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Database: UniProt
Entry: Q3MHE3_BOVIN
LinkDB: Q3MHE3_BOVIN
Original site: Q3MHE3_BOVIN 
ID   Q3MHE3_BOVIN            Unreviewed;       236 AA.
AC   Q3MHE3;
DT   25-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2005, sequence version 1.
DT   24-JAN-2024, entry version 87.
DE   RecName: Full=Dolichyldiphosphatase {ECO:0000256|RuleBase:RU367078};
DE            EC=3.6.1.43 {ECO:0000256|RuleBase:RU367078};
DE   Flags: Fragment;
GN   Name=DOLPP1 {ECO:0000313|EMBL:AAI05270.1};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|EMBL:AAI05270.1};
RN   [1] {ECO:0000313|EMBL:AAI05270.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=L1 Hereford {ECO:0000313|EMBL:AAI05270.1};
RC   TISSUE=Ascending colon {ECO:0000313|EMBL:AAI05270.1};
RA   Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y.,
RA   Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C.,
RA   Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J.,
RA   Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J.,
RA   Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D., Siddiqui A.,
RA   Holt R., Jones S.J., Marra M.A.;
RL   Submitted (SEP-2005) 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.
CC       {ECO:0000256|ARBA:ARBA00024907, ECO:0000256|RuleBase:RU367078}.
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:0000256|ARBA:ARBA00034028,
CC         ECO:0000256|RuleBase:RU367078};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|RuleBase:RU367078}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|RuleBase:RU367078}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU367078}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the dolichyldiphosphatase family.
CC       {ECO:0000256|ARBA:ARBA00005518, ECO:0000256|RuleBase:RU367078}.
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DR   EMBL; BC105269; AAI05270.1; -; mRNA.
DR   AlphaFoldDB; Q3MHE3; -.
DR   HOGENOM; CLU_074922_1_2_1; -.
DR   UniPathway; UPA00378; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0047874; F:dolichyldiphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IEA:UniProtKB-UniRule.
DR   CDD; cd03382; PAP2_dolichyldiphosphatase; 1.
DR   Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR   InterPro; IPR039667; Dolichyldiphosphatase_PAP2.
DR   InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   PANTHER; PTHR11247:SF1; DOLICHYLDIPHOSPHATASE 1; 1.
DR   PANTHER; PTHR11247; PALMITOYL-PROTEIN THIOESTERASE/DOLICHYLDIPHOSPHATASE 1; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum {ECO:0000256|RuleBase:RU367078};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU367078};
KW   Membrane {ECO:0000256|RuleBase:RU367078};
KW   Transmembrane {ECO:0000256|RuleBase:RU367078};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU367078}.
FT   TRANSMEM        30..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367078"
FT   TRANSMEM        104..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367078"
FT   TRANSMEM        132..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367078"
FT   TRANSMEM        163..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367078"
FT   DOMAIN          61..178
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAI05270.1"
SQ   SEQUENCE   236 AA;  26837 MW;  7D603EAC200205DB CRC64;
     ADGQCSLPAS WRPVTLTHVE YPAGDLSGHV LAYLSLSPVF VIVGFVTLII FKRELHTISF
     LGGLALNEGV NWLIKHVIQE PRPCGGPHTA VGTKYGMPSS HSQFMWFFSI YSFLFLYLRM
     HQTNNARFLD LLWRHVLSLG LLTVAFLVSY SRVYLLYHTW GQVLYGAVAG GLMAVAWFVF
     TQEVLTPLFP RIAAWPISEF FLIRDTSLIP NVLWFEYTVT RAEARNRQRK LGTKLQ
//
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