DPM1_USTMA
ID DPM1_USTMA Reviewed; 294 AA.
AC P54856; A0A0D1CUY2; Q4P0N4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 117.
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=UMAG_06329;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=H-156S;
RX PubMed=8813763;
RX DOI=10.1002/(sici)1097-0061(19960630)12:8<765::aid-yea974>3.0.co;2-a;
RA Zimmerman J.W., Specht C.A., Cazares B.X., Robbins P.W.;
RT "The isolation of a Dol-P-Man synthase from Ustilago maydis that functions
RT in Saccharomyces cerevisiae.";
RL Yeast 12:765-771(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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 membrane {ECO:0000305};
CC Single-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; U54797; AAC49401.1; -; Genomic_DNA.
DR EMBL; CM003143; KIS70243.1; -; Genomic_DNA.
DR PIR; S71642; S71642.
DR RefSeq; XP_011388316.1; XM_011390014.1.
DR AlphaFoldDB; P54856; -.
DR SMR; P54856; -.
DR STRING; 5270.UM06329P0; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR EnsemblFungi; KIS70243; KIS70243; UMAG_06329.
DR GeneID; 23565949; -.
DR KEGG; uma:UMAG_06329; -.
DR VEuPathDB; FungiDB:UMAG_06329; -.
DR eggNOG; KOG2978; Eukaryota.
DR HOGENOM; CLU_033536_13_1_1; -.
DR InParanoid; P54856; -.
DR OMA; FQVEMNY; -.
DR OrthoDB; 1445102at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000000561; Chromosome 4.
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:0004582; F:dolichyl-phosphate beta-D-mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0019348; P:dolichol metabolic process; IBA:GO_Central.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
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 3: Inferred from homology;
KW Endoplasmic reticulum; Glycosyltransferase; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..294
FT /note="Dolichol-phosphate mannosyltransferase"
FT /id="PRO_0000059174"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 97
FT /note="R -> A (in Ref. 1; AAC49401)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 294 AA; 32181 MW; 1C9663A89D3D28BB CRC64;
MSIALDMDAS AKMRKQPGSS GWSTSSTPSC SVIVPAFREN LNLRPLVTRL SSAFASQSSS
ELANTEIIIV DDNSRDGSVE TVSALQSEGY NVRIIVRTSE RGLSSAVVRG FREARGQRMI
CMDADLQHPP EAVPSLLLAL NGQKSFVLGT RYGVGVSMDK DWPLHRRIIS SGARMLARPL
TSASDPMSGF FGITKHSFHT ADHHINAQGF KIALDLLVKS GVHSTDIAEV PFSFGLRQEG
ESKLDGKVMF KYLQQLVELY RFRFGTVPIV FVLIVLLVLA LYIWSHVLAP MLGA
