DPM1_MOUSE
ID DPM1_MOUSE Reviewed; 260 AA.
AC O70152; Q9D829;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Dolichol-phosphate mannosyltransferase subunit 1;
DE EC=2.4.1.83 {ECO:0000305|PubMed:9535917};
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;
GN Name=Dpm1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=9535917; DOI=10.1074/jbc.273.15.9249;
RA Tomita S., Inoue N., Maeda Y., Ohishi K., Takeda J., Kinoshita T.;
RT "A homologue of Saccharomyces cerevisiae Dpm1p is not sufficient for
RT synthesis of dolichol-phosphate-mannose in mammalian cells.";
RL J. Biol. Chem. 273:9249-9254(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Lung, and Small intestine;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:0000305|PubMed:9535917}.
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 Evidence={ECO:0000305|PubMed:9535917};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:9535917}.
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.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; AB004789; BAA25759.1; -; mRNA.
DR EMBL; AK005268; BAB23920.1; -; mRNA.
DR EMBL; AK004834; BAB23602.1; -; mRNA.
DR EMBL; AK008548; BAB25735.1; -; mRNA.
DR EMBL; BC061151; AAH61151.1; -; mRNA.
DR CCDS; CCDS17109.1; -.
DR RefSeq; NP_001297013.1; NM_001310084.1.
DR RefSeq; NP_034202.1; NM_010072.4.
DR AlphaFoldDB; O70152; -.
DR SMR; O70152; -.
DR BioGRID; 199298; 5.
DR IntAct; O70152; 1.
DR MINT; O70152; -.
DR STRING; 10090.ENSMUSP00000118776; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR iPTMnet; O70152; -.
DR PhosphoSitePlus; O70152; -.
DR SwissPalm; O70152; -.
DR EPD; O70152; -.
DR jPOST; O70152; -.
DR MaxQB; O70152; -.
DR PaxDb; O70152; -.
DR PeptideAtlas; O70152; -.
DR PRIDE; O70152; -.
DR ProteomicsDB; 279477; -.
DR DNASU; 13480; -.
DR Ensembl; ENSMUST00000138667; ENSMUSP00000139070; ENSMUSG00000093752.
DR Ensembl; ENSMUST00000154111; ENSMUSP00000118776; ENSMUSG00000078919.
DR GeneID; 13480; -.
DR KEGG; mmu:13480; -.
DR UCSC; uc008oas.1; mouse.
DR CTD; 8813; -.
DR MGI; MGI:1330239; Dpm1.
DR VEuPathDB; HostDB:ENSMUSG00000078919; -.
DR VEuPathDB; HostDB:ENSMUSG00000093752; -.
DR eggNOG; KOG2978; Eukaryota.
DR GeneTree; ENSGT00940000153481; -.
DR HOGENOM; CLU_033536_13_3_1; -.
DR InParanoid; O70152; -.
DR OMA; TAYIHGF; -.
DR OrthoDB; 1445102at2759; -.
DR PhylomeDB; O70152; -.
DR TreeFam; TF105617; -.
DR Reactome; R-MMU-162699; Synthesis of dolichyl-phosphate mannose.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 13480; 8 hits in 74 CRISPR screens.
DR PRO; PR:O70152; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; O70152; protein.
DR Bgee; ENSMUSG00000078919; Expressed in spermatocyte and 189 other tissues.
DR ExpressionAtlas; O70152; baseline and differential.
DR Genevisible; O70152; MM.
DR GO; GO:0033185; C:dolichol-phosphate-mannose synthase complex; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:HGNC-UCL.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043178; F:alcohol binding; ISO:MGI.
DR GO; GO:0004582; F:dolichyl-phosphate beta-D-mannosyltransferase activity; IMP:MGI.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; ISS:HGNC-UCL.
DR GO; GO:0005537; F:mannose binding; ISO:MGI.
DR GO; GO:0019348; P:dolichol metabolic process; IMP:MGI.
DR GO; GO:0019673; P:GDP-mannose metabolic process; ISO:MGI.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IMP:MGI.
DR GO; GO:0035268; P:protein mannosylation; ISS:HGNC-UCL.
DR GO; GO:0035269; P:protein O-linked mannosylation; ISS:HGNC-UCL.
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 1: Evidence at protein 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_0000059171"
FT REGION 1..25
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 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60762"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60762"
FT CONFLICT 76
FT /note="E -> G (in Ref. 2; BAB25735)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="S -> Y (in Ref. 2; BAB25735)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 260 AA; 29175 MW; 8CB1BCDF1977EBA6 CRC64;
MASTGASRSL AASPRPPQGR SSRQDKYSVL LPTYNERENL PLIVWLLVKS FSESAINYEI
IIIDDGSPDG TREVAEQLAE IYGPDRILLR PREKKLGLGT AYIHGIKHAT GNYVIIMDAD
LSHHPKFIPE FIRKQKEGNF DIVSGTRYKG NGGVYGWDLK RKIISRGANF ITQILLRPGA
SDLTGSFRLY RKEVLQKLIE KCVSKGYVFQ MEMIVRARQM NYTIGEVPIS FVDRVYGESK
LGGNEIVSFL KGLLTLFATT
