ID   DPM2_RAT                Reviewed;          84 AA.
AC   Q9Z325;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Dolichol phosphate-mannose biosynthesis regulatory protein {ECO:0000305};
DE   AltName: Full=Dolichol-phosphate mannose synthase subunit 2;
DE            Short=DPM synthase subunit 2;
GN   Name=Dpm2 {ECO:0000312|RGD:2514};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION
RP   WITH DPM1, AND MUTAGENESIS OF PHE-21 AND TYR-23.
RX   PubMed=9724629; DOI=10.1093/emboj/17.17.4920;
RA   Maeda Y., Tomita S., Watanabe R., Ohishi K., Kinoshita T.;
RT   "DPM2 regulates biosynthesis of dolichol phosphate-mannose in mammalian
RT   cells: correct subcellular localization and stabilization of DPM1, and
RT   binding of dolichol phosphate.";
RL   EMBO J. 17:4920-4929(1998).
CC   -!- FUNCTION: Regulates the biosynthesis of dolichol phosphate-mannose
CC       (PubMed:9724629). Regulatory subunit of the dolichol-phosphate mannose
CC       (DPM) synthase complex; essential for the ER localization and stable
CC       expression of DPM1 (PubMed:9724629). Part of the
CC       glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT)
CC       complex that catalyzes the transfer of N-acetylglucosamine from UDP-N-
CC       acetylglucosamine to phosphatidylinositol and participates in the first
CC       step of GPI biosynthesis. May act by regulating the GPI-GNT complex (By
CC       similarity). {ECO:0000250|UniProtKB:O94777,
CC       ECO:0000269|PubMed:9724629}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000269|PubMed:9724629}.
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 (PubMed:9724629). Component of the
CC       glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT)
CC       complex composed at least by PIGA, PIGC, PIGH, PIGP, PIGQ, PIGY and
CC       DPM2. Interacts with PIGA, PIGC and PIGQ (By similarity).
CC       {ECO:0000250|UniProtKB:O94777, ECO:0000269|PubMed:9724629}.
CC   -!- INTERACTION:
CC       Q9Z325; Q9P2X0: DPM3; Xeno; NbExp=2; IntAct=EBI-9097185, EBI-9087337;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:9724629}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:9724629}.
CC   -!- SIMILARITY: Belongs to the DPM2 family. {ECO:0000305}.
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DR   EMBL; AB013359; BAA33972.1; -; mRNA.
DR   RefSeq; NP_062125.1; NM_019252.1.
DR   AlphaFoldDB; Q9Z325; -.
DR   IntAct; Q9Z325; 1.
DR   STRING; 10116.ENSRNOP00000065111; -.
DR   PaxDb; Q9Z325; -.
DR   GeneID; 29640; -.
DR   KEGG; rno:29640; -.
DR   CTD; 8818; -.
DR   RGD; 2514; Dpm2.
DR   eggNOG; KOG3488; Eukaryota.
DR   InParanoid; Q9Z325; -.
DR   OrthoDB; 1605216at2759; -.
DR   PhylomeDB; Q9Z325; -.
DR   Reactome; R-RNO-162699; Synthesis of dolichyl-phosphate mannose.
DR   Reactome; R-RNO-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR   UniPathway; UPA00378; -.
DR   PRO; PR:Q9Z325; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0033185; C:dolichol-phosphate-mannose synthase complex; IDA:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
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:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR   GO; GO:0004582; F:dolichyl-phosphate beta-D-mannosyltransferase activity; IDA:MGI.
DR   GO; GO:0008047; F:enzyme activator activity; ISO:RGD.
DR   GO; GO:0030234; F:enzyme regulator activity; IDA:RGD.
DR   GO; GO:0019348; P:dolichol metabolic process; IDA:MGI.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IDA:MGI.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   GO; GO:0031647; P:regulation of protein stability; ISO:RGD.
DR   InterPro; IPR009914; DPM2.
DR   PANTHER; PTHR15039; PTHR15039; 1.
DR   Pfam; PF07297; DPM2; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..84
FT                   /note="Dolichol phosphate-mannose biosynthesis regulatory
FT                   protein"
FT                   /id="PRO_0000220875"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         21
FT                   /note="F->L: Abolishes interaction with DPM1; when
FT                   associated with S-23."
FT                   /evidence="ECO:0000269|PubMed:9724629"
FT   MUTAGEN         23
FT                   /note="Y->S: Abolishes interaction with DPM1; when
FT                   associated with L-21."
FT                   /evidence="ECO:0000269|PubMed:9724629"
SQ   SEQUENCE   84 AA;  9344 MW;  345C9AC265573300 CRC64;
     MATGTDQAVG FGLVAVSLII FTYYTTWVIL LPFIDSQHVI HKYFLPRAYA VLLPLAAGLL
     LLLFVGLFIT YVLLKSQKVT KKAQ