ID   DPM2_CRIGR              Reviewed;          84 AA.
AC   Q9Z1P1;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Dolichol phosphate-mannose biosynthesis regulatory protein {ECO:0000250|UniProtKB:O94777};
DE   AltName: Full=Dolichol-phosphate mannose synthase subunit 2;
DE            Short=DPM synthase subunit 2;
GN   Name=DPM2 {ECO:0000250|UniProtKB:O94777};
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 [GENOMIC DNA], POLYMORPHISM, AND VARIANT GLU-10.
RC   TISSUE=Ovary;
RX   PubMed=14680801; DOI=10.1016/j.bbrc.2003.10.152;
RA   Pu L., Scocca J.R., Walker B.K., Krag S.S.;
RT   "A single point mutation resulting in an adversely reduced expression of
RT   DPM2 in the Lec15.1 cells.";
RL   Biochem. Biophys. Res. Commun. 312:555-561(2003).
CC   -!- FUNCTION: Regulates the biosynthesis of dolichol phosphate-mannose.
CC       Regulatory subunit of the dolichol-phosphate mannose (DPM) synthase
CC       complex; essential for the ER localization and stable expression of
CC       DPM1. Part of the glycosylphosphatidylinositol-N-
CC       acetylglucosaminyltransferase (GPI-GnT) complex that catalyzes the
CC       transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to
CC       phosphatidylinositol and participates in the first step of GPI
CC       biosynthesis. May act by regulating the GPI-GNT complex.
CC       {ECO:0000250|UniProtKB:O94777}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000250|UniProtKB:O94777}.
CC   -!- SUBUNIT: Component of the dolichol-phosphate mannose (DPM) synthase
CC       complex composed of DPM1, DPM2 and DPM3; in the complex interacts
CC       directly with DPM3. Component of the glycosylphosphatidylinositol-N-
CC       acetylglucosaminyltransferase (GPI-GnT) complex composed at least by
CC       PIGA, PIGC, PIGH, PIGP, PIGQ, PIGY and DPM2. Interacts with PIGA, PIGC
CC       and PIGQ. {ECO:0000250|UniProtKB:O94777}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- POLYMORPHISM: The Glu-10 variant in the Lec15.1/B4-2-1 cell line causes
CC       dramatic reduction of DPM2. {ECO:0000269|PubMed:14680801}.
CC   -!- SIMILARITY: Belongs to the DPM2 family. {ECO:0000305}.
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DR   EMBL; AF115410; AAD04344.1; -; mRNA.
DR   EMBL; AF155144; AAD38194.1; -; Genomic_DNA.
DR   RefSeq; NP_001231464.1; NM_001244535.1.
DR   AlphaFoldDB; Q9Z1P1; -.
DR   SMR; Q9Z1P1; -.
DR   STRING; 10029.NP_001231464.1; -.
DR   Ensembl; ENSCGRT00001008542; ENSCGRP00001005539; ENSCGRG00001007301.
DR   GeneID; 100689294; -.
DR   KEGG; cge:100689294; -.
DR   CTD; 8818; -.
DR   eggNOG; KOG3488; Eukaryota.
DR   GeneTree; ENSGT00390000001098; -.
DR   OMA; YVMLKSQ; -.
DR   OrthoDB; 1605216at2759; -.
DR   UniPathway; UPA00378; -.
DR   GO; GO:0000506; C:glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex; ISS:UniProtKB.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:InterPro.
DR   GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR   GO; GO:0019348; P:dolichol metabolic process; IEA:InterPro.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR009914; DPM2.
DR   PANTHER; PTHR15039; PTHR15039; 1.
DR   Pfam; PF07297; DPM2; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..84
FT                   /note="Dolichol phosphate-mannose biosynthesis regulatory
FT                   protein"
FT                   /id="PRO_0000220872"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   VARIANT         10
FT                   /note="G -> E (in Lec15.1/B4-2-1 cell line)"
FT                   /evidence="ECO:0000269|PubMed:14680801"
SQ   SEQUENCE   84 AA;  9491 MW;  23CBBAD7639E4F25 CRC64;
     MATGTDQVVG FGLVAVSLII FTYYTTWVIL LPFIDSQHVI HKYFLPRAYA VLIPLATGLL
     LLLFVGLFIT YVMLKSRRLT KKAQ