ID   DOPP1_PAPAN             Reviewed;         238 AA.
AC   B0CM95;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Dolichyldiphosphatase 1;
DE            EC=3.6.1.43;
DE   AltName: Full=Dolichyl pyrophosphate phosphatase 1;
GN   Name=DOLPP1;
OS   Papio anubis (Olive baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Antonellis A., Benjamin B., Blakesley R.W., Bouffard G.G., Brinkley C.,
RA   Brooks S., Chu G., Chub I., Coleman H., Fuksenko T., Gestole M.,
RA   Gregory M., Guan X., Gupta J., Gurson N., Han E., Han J., Hansen N.,
RA   Hargrove A., Hines-Harris K., Ho S.-L., Hu P., Hunter G., Hurle B.,
RA   Idol J.R., Johnson T., Knight E., Kwong P., Lee-Lin S.-Q., Legaspi R.,
RA   Madden M., Maduro Q.L., Maduro V.B., Margulies E.H., Masiello C.,
RA   Maskeri B., McDowell J., Merkulov G., Montemayor C., Mullikin J.C.,
RA   Park M., Prasad A., Ramsahoye C., Reddix-Dugue N., Riebow N., Schandler K.,
RA   Schueler M.G., Sison C., Smith L., Stantripop S., Thomas J.W., Thomas P.J.,
RA   Tsipouri V., Young A., Green E.D.;
RT   "NISC comparative sequencing initiative.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the dolichyldiphosphatase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DP000555; ABY56113.1; -; Genomic_DNA.
DR   RefSeq; NP_001162454.1; NM_001168983.1.
DR   RefSeq; XP_017804770.1; XM_017949281.1.
DR   AlphaFoldDB; B0CM95; -.
DR   STRING; 9555.ENSPANP00000018855; -.
DR   Ensembl; ENSPANT00000028367; ENSPANP00000018855; ENSPANG00000025954.
DR   GeneID; 100137451; -.
DR   KEGG; panu:100137451; -.
DR   CTD; 57171; -.
DR   eggNOG; KOG3146; Eukaryota.
DR   GeneTree; ENSGT00390000013112; -.
DR   OrthoDB; 1312138at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000028761; Chromosome 13.
DR   Bgee; ENSPANG00000025954; Expressed in cornea and 65 other tissues.
DR   ExpressionAtlas; B0CM95; baseline.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:Ensembl.
DR   GO; GO:0047874; F:dolichyldiphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IEA:Ensembl.
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   3: Inferred from homology;
KW   Endoplasmic reticulum; Hydrolase; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..238
FT                   /note="Dolichyldiphosphatase 1"
FT                   /id="PRO_0000330748"
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"
SQ   SEQUENCE   238 AA;  27017 MW;  76032D283896A575 CRC64;
     MAADGQCSLP ASWRPVTLTH VEYPAGDLSG HLLAYLSLSP VFVIVGFVTL IIFKRELHTI
     SFLGGLALNE GVNWLIKNVI QEPRPCGGPH TAVGTKYGMP SSHSQFMWFF SIYSFLFLYL
     RMHQTNNARF LDLLWRHVLS LGLLAAAFLV SYSRVYLLYH TWSQVLYGGI AGGLMAIAWF
     IFTQEVLTPL FPRIAAWPVS EFFLIRDTSL IPNVLWFEYT VTRAEARNRQ RKLGTKLQ