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   16-JUN-2009, entry version 25.
DE   RecName: Full=Phospholipase D2;
DE            Short=PLD 2;
DE            EC=3.1.4.4;
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;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; 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: May have a role in signal-induced cytoskeletal
CC       regulation and/or endocytosis (By similarity).
CC   -!- CATALYTIC ACTIVITY: A phosphatidylcholine + H(2)O = choline + a
CC       phosphatidate.
CC   -!- ENZYME REGULATION: Stimulated by phosphatidylinositol 4,5-
CC       bisphosphate and activated by the ADP-ribosylation factor-1 (ARF-
CC       1) (By similarity).
CC   -!- SUBUNIT: Interacts with EGFR and PIP5K1A (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the phospholipase D family.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 2 PLD phosphodiesterase domains.
CC   -!- SIMILARITY: Contains 1 PX (phox homology) domain.
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DR   EMBL; BT026202; ABG67041.1; -; mRNA.
DR   EMBL; BC123547; AAI23548.1; -; mRNA.
DR   IPI; IPI00704116; -.
DR   RefSeq; NP_001069295.1; -.
DR   UniGene; Bt.1009; -.
DR   GeneID; 522159; -.
DR   KEGG; bta:522159; -.
DR   HOVERGEN; Q0V8L6; -.
DR   BRENDA; 3.1.4.4; 251.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070290; F:NAPE-specific phospholipase D activity; IEA:EC.
DR   GO; GO:0035091; F:phosphoinositide binding; IEA:InterPro.
DR   GO; GO:0004630; F:phospholipase D activity; IEA:EC.
DR   GO; GO:0005515; F:protein binding; IEA:InterPro.
DR   GO; GO:0007154; P:cell communication; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR015679; Phospholipase_D.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   InterPro; IPR016555; PLipase_D_euk.
DR   InterPro; IPR001683; PX.
DR   Gene3D; G3DSA:3.30.1520.10; PX; 1.
DR   PANTHER; PTHR18896; Phospholipase_D; 1.
DR   Pfam; PF00614; PLDc; 2.
DR   Pfam; PF00787; PX; 1.
DR   PIRSF; PIRSF009376; Phospholipase_D_euk; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00155; PLDc; 2.
DR   SMART; SM00312; PX; 1.
DR   PROSITE; PS50003; PH_DOMAIN; FALSE_NEG.
DR   PROSITE; PS50035; PLD; 2.
DR   PROSITE; PS50195; PX; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Lipid degradation; Membrane; Repeat.
FT   CHAIN         1    933       Phospholipase D2.
FT                                /FTId=PRO_0000253038.
FT   DOMAIN       65    195       PX.
FT   DOMAIN      203    311       PH.
FT   DOMAIN      437    464       PLD phosphodiesterase 1.
FT   DOMAIN      751    778       PLD phosphodiesterase 2.
FT   REGION      441    788       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
//