DPM3_MOUSE
ID DPM3_MOUSE Reviewed; 92 AA.
AC Q9D1Q4;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Dolichol-phosphate mannosyltransferase subunit 3;
DE AltName: Full=Dolichol-phosphate mannose synthase subunit 3;
DE Short=DPM synthase subunit 3;
DE AltName: Full=Dolichyl-phosphate beta-D-mannosyltransferase subunit 3;
DE AltName: Full=Mannose-P-dolichol synthase subunit 3;
DE Short=MPD synthase subunit 3;
GN Name=Dpm3;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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: Stabilizer subunit of the dolichol-phosphate mannose (DPM)
CC synthase complex; tethers catalytic subunit DPM1 to the endoplasmic
CC reticulum. {ECO:0000250}.
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, associates
CC with DPM1 via its C-terminal domain and with DPM2 via its N-terminal
CC portion. This interaction stabilizes DPM1 protein.
CC {ECO:0000250|UniProtKB:Q9P2X0}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DPM3 family. {ECO:0000305}.
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DR EMBL; AK003223; BAB22652.1; -; mRNA.
DR EMBL; BC037761; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS38487.1; -.
DR RefSeq; NP_081043.1; NM_026767.4.
DR RefSeq; XP_006502046.1; XM_006501983.1.
DR AlphaFoldDB; Q9D1Q4; -.
DR SMR; Q9D1Q4; -.
DR BioGRID; 212928; 2.
DR STRING; 10090.ENSMUSP00000103086; -.
DR PhosphoSitePlus; Q9D1Q4; -.
DR EPD; Q9D1Q4; -.
DR MaxQB; Q9D1Q4; -.
DR PaxDb; Q9D1Q4; -.
DR PeptideAtlas; Q9D1Q4; -.
DR PRIDE; Q9D1Q4; -.
DR ProteomicsDB; 279765; -.
DR Antibodypedia; 3056; 39 antibodies from 21 providers.
DR Ensembl; ENSMUST00000040824; ENSMUSP00000040860; ENSMUSG00000042737.
DR Ensembl; ENSMUST00000107462; ENSMUSP00000103086; ENSMUSG00000042737.
DR GeneID; 68563; -.
DR KEGG; mmu:68563; -.
DR UCSC; uc008pym.2; mouse.
DR CTD; 54344; -.
DR MGI; MGI:1915813; Dpm3.
DR VEuPathDB; HostDB:ENSMUSG00000042737; -.
DR eggNOG; KOG4841; Eukaryota.
DR GeneTree; ENSGT00390000008892; -.
DR HOGENOM; CLU_150782_0_1_1; -.
DR InParanoid; Q9D1Q4; -.
DR OMA; MTKLMQW; -.
DR OrthoDB; 1612544at2759; -.
DR PhylomeDB; Q9D1Q4; -.
DR TreeFam; TF300274; -.
DR Reactome; R-MMU-162699; Synthesis of dolichyl-phosphate mannose.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 68563; 10 hits in 73 CRISPR screens.
DR ChiTaRS; Dpm3; mouse.
DR PRO; PR:Q9D1Q4; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9D1Q4; protein.
DR Bgee; ENSMUSG00000042737; Expressed in intestinal villus and 119 other tissues.
DR Genevisible; Q9D1Q4; MM.
DR GO; GO:0033185; C:dolichol-phosphate-mannose synthase complex; ISS:HGNC-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:HGNC-UCL.
DR GO; GO:0008047; F:enzyme activator activity; ISS:HGNC-UCL.
DR GO; GO:0019348; P:dolichol metabolic process; ISO:MGI.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; ISO:MGI.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0031647; P:regulation of protein stability; ISO:MGI.
DR InterPro; IPR013174; DPM3.
DR PANTHER; PTHR16433; PTHR16433; 1.
DR Pfam; PF08285; DPM3; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..92
FT /note="Dolichol-phosphate mannosyltransferase subunit 3"
FT /id="PRO_0000195001"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 92 AA; 10139 MW; B621E6E47337CC40 CRC64;
MTKLTQWLWG LALLGSAWAA LTMGALGLEL PFPCREVLWP LPAYLLVSAG CYALGTVGYR
VATFHDCEDA ARELQSQIVE ARADLARRGL RF
