ID A0A182V2K6_ANOME Unreviewed; 250 AA.
AC A0A182V2K6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Dolichyldiphosphatase {ECO:0000256|RuleBase:RU367078};
DE EC=3.6.1.43 {ECO:0000256|RuleBase:RU367078};
OS Anopheles merus (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=30066 {ECO:0000313|EnsemblMetazoa:AMEM007810-PA, ECO:0000313|Proteomes:UP000075903};
RN [1] {ECO:0000313|Proteomes:UP000075903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAF {ECO:0000313|Proteomes:UP000075903};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles merus MAF (V2).";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AMEM007810-PA}
RP IDENTIFICATION.
RC STRAIN=MAF {ECO:0000313|EnsemblMetazoa:AMEM007810-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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 AlphaFoldDB; A0A182V2K6; -.
DR STRING; 30066.A0A182V2K6; -.
DR EnsemblMetazoa; AMEM007810-RA; AMEM007810-PA; AMEM007810.
DR VEuPathDB; VectorBase:AMEM007810; -.
DR VEuPathDB; VectorBase:AMEM21_006121; -.
DR OrthoDB; 989449at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000075903; 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 Transmembrane {ECO:0000256|RuleBase:RU367078};
KW Transmembrane helix {ECO:0000256|RuleBase:RU367078}.
FT TRANSMEM 43..64
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367078"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367078"
FT TRANSMEM 111..133
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367078"
FT TRANSMEM 145..170
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367078"
FT TRANSMEM 176..198
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367078"
FT DOMAIN 70..191
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 250 AA; 28752 MW; 97AF8EA0C18C9894 CRC64;
MSSPDLLLPN EPSLSVDENV AIDWQPITLT LVEYPKGDLV GKLLAWISLA PLGIGAGFVA
LILFRRDLHT IVFFLGTLVN ECLNILLKHW IQEPRPVSRA QIWTEYGMPS SHSQFMCFFS
TYVLLFIFIR LHHINNSNSA RFERLVRLLV LAICWTAAFL VCFGRIYLLY HTLSQVLIGA
LVGTVMGALW FLLTHFVLTP YFPMVVLWRV SELFLLRDTT LIPNILWFEY TVTRHEARAR
SRKLVSMKSQ
//
