ID   DPM1_PIG                Reviewed;         259 AA.
AC   A5GFZ5;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Porcine genome sequencing project;
RL   Submitted (MAY-2007) 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; CR974565; CAN13124.1; -; Genomic_DNA.
DR   EMBL; CT009560; CAN13124.1; JOINED; Genomic_DNA.
DR   EMBL; CT009560; CAN13232.1; -; Genomic_DNA.
DR   EMBL; CR974565; CAN13232.1; JOINED; Genomic_DNA.
DR   RefSeq; NP_001095290.1; NM_001101820.1.
DR   AlphaFoldDB; A5GFZ5; -.
DR   SMR; A5GFZ5; -.
DR   STRING; 9823.ENSSSCP00000007962; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   PaxDb; A5GFZ5; -.
DR   PeptideAtlas; A5GFZ5; -.
DR   PRIDE; A5GFZ5; -.
DR   Ensembl; ENSSSCT00000040191; ENSSSCP00000055745; ENSSSCG00000034952.
DR   Ensembl; ENSSSCT00030000904; ENSSSCP00030000418; ENSSSCG00030000666.
DR   Ensembl; ENSSSCT00040054399; ENSSSCP00040022624; ENSSSCG00040040479.
DR   Ensembl; ENSSSCT00045044744; ENSSSCP00045031038; ENSSSCG00045026265.
DR   Ensembl; ENSSSCT00055054008; ENSSSCP00055043097; ENSSSCG00055027297.
DR   Ensembl; ENSSSCT00070035138; ENSSSCP00070029347; ENSSSCG00070017800.
DR   GeneID; 100124379; -.
DR   KEGG; ssc:100124379; -.
DR   CTD; 8813; -.
DR   VGNC; VGNC:96235; DPM1.
DR   eggNOG; KOG2978; Eukaryota.
DR   GeneTree; ENSGT00940000153481; -.
DR   InParanoid; A5GFZ5; -.
DR   OMA; TAYIHGF; -.
DR   OrthoDB; 1445102at2759; -.
DR   TreeFam; TF105617; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000008227; Chromosome 17.
DR   Proteomes; UP000314985; Chromosome 17.
DR   Bgee; ENSSSCG00000034952; Expressed in Ammon's horn and 44 other tissues.
DR   ExpressionAtlas; A5GFZ5; baseline and differential.
DR   Genevisible; A5GFZ5; SS.
DR   GO; GO:0033185; C:dolichol-phosphate-mannose synthase complex; IEA:Ensembl.
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:0019348; P:dolichol metabolic process; IBA:GO_Central.
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   3: Inferred from homology;
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..259
FT                   /note="Dolichol-phosphate mannosyltransferase subunit 1"
FT                   /id="PRO_0000296396"
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   259 AA;  29471 MW;  01E6C2B72CF32B68 CRC64;
     MASEEASRNS RSRWEPEGRF PRQDKYSVLL PTYNERENLP LIVWLLVKSF SESGINYEII
     IIDDGSPDGT RDIAEQLVKI YGSDKILLRP REKKLGLGTA YIHGMKHATG NYIIIMDADL
     SHHPKFIPEF IRKQKEGNFD IVSGTRYKGN GGVYGWDLKR KIISRGANFI TQILLRPGAS
     DLTGSFRLYR KEVLQKLIEK CVSKGYVFQM EMIVRARQLN YTIGEVPISF VDRVYGESKL
     GGNEIVSFLK GLLTLFATT