ID W8BIL3_CERCA Unreviewed; 400 AA.
AC W8BIL3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Putative phosphatidate phosphatase {ECO:0000313|EMBL:JAC01121.1};
GN Name=WUN {ECO:0000313|EMBL:JAC01121.1};
OS Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC Tephritidae; Ceratitis; Ceratitis.
OX NCBI_TaxID=7213 {ECO:0000313|EMBL:JAC01121.1};
RN [1] {ECO:0000313|EMBL:JAC01121.1}
RP NUCLEOTIDE SEQUENCE.
RA Geib S.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAC01121.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24495485; DOI=10.1186/1471-2164-15-98;
RA Calla B., Hall B., Hou S., Geib S.M.;
RT "A genomic perspective to assessing quality of mass-reared SIT flies used
RT in Mediterranean fruit fly (Ceratitis capitata) eradication in
RT California.";
RL BMC Genomics 15:98-98(2014).
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000256|ARBA:ARBA00008816}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GAMC01005437; JAC01119.1; -; mRNA.
DR EMBL; GAMC01005435; JAC01121.1; -; mRNA.
DR AlphaFoldDB; W8BIL3; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR CDD; cd03384; PAP2_wunen; 1.
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:SF103; FI04477P-RELATED; 1.
DR PANTHER; PTHR10165; LIPID PHOSPHATE PHOSPHATASE; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 109..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 320..339
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 351..369
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 216..366
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 400 AA; 45063 MW; A562AC8747185879 CRC64;
MSNESTSCEV TLLCRPERQN SADVSSSPLL LVKSSDVEKR YQNPNHNCNN INDSNCNCND
SNNINATVST AATVAIANLN NNNVKVRLSA GCTGEHVSET IRMDHNKRVL LRVALDVFIL
LCVGFPILFL YLWGKSYHRG FFCDDESLKH PFKDSTVPNW MLYVIGLVIP IGVITTSEIV
RAEHSKHSTE DVISTRRYVF MDYEIPVWMV ESYKSIGAFG FGAAVCQLIT DIAKYSIGRL
RPHFFAVCQP MKSDKAICDD PSNVGKYIED FTCRGLNSTE RMLKEVSLSF PSGHSSFTFY
TMVYTAIYLQ SRMNWRGSKL LRHFLQFLLI IIAWYTALSR VSDYKHHWSD VFAGSTIGAL
TAVIVANFVS DLFKRKSPQQ YLLPRTSQDA QPQTIASNGH
//
