ID F1L4Q0_ASCSU Unreviewed; 403 AA.
AC F1L4Q0;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Lipid phosphate phosphatase-related protein type 5 {ECO:0000313|EMBL:ADY45104.1};
OS Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY45104.1};
RN [1] {ECO:0000313|EMBL:ADY45104.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21685128; DOI=10.1101/gr.121426.111;
RA Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA Davis R.E.;
RT "Deep small RNA sequencing from the nematode Ascaris reveals conservation,
RT functional diversification, and novel developmental profiles.";
RL Genome Res. 21:1462-1477(2011).
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000256|ARBA:ARBA00008816}.
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DR EMBL; JI171304; ADY45104.1; -; mRNA.
DR AlphaFoldDB; F1L4Q0; -.
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:SF102; ACIDPPC DOMAIN-CONTAINING PROTEIN; 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 32..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 139..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 243..262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 274..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 143..289
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
FT REGION 354..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 403 AA; 47037 MW; 6EBB14479A2DFD0B CRC64;
MSIPPSRAQS EVFSASQYGT QPIRARRQIN HFILPTFILS VVGLACLWAL WYYMSFTSVF
PYHHRVFYCR DIYLYLPNFR PEDFQVYVSY ALLYTLGFAL PPLVILIGEI MFWLFSTKPR
KTVYANCGEC KVHLFTRRVV RFIGVFMFGA LITQIFVHTI KLMTGYQRPY FLSLCNVNMS
MCTAPLEHSP SPSPALACNY RNADDLRYAW LSFPSLHAAF SSYSCIFASC YIYYMINLRG
APLLRPFLIF GFLGLTIVDS FSRINGYKNH WRDIWVGWLI GFFIALFLCY SVLCFQEVYH
VVVDKVPMLE ERVSPFFSWF RLPRVHAPSL KEEYVVYEED VPEQGTTIRH RYTSSTESGS
HLRSHNNHRK LSSNHLTTPT TTTAQWLYCL LSMTFTYYHC LLL
//
