ID Q8T0D6_DROME Unreviewed; 300 AA.
AC Q8T0D6; Q9VND5; Q9VND6;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE SubName: Full=LD09836p {ECO:0000313|EMBL:AAL39535.1};
GN ORFNames=CG12746 {ECO:0000313|EMBL:AAL39535.1,
GN ECO:0000313|FlyBase:FBgn0037341};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AAL39535.1};
RN [1] {ECO:0000313|EMBL:AAL39535.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Berkeley {ECO:0000313|EMBL:AAL39535.1};
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Farfan D., Frise E., George R., Gonzalez M.,
RA Guarin H., Li P., Liao G., Miranda A., Mungall C.J., Nunoo J., Pacleb J.,
RA Paragas V., Park S., Phouanenavong S., Wan K., Yu C., Lewis S.E.,
RA Rubin G.M., Celniker S.;
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000256|ARBA:ARBA00008816}.
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DR EMBL; AY069390; AAL39535.1; -; mRNA.
DR AlphaFoldDB; Q8T0D6; -.
DR IntAct; Q8T0D6; 2.
DR UCSC; CG12746-RE; d. melanogaster.
DR AGR; FB:FBgn0037341; -.
DR FlyBase; FBgn0037341; CG12746.
DR VEuPathDB; VectorBase:FBgn0037341; -.
DR OrthoDB; 25293at2759; -.
DR ExpressionAtlas; Q8T0D6; baseline and differential.
DR GO; GO:0016020; C:membrane; ISS:FlyBase.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; ISS:FlyBase.
DR GO; GO:0046839; P:phospholipid dephosphorylation; IBA:GO_Central.
DR GO; GO:0006644; P:phospholipid metabolic process; ISS:FlyBase.
DR Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR InterPro; IPR043216; PA_PP_rel.
DR PANTHER; PTHR10165; LIPID PHOSPHATE PHOSPHATASE; 1.
DR PANTHER; PTHR10165:SF35; RE23632P; 1.
DR Pfam; PF01569; PAP2; 1.
DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE 2: Evidence at transcript level;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 169..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 221..240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 178..240
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|Pfam:PF01569"
FT REGION 1..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 300 AA; 34378 MW; 6A781894B005B8AB CRC64;
MPDSCTADLR SRRRENPIDR NGNIGGTGKE QATSTRPKLT TEYTQRTNEM TASKEGQESR
RTLSDSSAED VRNTGSRTRT NDDEMWRNEL AMNTDSSSVQ PEKREERSHR TGNSNAKLSD
AVDVVLRVLL VITFFKLETM TAFKREIHEE ELWLYKNPRR PDIVRGGELL FWVIVAPFLV
TIAFYWYTRD RRLCIAVIPL FIALLVAVSR TCDYHHHWQD VTIGGLIGLF AGYISYTQYY
PSIFCPDAGI PLVRWPSREG SQYQRLSGKD DNGSRGPHHL DGGDAVRRPL LADKEESKWY
//
