ID   DPM1_CRIGR              Reviewed;         266 AA.
AC   Q9WU83;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Dolichol-phosphate mannosyltransferase subunit 1;
DE            EC=2.4.1.83;
DE   AltName: Full=Dolichol-phosphate mannose synthase subunit 1;
DE            Short=DPM synthase subunit 1;
DE   AltName: Full=Dolichyl-phosphate beta-D-mannosyltransferase subunit 1;
DE   AltName: Full=Mannose-P-dolichol synthase subunit 1;
DE            Short=MPD synthase subunit 1;
GN   Name=DPM1;
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Pu L., Scocca J.R., Walker B.K., Wu J.S., Krag S.S.;
RT   "Mutation in B4-2-1 CHO cells defective in MPD synthase activity.";
RL   Submitted (JAN-1999) 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; catalytic subunit of the dolichol-phosphate mannose (DPM)
CC       synthase complex. {ECO:0000250}.
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   -!- SUBUNIT: Component of the dolichol-phosphate mannose (DPM) synthase
CC       complex composed of DPM1, DPM2 and DPM3; within the complex, directly
CC       interacts with DPM3. This interaction may stabilize DPM1.
CC       {ECO:0000250|UniProtKB:O60762}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR   EMBL; AF121895; AAD30975.1; -; mRNA.
DR   RefSeq; NP_001233614.1; NM_001246685.1.
DR   AlphaFoldDB; Q9WU83; -.
DR   SMR; Q9WU83; -.
DR   STRING; 10029.NP_001233614.1; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   GeneID; 100689420; -.
DR   KEGG; cge:100689420; -.
DR   CTD; 8813; -.
DR   eggNOG; KOG2978; Eukaryota.
DR   OrthoDB; 1445102at2759; -.
DR   UniPathway; UPA00378; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0004582; F:dolichyl-phosphate beta-D-mannosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
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   Acetylation; Endoplasmic reticulum; Glycosyltransferase; Phosphoprotein;
KW   Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O60762"
FT   CHAIN           2..266
FT                   /note="Dolichol-phosphate mannosyltransferase subunit 1"
FT                   /id="PRO_0000059169"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:O60762"
FT   MOD_RES         3
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60762"
SQ   SEQUENCE   266 AA;  29654 MW;  4AFB37EA3AC3329D CRC64;
     MASPGASRGA SAATAAAASP RPPQGRSSRR DKYSVLLPTY NERENLPLIV WLLVKSFSES
     SINYEIIIID DGSPDGTREV AEQLEKIYGP DRILLRPREK KLGLGTAYIH GIKHATGNYV
     IIMDADLSHH PKFIPEFIRK QKEGNFDIVS GTRYKGNGGV YGWDLKRKII SRGANFITQI
     LLRPGASDLT GSFRLYRKEV LQKLIEKCVS KGYVFQMEMI VRARQLNYTI GEVPISFVDR
     VYGESKLGGN EIVSFLKGLL TLFATT