PLDL_CAEEL
ID PLDL_CAEEL Reviewed; 554 AA.
AC O17405; G4RZL0; G8JY27;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Probable phospholipase D F09G2.8;
DE EC=3.1.4.4;
DE AltName: Full=Choline phosphatase F09G2.8;
DE AltName: Full=Phosphatidylcholine-hydrolyzing phospholipase D F09G2.8;
GN ORFNames=F09G2.8;
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], AND ALTERNATIVE SPLICING.
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-333, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=12754521; DOI=10.1038/nbt829;
RA Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA Kasai K., Takahashi N., Isobe T.;
RT "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT identify N-linked glycoproteins.";
RL Nat. Biotechnol. 21:667-672(2003).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-333 AND ASN-350, AND
RP IDENTIFICATION BY MASS 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 -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-
CC sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:14445,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58608; EC=3.1.4.4;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b;
CC IsoId=O17405-1; Sequence=Displayed;
CC Name=a;
CC IsoId=O17405-2; Sequence=VSP_042409, VSP_042410;
CC -!- SIMILARITY: Belongs to the phospholipase D family. {ECO:0000305}.
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DR EMBL; FO080529; CCD64428.1; -; Genomic_DNA.
DR EMBL; FO080529; CCD64430.1; -; Genomic_DNA.
DR PIR; T32489; T32489.
DR RefSeq; NP_001122905.1; NM_001129433.2. [O17405-1]
DR RefSeq; NP_001256080.1; NM_001269151.1. [O17405-2]
DR AlphaFoldDB; O17405; -.
DR SMR; O17405; -.
DR BioGRID; 44150; 1.
DR STRING; 6239.F09G2.8b; -.
DR EPD; O17405; -.
DR PaxDb; O17405; -.
DR PeptideAtlas; O17405; -.
DR EnsemblMetazoa; F09G2.8a.1; F09G2.8a.1; WBGene00017316. [O17405-2]
DR EnsemblMetazoa; F09G2.8b.1; F09G2.8b.1; WBGene00017316. [O17405-1]
DR GeneID; 179105; -.
DR KEGG; cel:CELE_F09G2.8; -.
DR UCSC; F09G2.8b; c. elegans. [O17405-1]
DR CTD; 179105; -.
DR WormBase; F09G2.8a; CE09303; WBGene00017316; -. [O17405-2]
DR WormBase; F09G2.8b; CE41221; WBGene00017316; -. [O17405-1]
DR eggNOG; KOG3603; Eukaryota.
DR GeneTree; ENSGT00950000183059; -.
DR InParanoid; O17405; -.
DR OMA; TSCCRRP; -.
DR OrthoDB; 1057467at2759; -.
DR PhylomeDB; O17405; -.
DR Reactome; R-CEL-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Reactome; R-CEL-2029485; Role of phospholipids in phagocytosis.
DR PRO; PR:O17405; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00017316; Expressed in adult organism and 4 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR032803; PLDc_3.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR Pfam; PF13918; PLDc_3; 1.
DR SMART; SM00155; PLDc; 2.
DR PROSITE; PS50035; PLD; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Membrane; Reference proteome; Repeat; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..554
FT /note="Probable phospholipase D F09G2.8"
FT /id="PRO_0000250583"
FT TOPO_DOM 1..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..554
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 272..299
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 492..518
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 277
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 279
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 284
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..25
FT /note="MPLRLINFRQQRRCRQSPSVARLES -> MVSGRTYLTPHEKEENGERKNTR
FT ME (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_042409"
FT VAR_SEQ 26..63
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_042410"
SQ SEQUENCE 554 AA; 63216 MW; 27FC4B5F9C98B4A0 CRC64;
MPLRLINFRQ QRRCRQSPSV ARLESIVLNR RELLLDHFQY SLFQNSSEIP MTTILINDRP
MRHTHDGRAD MTNFEMDLFD TRIEVPTSKN SGGDGMHSPY YDEESSKKRC CKCGNSRNRI
IKPACVPISI VSLFIIALVF LPLFNEEDLA SPIKLTTGCS VDCKTFLVES IPIGLPFKTN
NHTAEAWINI IDNSKQYLDI SVMYWNLNTS DYKSSVYGRR VYEAIIRAGK RGVKIRIAQD
GASNLSDNKE SAYLVQEGLA EVREINVTRL IGSGIIHTKF ILSDIATLYI GSANMDWKSL
SEVKEVGVVF QECPCVASDL YKIFAAYWKL GENDSVIPEK WPISYRTPFN FSSMAKLTMD
GEPAEYFISS SPGPFNPKGR EHDLAAIQKI MKDARKSVCI SVMDYIPSTL YMKKSNRFWP
EIDDSIRDAA YRGVNVRMLI SHWDHSRKEM IPFLKSLQTI TDGLPRYNRT EHGQVQVRIF
TVPPNGKEKI PFTRVNHAKY MVTEDIAYIG TSNWSGDYFI STAGVAMVVR QPSATKRLQN
VFDRDWNSEY SKDL
