ID   ALG5_SCHPO              Reviewed;         322 AA.
AC   O60061;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 122.
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;
GN   Name=alg5; ORFNames=SPBC56F2.10c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
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
CC       {ECO:0000269|PubMed:16823372}; Single-pass type II membrane protein
CC       {ECO:0000269|PubMed:16823372}. Note=Its interaction with the substrate
CC       UDP-glucose may occur at the cytoplasmic side of the ER, whereas the
CC       steps utilizing dolichyl beta-D-glucosyl phosphate take place in the
CC       lumen of the ER. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR   EMBL; CU329671; CAA18889.1; -; Genomic_DNA.
DR   PIR; T40534; T40534.
DR   RefSeq; NP_596707.1; NM_001022632.2.
DR   AlphaFoldDB; O60061; -.
DR   SMR; O60061; -.
DR   BioGRID; 277568; 57.
DR   STRING; 4896.SPBC56F2.10c.1; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   MaxQB; O60061; -.
DR   PaxDb; O60061; -.
DR   EnsemblFungi; SPBC56F2.10c.1; SPBC56F2.10c.1:pep; SPBC56F2.10c.
DR   GeneID; 2541053; -.
DR   KEGG; spo:SPBC56F2.10c; -.
DR   PomBase; SPBC56F2.10c; alg5.
DR   VEuPathDB; FungiDB:SPBC56F2.10c; -.
DR   eggNOG; KOG2977; Eukaryota.
DR   HOGENOM; CLU_033536_9_1_1; -.
DR   InParanoid; O60061; -.
DR   OMA; MVNTDAV; -.
DR   PhylomeDB; O60061; -.
DR   Reactome; R-SPO-480985; Synthesis of dolichyl-phosphate-glucose.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:O60061; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; EXP:PomBase.
DR   GO; GO:0004581; F:dolichyl-phosphate beta-glucosyltransferase activity; IDA:PomBase.
DR   GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IMP:PomBase.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR   GO; GO:0018279; P:protein N-linked glycosylation via asparagine; EXP:PomBase.
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   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..322
FT                   /note="Dolichyl-phosphate beta-glucosyltransferase"
FT                   /id="PRO_0000311759"
FT   TOPO_DOM        1
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        2..22
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT   TOPO_DOM        23..322
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        72
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        307
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   322 AA;  36774 MW;  B97B2EF2C8D872C0 CRC64;
     MVVYIVLYTC LAGFILLFLV YYYLTHSHCP RKQLEGEETC VFIENGQKKS LTLEKWSTSD
     NIQITVIVPA YNESKRIGNM LQETVDHLEK YYRSSSSAGQ RRWEILIVDD ESKDTTVNAV
     LEFSNKLDLR DHLRVCSLKR NRGKGGAVTW GMLYARGQYA IFADADGASQ FSDLELLFKN
     MPPGPRGGVV VGSRAHMVNT AAVVKRSFIR NFLMHCFHKL LQILGIREIG DTQCGFKLFS
     REAYQSIFPR MHVEGWIFDI EVLTLARFFG LPIIEVPITW HEVGGSKMTL LKDSISMAID
     LLVIRLNYTF GIWERPSAKR IT