ID A0A6I9YCC0_9SAUR Unreviewed; 576 AA.
AC A0A6I9YCC0;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 18-JUN-2025, entry version 23.
DE RecName: Full=Phospholipase D1 {ECO:0000256|ARBA:ARBA00074658};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
DE AltName: Full=Choline phosphatase 1 {ECO:0000256|ARBA:ARBA00042228};
DE AltName: Full=Phosphatidylcholine-hydrolyzing phospholipase D1 {ECO:0000256|ARBA:ARBA00079280};
GN Name=LOC106548779 {ECO:0000313|RefSeq:XP_013921704.1};
OS Thamnophis sirtalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Colubridae; Natricinae; Thamnophis.
OX NCBI_TaxID=35019 {ECO:0000313|Proteomes:UP000504617, ECO:0000313|RefSeq:XP_013921704.1};
RN [1] {ECO:0000313|RefSeq:XP_013921704.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- SUBUNIT: Interacts with PIP5K1B. {ECO:0000256|ARBA:ARBA00065403}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000256|ARBA:ARBA00004556}. Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00037811}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00037811}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00037811}. Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004444}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004444}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004444}. Late endosome membrane
CC {ECO:0000256|ARBA:ARBA00004577}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004577}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004577}.
CC -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|ARBA:ARBA00008664}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_013921704.1; XM_014066229.1.
DR AlphaFoldDB; A0A6I9YCC0; -.
DR GeneID; 106548779; -.
DR KEGG; tsr:106548779; -.
DR OrthoDB; 14911at2759; -.
DR Proteomes; UP000504617; Unplaced.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:TreeGrafter.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:TreeGrafter.
DR GO; GO:0032534; P:regulation of microvillus assembly; IEA:TreeGrafter.
DR GO; GO:0060627; P:regulation of vesicle-mediated transport; IEA:TreeGrafter.
DR CDD; cd01254; PH_PLD; 1.
DR FunFam; 2.30.29.30:FF:000114; Phospholipase; 1.
DR FunFam; 3.30.1520.10:FF:000021; Phospholipase; 1.
DR FunFam; 3.30.870.10:FF:000005; Phospholipase; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
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; PHOSPHOLIPASE D; 1.
DR PANTHER; PTHR18896:SF57; PHOSPHOLIPASE D1; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00614; PLDc; 1.
DR Pfam; PF00787; PX; 1.
DR PIRSF; PIRSF009376; Phospholipase_D_euk; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00155; PLDc; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50035; PLD; 1.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000504617};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 79..211
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 458..485
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT NON_TER 576
FT /evidence="ECO:0000313|RefSeq:XP_013921704.1"
SQ SEQUENCE 576 AA; 66734 MW; 38FB6F169E563DA0 CRC64;
MSLTNRRQVN TSSLKKIAAD MSNLIESLDS RELHFEGEEL DSDVVHDPKA PVGIPFSAIY
NTKGFKEPQV QLYLSGCPIR VRVLEVERFT STTKVPSPRV YTIELTHGEF TWQVKRKYKH
FQELHRELLR YKAFIRLPIP TRRHTVRRQT VKREEARQIP SLPRTSENMV RDDHLSSRRK
QLEDYVANLL KMPLYKNYHG TMEFLGVSQL SFIHDLGPKG IEGMIMKRSG GHRIPGLNCC
GQGRLCYRWS KRWLVVKDSF LLYMKPDSGA VSFVLLVDKE FSIKIGKKET ETKYGLRIDN
LSRSLILKCN SYRHALWWGQ GIEEFVQKNG KNFLKHHRFG SYAAIQENTL AKWYVNAKGY
FEDIANAMEA AKEEIFITDW WLSPEIFMKR PVVEGNRWRL DCILRRKAQQ GVRIFVILYK
EVELALGINS EYTKRTLMRL HPNIKVMRHP DHVSSTVYLW AHHEKLVIID QSVAFVGGID
LAYGRWDDNE HRLTDVGSVK RITANKSESS VNLSSLAETV QPQVETPVTT PLQGCSDDAQ
EISRMKGVGR TKKFVRFSIY KQLHRHTMHR ADSVSS
//
