ID A0A0K0ES84_STRER Unreviewed; 412 AA.
AC A0A0K0ES84;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 22-FEB-2023, entry version 20.
DE SubName: Full=AcidPPc domain-containing protein {ECO:0000313|WBParaSite:SSTP_0001231200.1};
OS Strongyloides stercoralis (Threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=6248 {ECO:0000313|Proteomes:UP000035681, ECO:0000313|WBParaSite:SSTP_0001231200.1};
RN [1] {ECO:0000313|Proteomes:UP000035681}
RP NUCLEOTIDE SEQUENCE.
RA Martin A.A.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SSTP_0001231200.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (AUG-2015) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000256|ARBA:ARBA00008816}.
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DR AlphaFoldDB; A0A0K0ES84; -.
DR STRING; 6248.A0A0K0ES84; -.
DR WBParaSite; SSTP_0001231200.1; SSTP_0001231200.1; SSTP_0001231200.
DR Proteomes; UP000035681; Unassembled WGS sequence.
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:SF114; 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 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000035681};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 31..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 92..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 139..157
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 391..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 412 AA; 47616 MW; AB561099894BAFC0 CRC64;
MSVPPSRAQS EVFSASQYGG KIRRPRYLIN YFVLPTFIVH VIGLACLWTL WYYLRFTDVF
PYHHRVFYCQ DIHLMLPNFK PEDFNVYVSY ELLYVLAFCL PPLVILLGEV AFWLFSTKPR
KTIYASFGEC KVHLFTRRLF RFISVFLFGA LITQIFVDSI KLLTGYQRPY FLSLCNVNMA
ACTAPLQYSP SPSPHLACNY KGASELRYAW LSFPSLHAAF SSYSAIFASC YIYYMINLRG
APLLRPFLIF GFLGLTLVDA FSRINGYKNH WRDIWVGWLI GFVIAFFLCY CVLCFQEVYH
YVIERPPVAV TQGEGGGVAV PEERVSPFFS WFRLPRVQAP SVKEEYVVYE EDVPQVSTVP
NGAPSRHRKG HDRTCEITTV TESYHRTIIP PGQQRERERE HSQANMSAYG AY
//