ALG5_MOUSE
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 03-AUG-2022, entry version 138.
DE RecName: Full=Dolichyl-phosphate beta-glucosyltransferase;
DE Short=DolP-glucosyltransferase;
DE EC=2.4.1.117;
DE AltName: Full=Asparagine-linked glycosylation protein 5 homolog;
GN Name=Alg5;
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 -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl phosphate + UDP-alpha-D-glucose = a dolichyl beta-
CC D-glucosyl phosphate + UDP; Xref=Rhea:RHEA:15401, Rhea:RHEA-
CC COMP:9517, Rhea:RHEA-COMP:9528, ChEBI:CHEBI:57525, ChEBI:CHEBI:57683,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.117;
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type II membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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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; 3.
DR STRING; 10090.ENSMUSP00000035879; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR GlyGen; Q9DB25; 1 site.
DR iPTMnet; Q9DB25; -.
DR PhosphoSitePlus; Q9DB25; -.
DR REPRODUCTION-2DPAGE; Q9DB25; -.
DR EPD; Q9DB25; -.
DR jPOST; Q9DB25; -.
DR MaxQB; Q9DB25; -.
DR PaxDb; Q9DB25; -.
DR PRIDE; Q9DB25; -.
DR ProteomicsDB; 296020; -.
DR Antibodypedia; 2385; 154 antibodies from 18 providers.
DR DNASU; 66248; -.
DR Ensembl; ENSMUST00000044567; ENSMUSP00000035879; ENSMUSG00000036632.
DR GeneID; 66248; -.
DR KEGG; mmu:66248; -.
DR UCSC; uc008pft.1; mouse.
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; MVNTDAV; -.
DR OrthoDB; 1107630at2759; -.
DR PhylomeDB; Q9DB25; -.
DR TreeFam; TF314844; -.
DR Reactome; R-MMU-480985; Synthesis of dolichyl-phosphate-glucose.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 66248; 17 hits in 74 CRISPR screens.
DR PRO; PR:Q9DB25; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9DB25; protein.
DR Bgee; ENSMUSG00000036632; Expressed in parotid gland and 245 other tissues.
DR ExpressionAtlas; Q9DB25; baseline and differential.
DR Genevisible; Q9DB25; 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:0004581; F:dolichyl-phosphate beta-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR CDD; cd04188; DPG_synthase; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR035518; DPG_synthase.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..324
FT /note="Dolichyl-phosphate beta-glucosyltransferase"
FT /id="PRO_0000059099"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..324
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
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
