 2.4.1.256; 2681.
DR PathwayCommons; Q5BKT4; -.
DR Reactome; R-HSA-446193; Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
DR SignaLink; Q5BKT4; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 84920; 54 hits in 1005 CRISPR screens.
DR ChiTaRS; ALG10; human.
DR GenomeRNAi; 84920; -.
DR Pharos; Q5BKT4; Tbio.
DR PRO; PR:Q5BKT4; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q5BKT4; protein.
DR Bgee; ENSG00000139133; Expressed in bone marrow cell and 107 other tissues.
DR ExpressionAtlas; Q5BKT4; baseline and differential.
DR Genevisible; Q5BKT4; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0106073; F:dolichyl pyrophosphate Glc2Man9GlcNAc2 alpha-1,2-glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:InterPro.
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 Endoplasmic reticulum; Glycosyltransferase; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..473
FT /note="Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-
FT glucosyltransferase"
FT /id="PRO_0000215447"
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..130
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..175
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..249
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 271..283
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..323
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 345..367
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..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 CONFLICT 184
FT /note="M -> V (in Ref. 2; AAH70347)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="I -> T (in Ref. 1; CAC41349)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="I -> T (in Ref. 3; BAB55272)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 473 AA; 55606 MW; 1860D4E61ACBC2A0 CRC64;
MAQLEGYYFS AALSCTFLVS CLLFSAFSRA LREPYMDEIF HLPQAQRYCE GHFSLSQWDP
MITTLPGLYL VSIGVIKPAI WIFGWSEHVV CSIGMLRFVN LLFSVGNFYL LYLLFCKVQP
RNKAASSIQR VLSTLTLAVF PTLYFFNFLY YTEAGSMFFT LFAYLMCLYG NHKTSAFLGF
CGFMFRQTNI IWAVFCAGNV IAQKLTEAWK TELQKKEDRL PPIKGPFAEF RKILQFLLAY
SMSFKNLSML LLLTWPYILL GFLFCAFVVV NGGIVIGDRS SHEACLHFPQ LFYFFSFTLF
FSFPHLLSPS KIKTFLSLVW KRRILFFVVT LVSVFLVWKF TYAHKYLLAD NRHYTFYVWK
RVFQRYETVK YLLVPAYIFA GWSIADSLKS KSIFWNLMFF ICLFTVIVPQ KLLEFRYFIL
PYVIYRLNIP LPPTSRLICE LSCYAVVNFI TFFIFLNKTF QWPNSQDIQR FMW
