ID A0A194QW33_PAPMA Unreviewed; 437 AA.
AC A0A194QW33;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Lipid phosphate phosphohydrolase 3 {ECO:0000313|EMBL:KPJ09519.1};
GN ORFNames=RR48_13153 {ECO:0000313|EMBL:KPJ09519.1};
OS Papilio machaon (Old World swallowtail butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Papilioninae; Papilio.
OX NCBI_TaxID=76193 {ECO:0000313|EMBL:KPJ09519.1, ECO:0000313|Proteomes:UP000053240};
RN [1] {ECO:0000313|EMBL:KPJ09519.1, ECO:0000313|Proteomes:UP000053240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ya'a_city_454_Pm {ECO:0000313|EMBL:KPJ09519.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KPJ09519.1};
RX PubMed=26354079; DOI=10.1038/ncomms9212;
RA Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA Wang W.;
RT "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL Nat. Commun. 6:8212-8212(2015).
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000256|ARBA:ARBA00008816}.
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DR EMBL; KQ461073; KPJ09519.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194QW33; -.
DR STRING; 76193.A0A194QW33; -.
DR InParanoid; A0A194QW33; -.
DR Proteomes; UP000053240; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 2.
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:SF205; ACIDPPC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR10165; LIPID PHOSPHATE PHOSPHATASE; 1.
DR Pfam; PF01569; PAP2; 2.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:KPJ09519.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000053240};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 53..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 208..226
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 247..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 88..227
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 437 AA; 49139 MW; 6E6BEDC0861E9CB6 CRC64;
MMDKLKCFWS KTNRWHRVIA LFVLVELKVL PGGQLGFQCN DPALSHPFTG DTISWKWLMG
ITLLLPLVIV IYSHEKNDSN KKNALCWYKE YVYGVLINLT VIQTLKLIVG SPRPHFFDTC
QPEEAITCVG SEYISSYTCT KAYWLSQSDK SFPSGHTSLG LHAALFIAYY LHRRGASVGR
GAVGVAQIVC VLSAVWCGLS RVQDRRHHWW DVLAGAIIAA PILLYTQHQL HESSSLSEIP
QSYRRQASSG MIALFVLVEL KVLPGGQLGF QCNDPALSHP FTGDTISWKW LMGITLLLPL
VIMLIVERQC NGREKNDLNK KNALCWYKEY VYGVLINLTV IQTLKLIVGS PRPHFFDTCQ
PEEAITCVGS EYISSYTCTK AYWLSQSDKS FPSGHTSLGL HAALFIAIKS LCKDFSCTNI
RNEVRQETKP LDNNCHS
//
