ID   DPM1_BOVIN              Reviewed;         260 AA.
AC   Q1JQ93;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 73.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAY-2006) 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; BC116151; AAI16152.1; -; mRNA.
DR   RefSeq; NP_001069481.1; NM_001076013.2.
DR   AlphaFoldDB; Q1JQ93; -.
DR   SMR; Q1JQ93; -.
DR   STRING; 9913.ENSBTAP00000010153; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   iPTMnet; Q1JQ93; -.
DR   PaxDb; Q1JQ93; -.
DR   GeneID; 534097; -.
DR   KEGG; bta:534097; -.
DR   CTD; 8813; -.
DR   eggNOG; KOG2978; Eukaryota.
DR   InParanoid; Q1JQ93; -.
DR   OrthoDB; 1445102at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0004582; F:dolichyl-phosphate beta-D-mannosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0035268; P:protein mannosylation; ISS:UniProtKB.
DR   GO; GO:0035269; P:protein O-linked mannosylation; ISS:UniProtKB.
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   Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O60762"
FT   CHAIN           2..260
FT                   /note="Dolichol-phosphate mannosyltransferase subunit 1"
FT                   /id="PRO_0000282826"
FT   REGION          1..20
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         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60762"
SQ   SEQUENCE   260 AA;  29592 MW;  16AF1CEE3D474801 CRC64;
     MAAEEASRSS PRFRREPKGR VSRQDKYSVL LPTYNERENL PFIVWLLVKS FSESGFNYEI
     IIIDDGSPDG TRDVAEQLEK IYGSDRILLR PREKKLGLGT AYIHGMKHAT GNYIIIMDAD
     LSHHPKFIPE FIRKQKEGNF DIVSGTRYKG NGGVYGWDLK RKIISRVANF ITQILLRPGA
     SDLTGSFRLY RKEVLQKLIG KCISKGYVFQ MEMIVRARQL NYTIGEVPIS FVDRVYGESK
     LGGNEIVSFL KGLLTLFATT