PLD2_BOVIN
ID PLD2_BOVIN Reviewed; 933 AA.
AC Q0V8L6; Q08DV7;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Phospholipase D2;
DE Short=PLD 2;
DE EC=3.1.4.4 {ECO:0000250|UniProtKB:P97813};
DE AltName: Full=Choline phosphatase 2;
DE AltName: Full=Phosphatidylcholine-hydrolyzing phospholipase D2;
GN Name=PLD2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Function as phospholipase selective for phosphatidylcholine.
CC May have a role in signal-induced cytoskeletal regulation and/or
CC endocytosis. {ECO:0000250|UniProtKB:P97813}.
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 Evidence={ECO:0000250|UniProtKB:P97813};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14446;
CC Evidence={ECO:0000250|UniProtKB:P97813};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1,2-
CC dihexadecanoyl-sn-glycero-3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:44872, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72859, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000250|UniProtKB:P97813};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44873;
CC Evidence={ECO:0000250|UniProtKB:P97813};
CC -!- SUBUNIT: Interacts with PIP5K1B (By similarity). Interacts with EGFR
CC (By similarity). {ECO:0000250|UniProtKB:O14939,
CC ECO:0000250|UniProtKB:P97813}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P97813};
CC Lipid-anchor {ECO:0000250|UniProtKB:P97813}.
CC -!- PTM: Phosphorylated by FGR. {ECO:0000250|UniProtKB:P70498}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. {ECO:0000305}.
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DR EMBL; BT026202; ABG67041.1; -; mRNA.
DR EMBL; BC123547; AAI23548.1; -; mRNA.
DR RefSeq; NP_001069295.1; NM_001075827.1.
DR AlphaFoldDB; Q0V8L6; -.
DR SMR; Q0V8L6; -.
DR STRING; 9913.ENSBTAP00000035115; -.
DR PaxDb; Q0V8L6; -.
DR PRIDE; Q0V8L6; -.
DR GeneID; 522159; -.
DR KEGG; bta:522159; -.
DR CTD; 5338; -.
DR eggNOG; KOG1329; Eukaryota.
DR InParanoid; Q0V8L6; -.
DR OrthoDB; 755722at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0004630; F:phospholipase D activity; IBA:GO_Central.
DR GO; GO:0048017; P:inositol lipid-mediated signaling; IEA:InterPro.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
DR GO; GO:0009395; P:phospholipid catabolic process; IBA:GO_Central.
DR GO; GO:0060627; P:regulation of vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR016555; PLipase_D_euk.
DR InterPro; IPR015679; PLipase_D_fam.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR PANTHER; PTHR18896; PTHR18896; 2.
DR Pfam; PF00614; PLDc; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR Pfam; PF00787; PX; 1.
DR PIRSF; PIRSF009376; Phospholipase_D_euk; 1.
DR SMART; SM00155; PLDc; 2.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50035; PLD; 2.
DR PROSITE; PS50195; PX; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Hydrolase; Lipid degradation; Lipid metabolism; Lipoprotein;
KW Membrane; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..933
FT /note="Phospholipase D2"
FT /id="PRO_0000253038"
FT DOMAIN 65..195
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 203..311
FT /note="PH"
FT DOMAIN 437..464
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 751..778
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..788
FT /note="Catalytic"
SQ SEQUENCE 933 AA; 105766 MW; 8B5C417338397455 CRC64;
MAATPQSLFP SGDDLDSSQL QMEPDEVDTL KEGEDPADRM HPFLAIYHLQ PLKLHPLVFA
PGVPVIAQVV GTERYTSGSK VGTCTLYSVR LTHGDFTWTT KKKFRHFQEL HRDLLRHKVF
MSLLPLARFA VASSPAPEGD SREIPSLPRA GPEGSSRRTA SKQKYLENYL NRLLTMSFYR
NYHAMTEFLE VSQLSFIPDL GCKGLEGVIR KRSGGHRVPG LTCCGRDQVC YRWSKRWLVV
KDSFLLYMCL ETGAISFVQL FDPGFKVQVG KRSTEARYGV RVDTSHRSLI LKCSSYRQAR
WWAQEITELA QGPGRDFIQL HRHDSYAPPR PGTLARWFVN GAGYFAAVAD AILRAQEEIF
ITDWWLSPEI YLKRPAHSDD WRLDIMLKKK AEEGVHVSVL LFKEVELALA INSGYSKKAL
MLLHPNIKVM RHPDQVTLWA HHEKLLVVDQ VVAFLGGLDL AYGRWDDLHY RLTDLGDSSE
SAAPQPPTSC SDLPATPDLT HNQLFWLGKD YSNLITKDWV QLDRPFDDFI DRETMPRMPW
RDIGVVVHGS PARDLARHFI QRWNFTKTTK TKYKIPIYPY LLPKSTSTAN QLPFTLSGGQ
CATVQVLRSV DRWSAGTLEN SILNAYLHTI RESQHFLYIE NQFFISCSDG RTVLNKVGDE
IVDRILKAHK QGQCFRVYVL LPLLPGFEGD ISTGGGNSIQ AILHFTYRTL CRGEYSILHR
LKAAMGTEWR NYISVCGLRT HGELGGHPVS ELIYIHSKML IADDRTVIIG SANINDRSLL
GKRDSELAVL IEDTEMEPSL MNGVEYQAGR FALSLRKHCF SVILGAAARP HLDLRDPVCD
AFFQLWQDTA ESNANIYEQI FRCLPSNATR SLRALREYVV VEPLATVSPP LARSELNQVQ
GHLVHFPLKF LEDEYLLPSL GSKEGVMPLE VWT
