ID   PLP12_CAEEL             Reviewed;         341 AA.
AC   Q10022;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Phospholipid phosphatase homolog 1.2 homolog {ECO:0000312|WormBase:T28D9.3a};
DE            EC=3.1.3.- {ECO:0000305};
GN   Name=plpp-1.2 {ECO:0000312|WormBase:T28D9.3a};
GN   ORFNames=T28D9.3 {ECO:0000312|WormBase:T28D9.3a};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Bristol N2;
RX   PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA   Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA   Taoka M., Takahashi N., Isobe T.;
RT   "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT   elegans and suggests an atypical translocation mechanism for integral
RT   membrane proteins.";
RL   Mol. Cell. Proteomics 6:2100-2109(2007).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family. {ECO:0000305}.
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DR   EMBL; BX284602; CCD72701.1; -; Genomic_DNA.
DR   PIR; T16951; T16951.
DR   RefSeq; NP_001022377.1; NM_001027206.1.
DR   AlphaFoldDB; Q10022; -.
DR   STRING; 6239.T28D9.3d; -.
DR   iPTMnet; Q10022; -.
DR   EPD; Q10022; -.
DR   PaxDb; Q10022; -.
DR   EnsemblMetazoa; T28D9.3a.1; T28D9.3a.1; WBGene00020895.
DR   GeneID; 174071; -.
DR   UCSC; T28D9.3d; c. elegans.
DR   CTD; 174071; -.
DR   WormBase; T28D9.3a; CE02068; WBGene00020895; plpp-1.2.
DR   eggNOG; KOG3030; Eukaryota.
DR   InParanoid; Q10022; -.
DR   OMA; YNLVMNA; -.
DR   Reactome; R-CEL-1660661; Sphingolipid de novo biosynthesis.
DR   PRO; PR:Q10022; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00020895; Expressed in larva and 3 other tissues.
DR   ExpressionAtlas; Q10022; baseline and differential.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0042577; F:lipid phosphatase activity; IBA:GO_Central.
DR   GO; GO:0008195; F:phosphatidate phosphatase activity; IBA:GO_Central.
DR   GO; GO:0046839; P:phospholipid dephosphorylation; IBA:GO_Central.
DR   GO; GO:0006644; P:phospholipid metabolic process; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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; PTHR10165; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; SSF48317; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Hydrolase; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..341
FT                   /note="Phospholipid phosphatase homolog 1.2 homolog"
FT                   /id="PRO_0000065485"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        71..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        223..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        257..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          284..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          322..341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        162
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17761667"
SQ   SEQUENCE   341 AA;  39028 MW;  DF74E39BC3E2DA8E CRC64;
     MRDHVEFCYY VIIYSLEKFQ QRSKQFGISL FIFFLATAAV TVIVPTLLGV SQRGFFCDDD
     SIRYEYRKDT ITAVQLMLYN LVLNAATVLF VEYYRMQKVE SNINNPRYRW RNNHLHVLFV
     RLLTYFGYSQ IGFVMNIALN IVTKHVVGRL RPHFLDVCKL ANDTCVTGDS HRYITDYTCT
     GPPELVLEAR KSFYSGHSAV SLYCATWSAL YIQARLGPVL NNRIVVPISQ TLMFMIGLGI
     SFSRITDNKH HWSDVLVGIF IGIFLAVYTC TFWTDLFSNN STESETQPLL LPRPPRTPRN
     SEDEERHRLD AVLPSTDSSI VFEATGPQDS DTILLPVPQS A