ID   A0A0K0CUA2_ANGCA        Unreviewed;       319 AA.
AC   A0A0K0CUA2;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=AcidPPc domain-containing protein {ECO:0000313|WBParaSite:ACAC_0000076901-mRNA-1};
OS   Angiostrongylus cantonensis (Rat lungworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC   Angiostrongylus.
OX   NCBI_TaxID=6313 {ECO:0000313|Proteomes:UP000035642, ECO:0000313|WBParaSite:ACAC_0000076901-mRNA-1};
RN   [1] {ECO:0000313|Proteomes:UP000035642}
RP   NUCLEOTIDE SEQUENCE.
RA   Martin A.A.;
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:ACAC_0000076901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family. {ECO:0000256|ARBA:ARBA00008816}.
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DR   AlphaFoldDB; A0A0K0CUA2; -.
DR   STRING; 6313.A0A0K0CUA2; -.
DR   WBParaSite; ACAC_0000076901-mRNA-1; ACAC_0000076901-mRNA-1; ACAC_0000076901.
DR   Proteomes; UP000035642; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
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:SF185; 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:UP000035642};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        57..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        155..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        216..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        248..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        280..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          154..295
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
SQ   SEQUENCE   319 AA;  36524 MW;  EA5EDDB76A8A0E05 CRC64;
     LFWLSRCEVG IVTSRKGFAG TSLNNLGERL YTNFRITFSG RLSTQDGDGE RSFRGTLVRG
     LICMVLDISI TLVISIVLFY TFSGYAISPY ERPIPCNDES IRQPFKPNTV GMKQLLVVSL
     GSPFLIICFV EALVFHYSQG YNKLANYFSI STLLYLKYLL TYTLCTILME YFKCTVGRLR
     PHFIAVCQPD WSRMDFSETY CMNPDSRRIR SARTSFPSGH AAAAFHVLIF ICIYLPRMAK
     ITGIPYLFKI RNILLVIYTS WTVFTAITRV TDFWHHSTDV LGGIILATVC VIPVFGWQWK
     NDDDVYVPRQ LTKSHLHIE
//