PLD1_CRIGR
ID PLD1_CRIGR Reviewed; 1036 AA.
AC O08684;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Phospholipase D1;
DE Short=PLD 1;
DE EC=3.1.4.4;
DE AltName: Full=Choline phosphatase 1;
DE AltName: Full=Phosphatidylcholine-hydrolyzing phospholipase D1;
GN Name=PLD1;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Klaus J.R., Baldassare J.J., Raben D.M.;
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Implicated as a critical step in numerous cellular pathways,
CC including signal transduction, membrane trafficking, and the regulation
CC of mitosis. May be involved in the regulation of perinuclear
CC intravesicular membrane traffic (By similarity). {ECO:0000250}.
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 -!- ACTIVITY REGULATION: Stimulated by phosphatidylinositol 4,5-
CC bisphosphate and phosphatidylinositol 3,4,5-trisphosphate, activated by
CC the phosphokinase C-alpha, by the ADP-ribosylation factor-1 (ARF-1),
CC and to a lesser extent by GTP-binding proteins: RHO A, RAC-1 and CDC42.
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PIP5K1B. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}.
CC Endoplasmic reticulum membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus membrane
CC {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Late endosome membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. {ECO:0000305}.
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DR EMBL; U94995; AAB53631.1; -; mRNA.
DR PIR; T18530; T18530.
DR RefSeq; NP_001233757.1; NM_001246828.1.
DR AlphaFoldDB; O08684; -.
DR SMR; O08684; -.
DR STRING; 10029.NP_001233757.1; -.
DR PRIDE; O08684; -.
DR GeneID; 100689404; -.
DR KEGG; cge:100689404; -.
DR CTD; 5337; -.
DR eggNOG; KOG1329; Eukaryota.
DR OrthoDB; 755722at2759; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; 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; IEA:UniProtKB-EC.
DR GO; GO:0048017; P:inositol lipid-mediated signaling; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
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; PF00169; PH; 1.
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; SM00233; PH; 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 Cytoplasm; Endoplasmic reticulum; Endosome; Golgi apparatus; Hydrolase;
KW Lipid degradation; Lipid metabolism; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Repeat.
FT CHAIN 1..1036
FT /note="Phospholipase D1"
FT /id="PRO_0000218801"
FT DOMAIN 81..212
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 219..328
FT /note="PH"
FT DOMAIN 459..486
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 853..880
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT REGION 463..890
FT /note="Catalytic"
FT MOD_RES 499
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70496"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13393"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13393"
FT LIPID 240
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 241
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1036 AA; 119515 MW; 342A561E2BBFE51E CRC64;
MSLKSEHRVN TSALQKIAAD MSNLIDNLDT RELHFEGEEV EFDTSPGDPK AQEKYIPFSS
IYNTQGFKEP NIQTYLSGCP IKAQVLEVER FTSTTRVPSI NLYTIELTHG EFTWQVKRKF
KHFQEFHREL LKYKAFIRIP IPTKRHTFRR QNVKEEPREM PSLPRSSENT IQEEQFFGRR
KQLEDYLTKI LKMPMYRNYH ATTEFLDVSQ LSFIHDLGPK GLEGMIMKRS GGHRIPGLNC
CGQGRACYRW SKRWLIVKDS FLLYMKPDSG AIAFVLLVDK EFRIKVGRKE TETKYGLRID
NLSRTLILKC NSYRHARWWG GAIEEFIQKH GSDFLKDHRF GSYAAVHENM LAKWYVNAKG
YFEDIANAME EAAEEIFITD WWLSPEIFLK RPVVEGNRWR LDCILKRKAQ QGVRIFIMLY
KEVELALGIN SEYSKRTLMR LHPNIKVMRH PDHVSSSVYL WAHHEKLVII DQSVAFVGGI
DLAYGRWDDN EHRLTDVGSV KRVTSGLSMG SLAAATMESM ESLSLKDNHR SHKNEPILKS
VDDVDPKLKG VGKPRKFSKF SLYRQLHRRH LHNSDSVSSI DSASNTGSIR SVQTGVGELH
GETRFWHGKD YCNFVFKDWV QLDKPFADFI DRYSTPRIPW HDIGSVLHGK AARDVARHFI
QRWNFTKIMK PKYRSLSYPF LLPKSQSTAH ELRYQVPGAV PAKVQLLRSA ADWSAGIKHH
EESIHSAYIN VIENSKHYIY IENQFFISCA DDKVVFNKVG DAIAQRILKA HREGQRYRVY
IVIPRLPGFE GDISTGGGNA LQAIMHFNYR TMCRGENSIL GQLKPELGNQ WINYISFCGL
RTHAELEGNL VTELIYVHSK LLIADDNTVI IGSANINDRS MLGKRDSEMA VIVQDTETVP
SIMDGKEYQA GCFAQGLRLQ CFRLVLGYLS DPSEDLQDPV SDKFFKEIWV STAARNATIY
DKVFRCLPND EVHNLMQLRD FISKPILAKD DPIRAEEELR KIRGFLVQFP FYFLSEENLL
PSVGTKEAIV PMEVWT
