ID A0A1X7RL15_ZYMTR Unreviewed; 225 AA.
AC A0A1X7RL15;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Dolichyldiphosphatase {ECO:0000256|RuleBase:RU367078};
DE EC=3.6.1.43 {ECO:0000256|RuleBase:RU367078};
GN ORFNames=ZT3D7_G3247 {ECO:0000313|EMBL:SMQ48098.1};
OS Zymoseptoria tritici ST99CH_3D7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1276538 {ECO:0000313|EMBL:SMQ48098.1, ECO:0000313|Proteomes:UP000215127};
RN [1] {ECO:0000313|EMBL:SMQ48098.1, ECO:0000313|Proteomes:UP000215127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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|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|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|RuleBase:RU367078}.
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DR EMBL; LT853693; SMQ48098.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7RL15; -.
DR STRING; 1276538.A0A1X7RL15; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000215127; Chromosome 2.
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 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU367078};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU367078};
KW Membrane {ECO:0000256|RuleBase:RU367078};
KW Reference proteome {ECO:0000313|Proteomes:UP000215127};
KW Transmembrane {ECO:0000256|RuleBase:RU367078};
KW Transmembrane helix {ECO:0000256|RuleBase:RU367078}.
FT TRANSMEM 22..45
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367078"
FT TRANSMEM 89..108
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367078"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367078"
FT TRANSMEM 160..181
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367078"
FT DOMAIN 52..175
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 225 AA; 24880 MW; 420C6BF3339A82BF CRC64;
MDGPPLASLS LTHVNYDPTD RIAWLCAHLA LVPQALVITY TALIWSTREI EILLMFAGQM
GCEALNWILK RYFKEQRPTQ IVGKGYGMPS SHAQFVAFFA TYLTLFLLLR HDPHNHPLAS
STHTPIPLWQ RIGTALAAIG GAAAVALSRT YLKYHSPKQI NVGCLVGVAC GIAWFVVTSI
ARRTGLVHKL LELPPLRSVD DGKRKNNFAT NDQRLQLPDS SLQLA
//
