ID   DOPP1_CALJA             Reviewed;         238 AA.
AC   B0KWE9;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Dolichyldiphosphatase 1;
DE            EC=3.6.1.43;
DE   AltName: Full=Dolichyl pyrophosphate phosphatase 1;
GN   Name=DOLPP1;
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483;
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}.
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DR   EMBL; DP000573; ABY84174.1; -; Genomic_DNA.
DR   RefSeq; XP_002743415.1; XM_002743369.3.
DR   AlphaFoldDB; B0KWE9; -.
DR   STRING; 9483.ENSCJAP00000037716; -.
DR   GeneID; 100413735; -.
DR   KEGG; cjc:100413735; -.
DR   CTD; 57171; -.
DR   eggNOG; KOG3146; Eukaryota.
DR   HOGENOM; CLU_074922_1_2_1; -.
DR   InParanoid; B0KWE9; -.
DR   OMA; VYATLIW; -.
DR   OrthoDB; 1312138at2759; -.
DR   TreeFam; TF323451; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000008225; Unplaced.
DR   Bgee; ENSCJAG00000020287; Expressed in liver and 6 other tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0047874; F:dolichyldiphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
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_0000344994"
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;  27003 MW;  8EB32E282A19B7F6 CRC64;
     MAADGQCSLP ASWRPVTLTH VEYPAGDLSG HLLAYLSLSP VFVIVGFVTL IIFKRELHTI
     SFLGGLALNE GVNWLIKNVI QEPRPCGGPH TAVGTKYGMP SSHSQFMWFF SVYSFLFLYL
     RMHQTNNARF LDLLWRHVLS LGLLAAAFLV SYSRVYLLYH TWSQVLYGGI AGGLMAVAWF
     IFTQEVLTPL FPRIAAWPIS EFFLIRDTSL IPNVLWFEYT VTRAEARNRQ RKLGTKLQ