DPM1_SCHPO
ID DPM1_SCHPO Reviewed; 236 AA.
AC O14466;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Dolichol-phosphate mannosyltransferase;
DE EC=2.4.1.83;
DE AltName: Full=Dolichol-phosphate mannose synthase;
DE Short=DPM synthase;
DE AltName: Full=Dolichyl-phosphate beta-D-mannosyltransferase;
DE AltName: Full=Mannose-P-dolichol synthase;
DE Short=MPD synthase;
GN Name=dpm1; ORFNames=SPAC31G5.16c;
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 [MRNA].
RX PubMed=9223280; DOI=10.1073/pnas.94.15.7873;
RA Colussi P.A., Taron C.H., Mack J.C., Orlean P.;
RT "Human and Saccharomyces cerevisiae dolichol phosphate mannose synthases
RT represent two classes of the enzyme, but both function in
RT Schizosaccharomyces pombe.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:7873-7878(1997).
RN [2]
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).
CC -!- FUNCTION: Transfers mannose from GDP-mannose to dolichol monophosphate
CC to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl
CC donor in pathways leading to N-glycosylation, glycosyl
CC phosphatidylinositol membrane anchoring, and O-mannosylation of
CC proteins.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl phosphate + GDP-alpha-D-mannose = a dolichyl beta-
CC D-mannosyl phosphate + GDP; Xref=Rhea:RHEA:21184, Rhea:RHEA-
CC COMP:9517, Rhea:RHEA-COMP:9527, ChEBI:CHEBI:57527, ChEBI:CHEBI:57683,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:58211; EC=2.4.1.83;
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; AF007873; AAC98795.1; -; mRNA.
DR EMBL; CU329670; CAB11700.1; -; Genomic_DNA.
DR PIR; T38633; T38633.
DR RefSeq; NP_594017.1; NM_001019443.2.
DR AlphaFoldDB; O14466; -.
DR SMR; O14466; -.
DR BioGRID; 279553; 2.
DR STRING; 4896.SPAC31G5.16c.1; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR iPTMnet; O14466; -.
DR MaxQB; O14466; -.
DR PaxDb; O14466; -.
DR PRIDE; O14466; -.
DR EnsemblFungi; SPAC31G5.16c.1; SPAC31G5.16c.1:pep; SPAC31G5.16c.
DR GeneID; 2543121; -.
DR KEGG; spo:SPAC31G5.16c; -.
DR PomBase; SPAC31G5.16c; dpm1.
DR VEuPathDB; FungiDB:SPAC31G5.16c; -.
DR eggNOG; KOG2978; Eukaryota.
DR HOGENOM; CLU_033536_13_3_1; -.
DR InParanoid; O14466; -.
DR OMA; TAYIHGF; -.
DR PhylomeDB; O14466; -.
DR Reactome; R-SPO-162699; Synthesis of dolichyl-phosphate mannose.
DR UniPathway; UPA00378; -.
DR PRO; PR:O14466; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0033185; C:dolichol-phosphate-mannose synthase complex; ISO:PomBase.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:PomBase.
DR GO; GO:0004582; F:dolichyl-phosphate beta-D-mannosyltransferase activity; ISO:PomBase.
DR GO; GO:0019348; P:dolichol metabolic process; IBA:GO_Central.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; ISO:PomBase.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; ISO:PomBase.
DR GO; GO:0006493; P:protein O-linked glycosylation; IC:PomBase.
DR GO; GO:0035269; P:protein O-linked mannosylation; IBA:GO_Central.
DR CDD; cd06442; DPM1_like; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR039528; DPM1-like.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR43398; PTHR43398; 1.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycosyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..236
FT /note="Dolichol-phosphate mannosyltransferase"
FT /id="PRO_0000059173"
SQ SEQUENCE 236 AA; 26672 MW; ECDB1DE892C1795E CRC64;
MSKYSVLLPT YNERKNLPII TYLIAKTFDQ EKLDWEIVII DDASPDGTQE VAKELQKIYG
EDKILLKPRS GKLGLGTAYI HGLKFATGDF VIIMDADFSH HPKYLPEFIK LQKEHNYDIV
LGTRYAKDGG VYGWNLKRKF ISRGANLLAS TVLGTGVSDV TGSFRLYKKP VLETLMSEVT
SKGYVFQMEI IARAREHNYT IGEVPIAFVD RLYGESKLGM DDILGYLKGV FSLLFI
