DOPP1_MOUSE
ID DOPP1_MOUSE Reviewed; 238 AA.
AC Q9JMF7; Q8BN02; Q8R0P7; Q9CRF2;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Dolichyldiphosphatase 1;
DE EC=3.6.1.43;
DE AltName: Full=Dolichyl pyrophosphate phosphatase 1;
DE AltName: Full=Protein 2-23;
GN Name=Dolpp1;
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 {ECO:0000312|EMBL:BAA92753.1};
RN [1] {ECO:0000312|EMBL:BAA92753.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:BAA92753.1};
RX PubMed=10679242; DOI=10.1006/bbrc.2000.2170;
RA Inoue S., Sano H., Ohta M.;
RT "Growth suppression of Escherichia coli by induction of expression of
RT mammalian genes with transmembrane or ATPase domains.";
RL Biochem. Biophys. Res. Commun. 268:553-561(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Brain cortex, Embryonic stem cell, Kidney, and Oviduct;
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH26544.1};
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH26544.1};
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] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12198133; DOI=10.1074/jbc.m207076200;
RA Rush J.S., Cho S.K., Jiang S., Hofmann S.L., Waechter C.J.;
RT "Identification and characterization of a cDNA encoding a dolichyl
RT pyrophosphate phosphatase located in the endoplasmic reticulum of mammalian
RT cells.";
RL J. Biol. Chem. 277:45226-45234(2002).
CC -!- FUNCTION: Required for efficient N-glycosylation. Necessary for
CC maintaining optimal levels of dolichol-linked oligosaccharides.
CC Hydrolyzes dolichyl pyrophosphate at a very high rate and dolichyl
CC monophosphate at a much lower rate. Does not act on phosphatidate.
CC {ECO:0000269|PubMed:12198133}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl diphosphate + H2O = a dolichyl phosphate + H(+) +
CC phosphate; Xref=Rhea:RHEA:14385, Rhea:RHEA-COMP:9517, Rhea:RHEA-
CC COMP:9529, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57497, ChEBI:CHEBI:57683; EC=3.6.1.43;
CC Evidence={ECO:0000269|PubMed:12198133};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12198133}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12198133}.
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in brain,
CC kidney, lung and intestine. {ECO:0000269|PubMed:12198133}.
CC -!- SIMILARITY: Belongs to the dolichyldiphosphatase family. {ECO:0000305}.
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DR EMBL; AB030189; BAA92753.1; -; mRNA.
DR EMBL; AK002544; BAC24998.1; ALT_SEQ; mRNA.
DR EMBL; AK010797; BAB27187.1; -; mRNA.
DR EMBL; AK044141; BAC31797.1; -; mRNA.
DR EMBL; AK053923; BAC35595.1; -; mRNA.
DR EMBL; BC026544; AAH26544.1; -; mRNA.
DR CCDS; CCDS15881.1; -.
DR RefSeq; NP_001277437.1; NM_001290508.1.
DR RefSeq; NP_001277438.1; NM_001290509.1.
DR RefSeq; NP_065062.1; NM_020329.4.
DR RefSeq; XP_006498270.1; XM_006498207.3.
DR AlphaFoldDB; Q9JMF7; -.
DR STRING; 10090.ENSMUSP00000028209; -.
DR MaxQB; Q9JMF7; -.
DR PaxDb; Q9JMF7; -.
DR PeptideAtlas; Q9JMF7; -.
DR PRIDE; Q9JMF7; -.
DR ProteomicsDB; 279472; -.
DR Antibodypedia; 17806; 85 antibodies from 16 providers.
DR DNASU; 57170; -.
DR Ensembl; ENSMUST00000028209; ENSMUSP00000028209; ENSMUSG00000026856.
DR GeneID; 57170; -.
DR KEGG; mmu:57170; -.
DR UCSC; uc008jci.2; mouse.
DR CTD; 57171; -.
DR MGI; MGI:1914093; Dolpp1.
DR VEuPathDB; HostDB:ENSMUSG00000026856; -.
DR eggNOG; KOG3146; Eukaryota.
DR GeneTree; ENSGT00390000013112; -.
DR HOGENOM; CLU_074922_1_2_1; -.
DR InParanoid; Q9JMF7; -.
DR OMA; VYATLIW; -.
DR OrthoDB; 1312138at2759; -.
DR PhylomeDB; Q9JMF7; -.
DR TreeFam; TF323451; -.
DR BRENDA; 3.6.1.43; 3474.
DR Reactome; R-MMU-446199; Synthesis of Dolichyl-phosphate.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 57170; 15 hits in 75 CRISPR screens.
DR ChiTaRS; Dolpp1; mouse.
DR PRO; PR:Q9JMF7; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9JMF7; protein.
DR Bgee; ENSMUSG00000026856; Expressed in ileal epithelium and 172 other tissues.
DR ExpressionAtlas; Q9JMF7; baseline and differential.
DR Genevisible; Q9JMF7; MM.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0047874; F:dolichyldiphosphatase activity; IDA:UniProtKB.
DR GO; GO:0008610; P:lipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:UniProtKB.
DR CDD; cd03382; PAP2_dolichyldiphosphatase; 1.
DR InterPro; IPR039667; Dolichyldiphosphatase_PAP2.
DR InterPro; IPR039666; Dolpp1/Cax4.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR PANTHER; PTHR11247:SF1; PTHR11247:SF1; 1.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; SSF48317; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Hydrolase; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..238
FT /note="Dolichyldiphosphatase 1"
FT /id="PRO_0000215627"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 93
FT /note="V -> A (in Ref. 3; AAH26544)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="L -> S (in Ref. 2; BAB27187)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 238 AA; 27099 MW; 64E5E3165FC8BDBB CRC64;
MAADGQCSLP ASWRPVTLTH VEYPAGDLSG HLLAYLSLSP IFVVVGFLTL IIFKRELHTI
SFLGGLALNQ GVNWLIKHVI QEPRPCGGPH TAVGTKYGMP SSHSQFMWFF SVYSFLFLYL
RMHQTNNARF LDLLWRHVLS LGLLTAAFLV SYSRVYLLYH TWSQVFYGGV AGSLMAVAWF
IITQEILTPL FPRIAAWPIS EFFLIRDTSL IPNVLWFEYT VTRAEARNRQ RKLGTKLQ
