DPM1_YEAST
ID DPM1_YEAST Reviewed; 267 AA.
AC P14020; D6W4I3;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Dolichol-phosphate mannosyltransferase;
DE EC=2.4.1.83 {ECO:0000269|PubMed:15548536, ECO:0000269|PubMed:3053713};
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; Synonyms=SED3; OrderedLocusNames=YPR183W; ORFNames=P9705.3;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=3053713; DOI=10.1016/s0021-9258(19)77863-6;
RA Orlean P., Albright C., Robbins P.W.;
RT "Cloning and sequencing of the yeast gene for dolichol phosphate mannose
RT synthase, an essential protein.";
RL J. Biol. Chem. 263:17499-17507(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP PROTEIN SEQUENCE OF 2-65; 88-137; 150-166; 184-191; 200-212 AND 223-232,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RA Bienvenut W.V., Peters C.;
RL Submitted (MAY-2005) to UniProtKB.
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP INTERACTION WITH SAC1, AND SUBCELLULAR LOCATION.
RX PubMed=15657391; DOI=10.1083/jcb.200407118;
RA Faulhammer F., Konrad G., Brankatschk B., Tahirovic S., Knoedler A.,
RA Mayinger P.;
RT "Cell growth-dependent coordination of lipid signaling and glycosylation is
RT mediated by interactions between Sac1p and Dpm1p.";
RL J. Cell Biol. 168:185-191(2005).
RN [8]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PHOSPHORYLATION AT
RP SER-141 BY PKA, AND MUTAGENESIS OF SER-141.
RX PubMed=15548536; DOI=10.1074/jbc.m406962200;
RA Banerjee D.K., Carrasquillo E.A., Hughey P., Schutzbach J.S.,
RA Martinez J.A., Baksi K.;
RT "In vitro phosphorylation by cAMP-dependent protein kinase up-regulates
RT recombinant Saccharomyces cerevisiae mannosylphosphodolichol synthase.";
RL J. Biol. Chem. 280:4174-4181(2005).
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. {ECO:0000269|PubMed:3053713}.
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 Evidence={ECO:0000269|PubMed:15548536, ECO:0000269|PubMed:3053713};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21185;
CC Evidence={ECO:0000269|PubMed:3053713};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.2 uM for GDP-mannose {ECO:0000269|PubMed:15548536};
CC Vmax=25.1 nmol/min/mg enzyme for GDP-mannose
CC {ECO:0000269|PubMed:15548536};
CC Note=For the phosphorylated protein, the Vmax increases to 146.7
CC nmol/min/mg enzyme, whereas the KM stays at 1.1 uM for GDP-mannose,
CC increasing the catalytic efficiency 6-fold.
CC {ECO:0000269|PubMed:15548536};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000305|PubMed:3053713}.
CC -!- SUBUNIT: Interacts with the C-terminus of SAC1, thereby sequestering it
CC to the endoplasmic reticulum in exponentially growing cells. Under
CC nutrient limitation conditions, this interaction is rapidly abolished.
CC {ECO:0000269|PubMed:15657391}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15657391}; Single-pass
CC type IV membrane protein {ECO:0000269|PubMed:15657391}; Cytoplasmic
CC side {ECO:0000269|PubMed:15657391}.
CC -!- MISCELLANEOUS: Present with 1885 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; J04184; AAA34578.1; -; Genomic_DNA.
DR EMBL; U25842; AAB68116.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11599.1; -; Genomic_DNA.
DR PIR; A32122; A32122.
DR RefSeq; NP_015509.1; NM_001184280.1.
DR AlphaFoldDB; P14020; -.
DR SMR; P14020; -.
DR BioGRID; 36355; 489.
DR DIP; DIP-4087N; -.
DR IntAct; P14020; 15.
DR MINT; P14020; -.
DR STRING; 4932.YPR183W; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR iPTMnet; P14020; -.
DR MaxQB; P14020; -.
DR PaxDb; P14020; -.
DR PRIDE; P14020; -.
DR EnsemblFungi; YPR183W_mRNA; YPR183W; YPR183W.
DR GeneID; 856313; -.
DR KEGG; sce:YPR183W; -.
DR SGD; S000006387; DPM1.
DR VEuPathDB; FungiDB:YPR183W; -.
DR eggNOG; KOG2978; Eukaryota.
DR GeneTree; ENSGT00940000153481; -.
DR HOGENOM; CLU_033536_13_1_1; -.
DR InParanoid; P14020; -.
DR OMA; FQVEMNY; -.
DR BioCyc; MetaCyc:YPR183W-MON; -.
DR BioCyc; YEAST:YPR183W-MON; -.
DR BRENDA; 2.4.1.83; 984.
DR SABIO-RK; P14020; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:P14020; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P14020; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
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:0005741; C:mitochondrial outer membrane; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0042175; C:nuclear outer membrane-endoplasmic reticulum membrane network; IDA:SGD.
DR GO; GO:0004582; F:dolichyl-phosphate beta-D-mannosyltransferase activity; IDA:SGD.
DR GO; GO:0019348; P:dolichol metabolic process; IBA:GO_Central.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IMP:SGD.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IMP:SGD.
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 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Endoplasmic reticulum;
KW Glycosyltransferase; Membrane; Phosphoprotein; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 2..267
FT /note="Dolichol-phosphate mannosyltransferase"
FT /id="PRO_0000059175"
FT TOPO_DOM 2..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..267
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.4"
FT MOD_RES 141
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:15548536"
FT MUTAGEN 141
FT /note="S->A: Reduces specific activity 2-fold."
FT /evidence="ECO:0000269|PubMed:15548536"
SQ SEQUENCE 267 AA; 30362 MW; 14F2F59F7B6A391A CRC64;
MSIEYSVIVP AYHEKLNIKP LTTRLFAGMS PEMAKKTELI FVDDNSQDGS VEEVDALAHQ
GYNVRIIVRT NERGLSSAVL KGFYEAKGQY LVCMDADLQH PPETVPKLFE SLHDHAFTLG
TRYAPGVGID KDWPMYRRVI SSTARMMARP LTIASDPMSG FFGLQKKYLE NCNPRDINSQ
GFKIALELLA KLPLPRDPRV AIGEVPFTFG VRTEGESKLS GKVIIQYLQQ LKELYVFKFG
ANNLILFITF WSILFFYVCY QLYHLVF
