DOPP1_HUMAN
ID DOPP1_HUMAN Reviewed; 238 AA.
AC Q86YN1; A8K3U8; B0QZG4; Q96GF8; Q9Y3G1;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Dolichyldiphosphatase 1;
DE EC=3.6.1.43;
DE AltName: Full=Dolichyl pyrophosphate phosphatase 1;
GN Name=DOLPP1; Synonyms=LSFR2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000312|EMBL:AAO34712.1};
RN [1] {ECO:0000312|EMBL:AAO34712.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Denecke J., Marquardt T., Kranz C.;
RT "Dolichyl pyrophosphate phosphatase (human CWH8).";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cerebellum, and Lung;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4] {ECO:0000312|EMBL:AAO34712.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Lung {ECO:0000312|EMBL:AAH09493.2};
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 198-227.
RX PubMed=10369878; DOI=10.1093/hmg/8.7.1313;
RA Gilley J., Fried M.;
RT "Extensive gene order differences within regions of conserved synteny
RT between the Fugu and human genomes: implications for chromosomal evolution
RT and the cloning of disease genes.";
RL Hum. Mol. Genet. 8:1313-1320(1999).
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 (By
CC similarity). {ECO:0000250|UniProtKB:Q9JMF7}.
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:0000250|UniProtKB:Q9JMF7};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86YN1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86YN1-2; Sequence=VSP_042210;
CC -!- SIMILARITY: Belongs to the dolichyldiphosphatase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB44348.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY189675; AAO34712.1; -; mRNA.
DR EMBL; AK290713; BAF83402.1; -; mRNA.
DR EMBL; AK293627; BAG57084.1; -; mRNA.
DR EMBL; AL592211; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87868.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW87872.1; -; Genomic_DNA.
DR EMBL; BC009493; AAH09493.2; -; mRNA.
DR EMBL; BC033686; AAH33686.1; -; mRNA.
DR EMBL; Y17455; CAB44348.1; ALT_SEQ; Genomic_DNA.
DR CCDS; CCDS48039.1; -. [Q86YN1-2]
DR CCDS; CCDS6918.1; -. [Q86YN1-1]
DR RefSeq; NP_001129389.1; NM_001135917.1. [Q86YN1-2]
DR RefSeq; NP_065171.2; NM_020438.4. [Q86YN1-1]
DR AlphaFoldDB; Q86YN1; -.
DR SMR; Q86YN1; -.
DR BioGRID; 121423; 46.
DR IntAct; Q86YN1; 9.
DR STRING; 9606.ENSP00000361625; -.
DR SwissPalm; Q86YN1; -.
DR BioMuta; DOLPP1; -.
DR DMDM; 45476905; -.
DR EPD; Q86YN1; -.
DR jPOST; Q86YN1; -.
DR MassIVE; Q86YN1; -.
DR MaxQB; Q86YN1; -.
DR PaxDb; Q86YN1; -.
DR PeptideAtlas; Q86YN1; -.
DR PRIDE; Q86YN1; -.
DR ProteomicsDB; 70438; -. [Q86YN1-1]
DR ProteomicsDB; 70439; -. [Q86YN1-2]
DR Antibodypedia; 17806; 85 antibodies from 16 providers.
DR DNASU; 57171; -.
DR Ensembl; ENST00000372546.9; ENSP00000361625.4; ENSG00000167130.18. [Q86YN1-1]
DR Ensembl; ENST00000406974.7; ENSP00000384043.3; ENSG00000167130.18. [Q86YN1-2]
DR GeneID; 57171; -.
DR KEGG; hsa:57171; -.
DR MANE-Select; ENST00000372546.9; ENSP00000361625.4; NM_020438.5; NP_065171.2.
DR UCSC; uc004bxc.4; human. [Q86YN1-1]
DR CTD; 57171; -.
DR DisGeNET; 57171; -.
DR GeneCards; DOLPP1; -.
DR HGNC; HGNC:29565; DOLPP1.
DR HPA; ENSG00000167130; Low tissue specificity.
DR MIM; 614516; gene.
DR neXtProt; NX_Q86YN1; -.
DR OpenTargets; ENSG00000167130; -.
DR PharmGKB; PA134937229; -.
DR VEuPathDB; HostDB:ENSG00000167130; -.
DR eggNOG; KOG3146; Eukaryota.
DR GeneTree; ENSGT00390000013112; -.
DR HOGENOM; CLU_074922_1_2_1; -.
DR InParanoid; Q86YN1; -.
DR OMA; VYATLIW; -.
DR PhylomeDB; Q86YN1; -.
DR TreeFam; TF323451; -.
DR PathwayCommons; Q86YN1; -.
DR Reactome; R-HSA-446199; Synthesis of Dolichyl-phosphate.
DR SignaLink; Q86YN1; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 57171; 134 hits in 1084 CRISPR screens.
DR ChiTaRS; DOLPP1; human.
DR GenomeRNAi; 57171; -.
DR Pharos; Q86YN1; Tdark.
DR PRO; PR:Q86YN1; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q86YN1; protein.
DR Bgee; ENSG00000167130; Expressed in ileal mucosa and 175 other tissues.
DR ExpressionAtlas; Q86YN1; baseline and differential.
DR Genevisible; Q86YN1; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0047874; F:dolichyldiphosphatase activity; ISS:UniProtKB.
DR GO; GO:0006489; P:dolichyl diphosphate biosynthetic process; TAS:Reactome.
DR GO; GO:0008610; P:lipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISS: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 Alternative splicing; Endoplasmic reticulum; Hydrolase; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..238
FT /note="Dolichyldiphosphatase 1"
FT /id="PRO_0000215626"
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 VAR_SEQ 155..197
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042210"
SQ SEQUENCE 238 AA; 27031 MW; 3A9DD3383C61BE94 CRC64;
MAADGQCSLP ASWRPVTLTH VEYPAGDLSG HLLAYLSLSP VFVIVGFVTL IIFKRELHTI
SFLGGLALNE GVNWLIKNVI QEPRPCGGPH TAVGTKYGMP SSHSQFMWFF SVYSFLFLYL
RMHQTNNARF LDLLWRHVLS LGLLAVAFLV SYSRVYLLYH TWSQVLYGGI AGGLMAIAWF
IFTQEVLTPL FPRIAAWPVS EFFLIRDTSL IPNVLWFEYT VTRAEARNRQ RKLGTKLQ
