ALG6_MOUSE
ID ALG6_MOUSE Reviewed; 507 AA.
AC Q3TAE8; Q3TZF4;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase;
DE EC=2.4.1.267;
DE AltName: Full=Asparagine-linked glycosylation protein 6 homolog;
DE AltName: Full=Dol-P-Glc:Man(9)GlcNAc(2)-PP-Dol alpha-1,3-glucosyltransferase;
DE AltName: Full=Dolichyl-P-Glc:Man9GlcNAc2-PP-dolichyl glucosyltransferase;
GN Name=Alg6;
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=NOD; TISSUE=Spleen;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
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).
CC -!- FUNCTION: Adds the first 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 Man(9)GlcNAc(2)-PP-Dol (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-glucosyl phosphate + alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-
CC (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-
CC diphosphodolichol = a dolichyl phosphate + alpha-D-Glc-(1->3)-alpha-
CC D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC (1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-
CC alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-
CC GlcNAc-diphosphodolichol + H(+); Xref=Rhea:RHEA:30635, Rhea:RHEA-
CC COMP:9517, Rhea:RHEA-COMP:9528, Rhea:RHEA-COMP:12631, Rhea:RHEA-
CC COMP:12632, ChEBI:CHEBI:15378, ChEBI:CHEBI:57525, ChEBI:CHEBI:57683,
CC ChEBI:CHEBI:132520, ChEBI:CHEBI:132521; EC=2.4.1.267;
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ALG6/ALG8 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; AK157903; BAE34254.1; -; mRNA.
DR EMBL; AK171887; BAE42720.1; -; mRNA.
DR EMBL; BX005053; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050854; AAH50854.1; -; mRNA.
DR CCDS; CCDS38818.1; -.
DR RefSeq; NP_001074733.1; NM_001081264.1.
DR AlphaFoldDB; Q3TAE8; -.
DR SMR; Q3TAE8; -.
DR BioGRID; 236020; 1.
DR STRING; 10090.ENSMUSP00000095574; -.
DR CAZy; GT57; Glycosyltransferase Family 57.
DR PhosphoSitePlus; Q3TAE8; -.
DR MaxQB; Q3TAE8; -.
DR PaxDb; Q3TAE8; -.
DR PeptideAtlas; Q3TAE8; -.
DR PRIDE; Q3TAE8; -.
DR ProteomicsDB; 296223; -.
DR Antibodypedia; 33348; 111 antibodies from 23 providers.
DR Ensembl; ENSMUST00000097961; ENSMUSP00000095574; ENSMUSG00000073792.
DR GeneID; 320438; -.
DR KEGG; mmu:320438; -.
DR UCSC; uc008tuw.1; mouse.
DR CTD; 29929; -.
DR MGI; MGI:2444031; Alg6.
DR VEuPathDB; HostDB:ENSMUSG00000073792; -.
DR eggNOG; KOG2575; Eukaryota.
DR GeneTree; ENSGT00940000153733; -.
DR HOGENOM; CLU_008110_3_0_1; -.
DR InParanoid; Q3TAE8; -.
DR OMA; RQWYFNT; -.
DR OrthoDB; 595382at2759; -.
DR PhylomeDB; Q3TAE8; -.
DR TreeFam; TF314522; -.
DR Reactome; R-MMU-446193; Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 320438; 17 hits in 75 CRISPR screens.
DR PRO; PR:Q3TAE8; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q3TAE8; protein.
DR Bgee; ENSMUSG00000073792; Expressed in yolk sac and 61 other tissues.
DR ExpressionAtlas; Q3TAE8; baseline and differential.
DR Genevisible; Q3TAE8; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042281; F:dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0046527; F:glucosyltransferase activity; ISO:MGI.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:InterPro.
DR GO; GO:0006490; P:oligosaccharide-lipid intermediate biosynthetic process; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISO:MGI.
DR InterPro; IPR039488; ALG6.
DR InterPro; IPR004856; Glyco_trans_ALG6/ALG8.
DR PANTHER; PTHR12413; PTHR12413; 1.
DR PANTHER; PTHR12413:SF1; PTHR12413:SF1; 1.
DR Pfam; PF03155; Alg6_Alg8; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycosyltransferase; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..507
FT /note="Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-
FT glucosyltransferase"
FT /id="PRO_0000284132"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 442
FT /note="L -> F (in Ref. 1; BAE34254)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 507 AA; 57874 MW; 55D661178739A2CF CRC64;
MESWPWMAVV VLLGLTVRWT VSLSSYSGAG KPPMFGDYEA QRHWQEITLN LPVKQWYFNS
SDNNLLYWGL DYPPLTAYHS LLCAYVAKFI NPDWVALHTS RGYESQAHKL FMRATVLAAD
LLIYVPAVLL YCYSLKEISP KRKIASALCI LLYPGLILID YGHFQYNSVS LGFALWGVLG
VSWDWDLLGS LAFCLALNYK QMELYHSLPF FCFLLGKCFK KGLKGKGLAL FIRIACTVLA
SFLLCWLPFL TEREHALQVV RRLFPVDRGL FEDKVANIWC SVNVFLKIKD TLPRHIQIAI
SFCFTLLSLL PACIKLTVRP SCKGFRFTLV SCALSFFLFS FQVHEKSILL VSLPVCLVLT
EIPFMSTWFL LVSTFSMLPL LLKDELLLPS VVTVMAFVIA CGTFFPMLEN TSEEQLQLKS
FAVSVRRHLP GFTFLPRIMQ CLFLSSVITM VLLTILSVTL DPPQKLPDLF PVLICFVSCV
NFVFFLVYFN IVIMWDSKNG RNRKKIE
