ID   ALG5_MOUSE              Reviewed;         324 AA.
AC   Q9DB25;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   02-SEP-2026, entry version 154.
DE   RecName: Full=Dolichyl-phosphate beta-glucosyltransferase {ECO:0000250|UniProtKB:Q9Y673};
DE            Short=DolP-glucosyltransferase {ECO:0000250|UniProtKB:Q9Y673};
DE            EC=2.4.1.117 {ECO:0000250|UniProtKB:Q9Y673};
DE   AltName: Full=Asparagine-linked glycosylation protein 5 homolog {ECO:0000312|MGI:MGI:1913498};
GN   Name=Alg5 {ECO:0000312|MGI:MGI:1913498};
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=Cerebellum;
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 MRNA].
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Heart, Kidney, Liver, and Pancreas;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Dolichyl-phosphate beta-glucosyltransferase that operates in
CC       the biosynthetic pathway of dolichol-linked oligosaccharides, the
CC       glycan precursors employed in protein asparagine (N)-glycosylation. The
CC       assembly of dolichol-linked oligosaccharides begins on the cytosolic
CC       side of the endoplasmic reticulum membrane and finishes in its lumen.
CC       The sequential addition of sugars to dolichol pyrophosphate produces
CC       dolichol-linked oligosaccharides containing fourteen sugars, including
CC       two GlcNAcs, nine mannoses and three glucoses. Once assembled, the
CC       oligosaccharide is transferred from the lipid to nascent proteins by
CC       oligosaccharyltransferases. Dolichyl-phosphate beta-glucosyltransferase
CC       produces dolichyl beta-D-glucosyl phosphate/Dol-P-Glc, the glucose
CC       donor substrate used sequentially by ALG6, ALG8 and ALG10 to add
CC       glucose residues on top of the Man(9)GlcNAc(2)-PP-Dol structure. These
CC       are the three last steps in the biosynthetic pathway of dolichol-linked
CC       oligosaccharides to produce Glc(3)Man(9)GlcNAc(2)-PP-Dol. The enzyme is
CC       most probably active on the cytoplasmic side of the endoplasmic
CC       reticulum while its product Dol-P-Glc is the substrate for ALG6, ALG8
CC       and ALG11 in the lumen of the endoplasmic reticulum.
CC       {ECO:0000250|UniProtKB:Q9Y673}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a di-trans,poly-cis-dolichyl phosphate + UDP-alpha-D-glucose =
CC         a di-trans,poly-cis-dolichyl beta-D-glucosyl phosphate + UDP;
CC         Xref=Rhea:RHEA:15401, Rhea:RHEA-COMP:19498, Rhea:RHEA-COMP:19502,
CC         ChEBI:CHEBI:57525, ChEBI:CHEBI:57683, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:58885; EC=2.4.1.117;
CC         Evidence={ECO:0000250|UniProtKB:Q9Y673};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15402;
CC         Evidence={ECO:0000250|UniProtKB:Q9Y673};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000250|UniProtKB:Q9Y673}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q9Y673}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {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; AK005296; BAB23938.1; -; mRNA.
DR   EMBL; BC027160; AAH27160.1; -; mRNA.
DR   CCDS; CCDS17353.1; -.
DR   RefSeq; NP_079718.1; NM_025442.3.
DR   AlphaFoldDB; Q9DB25; -.
DR   SMR; Q9DB25; -.
DR   BioGRID; 211325; 5.
DR   FunCoup; Q9DB25; 2017.
DR   STRING; 10090.ENSMUSP00000035879; -.
DR   GlyCosmos; Q9DB25; 1 site, No reported glycans.
DR   iPTMnet; Q9DB25; -.
DR   PhosphoSitePlus; Q9DB25; -.
DR   SwissPalm; Q9DB25; -.
DR   REPRODUCTION-2DPAGE; Q9DB25; -.
DR   jPOST; Q9DB25; -.
DR   PaxDb; 10090-ENSMUSP00000035879; -.
DR   ProteomicsDB; 296020; -.
DR   Pumba; Q9DB25; -.
DR   Antibodypedia; 2385; 152 antibodies from 19 providers.
DR   DNASU; 66248; -.
DR   Ensembl; ENSMUST00000044567.4; ENSMUSP00000035879.4; ENSMUSG00000036632.10.
DR   GeneID; 66248; -.
DR   KEGG; mmu:66248; -.
DR   UCSC; uc008pft.1; mouse.
DR   AGR; MGI:1913498; -.
DR   CTD; 29880; -.
DR   MGI; MGI:1913498; Alg5.
DR   VEuPathDB; HostDB:ENSMUSG00000036632; -.
DR   eggNOG; KOG2977; Eukaryota.
DR   GeneTree; ENSGT00940000153481; -.
DR   HOGENOM; CLU_033536_9_1_1; -.
DR   InParanoid; Q9DB25; -.
DR   OMA; HMVNTDA; -.
DR   OrthoDB; 3784at2759; -.
DR   PhylomeDB; Q9DB25; -.
DR   Reactome; R-MMU-480985; Synthesis of dolichyl-phosphate-glucose.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 66248; 17 hits in 79 CRISPR screens.
DR   PRO; PR:Q9DB25; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q9DB25; protein.
DR   Bgee; ENSMUSG00000036632; Expressed in parotid gland and 248 other cell types or tissues.
DR   ExpressionAtlas; Q9DB25; baseline and differential.
DR   GO; GO:0098554; C:cytoplasmic side of endoplasmic reticulum membrane; ISO:GO_Central.
DR   GO; GO:0098556; C:cytoplasmic side of rough endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0004581; F:dolichyl-phosphate beta-glucosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR   GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0006487; P:protein N-linked glycosylation; ISS:UniProtKB.
DR   CDD; cd04188; DPG_synthase; 1.
DR   FunFam; 3.90.550.10:FF:000068; ALG5, dolichyl-phosphate beta-glucosyltransferase; 1.
DR   Gene3D; 3.90.550.10; Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A; 1.
DR   InterPro; IPR035518; DPG_synthase.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR10859:SF91; DOLICHYL-PHOSPHATE BETA-GLUCOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR10859; GLYCOSYL TRANSFERASE; 1.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Glycosyltransferase; Membrane; Reference proteome;
KW   Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..324
FT                   /note="Dolichyl-phosphate beta-glucosyltransferase"
FT                   /id="PRO_0000059099"
FT   TOPO_DOM        1..7
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..324
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   324 AA;  36791 MW;  83203C070D571523 CRC64;
     MATLLLQLLG LGVALAAAAL ILVSIVAFIT ATKMPPCYQH EEEKFFLNAK GQKEALPSIW
     DSPTKQLSVV VPSYNEEKRL PVMMDEALNY LEKRQKHDCT FTYEVIVVDD GSEDQTSKVA
     LKYCQKYGSD KVRVITLVRN RGKGGAVRMG VFSSRGEKIL MADADGATKF PDVEKLEKGL
     SDLQPWPEQM AIACGSRAHL EKESIAQRSY FRTFLMYGFH FLVWFLCVKG IRDTQCGFKL
     LTREAAARTF SSLHIERWAF DVELLYIAQC LQIPIAEVAV NWTEIEGSKL VPFWSWLQMG
     KDLLFIRLRY LTGAWRLKQT RKAS
//