DPM2_BOVIN
ID DPM2_BOVIN Reviewed; 84 AA.
AC Q2KIN1;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 69.
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 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=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the DPM2 family. {ECO:0000305}.
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DR EMBL; BC112577; AAI12578.1; -; mRNA.
DR RefSeq; NP_001039733.1; NM_001046268.2.
DR AlphaFoldDB; Q2KIN1; -.
DR SMR; Q2KIN1; -.
DR STRING; 9913.ENSBTAP00000004393; -.
DR PaxDb; Q2KIN1; -.
DR GeneID; 523737; -.
DR KEGG; bta:523737; -.
DR CTD; 8818; -.
DR eggNOG; KOG3488; Eukaryota.
DR InParanoid; Q2KIN1; -.
DR OrthoDB; 1605216at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000009136; Unplaced.
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; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..84
FT /note="Dolichol phosphate-mannose biosynthesis regulatory
FT protein"
FT /id="PRO_0000240350"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 84 AA; 9395 MW; 024A9E4BBF9C8872 CRC64;
MATGTDQVVG LGLVALSLII FTYYTAWVIL LPFIDSQHVI HKYFLPRAYA IAIPLAAGHL
LLLFVGIFIT YVMLKNQNDT KKTQ
