ID   DOPP1_RHIFE             Reviewed;         238 AA.
AC   B2KI79;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Dolichyldiphosphatase 1;
DE            EC=3.6.1.43;
DE   AltName: Full=Dolichyl pyrophosphate phosphatase 1;
GN   Name=DOLPP1;
OS   Rhinolophus ferrumequinum (Greater horseshoe bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Rhinolophidae;
OC   Rhinolophinae; Rhinolophus.
OX   NCBI_TaxID=59479;
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 (APR-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}.
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DR   EMBL; DP000711; ACC64539.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2KI79; -.
DR   Ensembl; ENSRFET00010035446; ENSRFEP00010032727; ENSRFEG00010021538.
DR   GeneTree; ENSGT00390000013112; -.
DR   OMA; VYATLIW; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000472240; Chromosome 12.
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_0000344996"
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;  27064 MW;  32A3BD71E2C91AFD CRC64;
     MAADGQCSLP ASWRPVTLTH VEYPAGDLSG HLLAYLSLSP VVIIVGFVTL IIFKRELHTI
     SFLGGLVLNE GVNWLIKHVI QEPRPCGGPH PTVGTKYGMP SSHSQFMWFF SVYSFLFLYL
     RMHQTNNARF LDLLWRHVLS LGLLTAAFLV SYSRVYLLYH TWSQVLYGGV AGSLMAIAWF
     AFTQEVLTPL FPRIAAWPIS EFFLIRDTSL IPNVLWFEYT VTRAEARNRQ RKLGTKLQ