ID A0A1L9PT63_ASPVE Unreviewed; 230 AA.
AC A0A1L9PT63;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Dolichyldiphosphatase {ECO:0000256|RuleBase:RU367078};
DE EC=3.6.1.43 {ECO:0000256|RuleBase:RU367078};
GN ORFNames=ASPVEDRAFT_86113 {ECO:0000313|EMBL:OJJ04730.1};
OS Aspergillus versicolor CBS 583.65.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=1036611 {ECO:0000313|EMBL:OJJ04730.1, ECO:0000313|Proteomes:UP000184073};
RN [1] {ECO:0000313|Proteomes:UP000184073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 583.65 {ECO:0000313|Proteomes:UP000184073};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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; KV878132; OJJ04730.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9PT63; -.
DR STRING; 1036611.A0A1L9PT63; -.
DR VEuPathDB; FungiDB:ASPVEDRAFT_86113; -.
DR OrthoDB; 989449at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000184073; Unassembled WGS sequence.
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:UP000184073};
KW Transmembrane {ECO:0000256|RuleBase:RU367078};
KW Transmembrane helix {ECO:0000256|RuleBase:RU367078}.
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367078"
FT TRANSMEM 94..110
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367078"
FT TRANSMEM 122..147
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367078"
FT TRANSMEM 153..174
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367078"
FT DOMAIN 53..168
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 230 AA; 25757 MW; 9B08171248D09756 CRC64;
MGKEPPLASL SLTHVHYNPE DPLSFLSAWL ALVPQALCVV YVTLVWATRE VEVGLMFAGQ
LACEALNFAL KRIIKEERPK EMFGKGYGMP SSHAQFVAFF AVYMGLFLMF RHSPNHQNKG
IIFRIIASIG ISLGAIAVAV SRIYLTYHTP RQVLAGGAVG VVYALAWFIF TGFLRSYGWI
DWGLDHSVAR CFRLRDLVVS EDLAEAGWQR WEAKHKVKRS ENGGHTSKLD
//
