ID A0A2U4C889_TURTR Unreviewed; 1074 AA.
AC A0A2U4C889;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 2.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN Name=PLD1 {ECO:0000313|RefSeq:XP_019801667.2,
GN ECO:0000313|RefSeq:XP_033711362.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019801667.2};
RN [1] {ECO:0000313|RefSeq:XP_019801667.2, ECO:0000313|RefSeq:XP_033711362.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_019801667.2,
RC ECO:0000313|RefSeq:XP_033711362.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|PIRNR:PIRNR009376};
CC -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|ARBA:ARBA00008664, ECO:0000256|PIRNR:PIRNR009376}.
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DR RefSeq; XP_019801667.2; XM_019946108.2.
DR RefSeq; XP_033711362.1; XM_033855471.1.
DR STRING; 9739.ENSTTRP00000004926; -.
DR Ensembl; ENSTTRT00000005222; ENSTTRP00000004926; ENSTTRG00000005218.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000245320; Chromosome 4.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0098981; C:cholinergic synapse; IEA:Ensembl.
DR GO; GO:0030139; C:endocytic vesicle; IEA:Ensembl.
DR GO; GO:0005768; C:endosome; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-UniRule.
DR GO; GO:0031670; P:cellular response to nutrient; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; 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 GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl.
DR GO; GO:0032534; P:regulation of microvillus assembly; IEA:Ensembl.
DR GO; GO:0098693; P:regulation of synaptic vesicle cycle; IEA:Ensembl.
DR CDD; cd01254; PH_PLD; 1.
DR CDD; cd09842; PLDc_vPLD1_1; 1.
DR CDD; cd09844; PLDc_vPLD1_2; 1.
DR CDD; cd07296; PX_PLD1; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 3.
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; 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; PHOSPHOLIPASE D; 1.
DR PANTHER; PTHR18896:SF57; PHOSPHOLIPASE D1; 1.
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; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50035; PLD; 2.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR009376};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR009376};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR009376};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Reference proteome {ECO:0000313|Proteomes:UP000245320}.
FT DOMAIN 81..212
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 219..328
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 459..486
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 891..918
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 1074 AA; 123971 MW; 3CCBB530DC336AD7 CRC64;
MSLKDEPRVN TSALQKIAAD MSNLIENLDT RELHFEGEEV DYEVSPSDPR IREVYIPFSA
IYKTQGFKEP NTQTYLSGCP IKVQVLEVER LTSTKRVPSI NLYTIELTHG EFKWQVKRKF
KHFQEFHREL LKYKAFIRIP IPTKRHTFRR QNVKEEPREM PSLPRSSENM IREEQLFGRR
KQLEDYLTKL LKMPMYRNYH ATTEFLDISQ LSFIHDLGPK GIEGMIMKRS GGHRIPGLNC
CGQGRACYRW SKRWLIVKDS FLLYMKPDSG AIAFVLLVDK EFRVKVGKKE TETKYGLRID
NLSRTLILKC NSYRHARWWG GAIEEFIHKH GPNFLKDHRF GSYAAIQENT LAKWYVNAKG
YFEDVANAME EAKEEIFITD WWLSPEIFLK RPVVEGNRWR LDCILKRKAQ QGVRIFIMLY
KEVELALGIN SEYSKRTLMH LHPNIKVMRH PDHVSSSVYL WAHHEKLIII DQSVAFVGGI
DLAYGRWDDN EHRLTDVGSV KRVIGAPSLV SLTAETTESM ESLCLKDKNE SNKNLPVLKT
VDDADSKLKG IGKPRKFSRF SLYRQLHRHH LRSTDSISSI DSASSDYNHC RSRQNLIHGL
KPHLKFFRSS SESEQGLTRP NVDTGSIQSL QTGVGELHGE TRFWHGKDYC NFVFKDWVQL
DKPFADFIDR HSTPRMPWHD IASVVHGKAA RDVARHFIQR WNFTKIMKPK YRSLSYPFLL
PKSQTTAHEL KHQVPGSVHA NVQLLRSAAD WSAGIKYHEE SIHAAYVYVI ENSKHYIYIE
NQFFISCSDD KVVFNKVGDA IAQRILKAHR ESQRYRVYVV IPLLPGFEGD ISTGGGNALQ
AIMHFNYRTM CRGENSILGQ LKAEIGNQWI NYISFCGLRT HAELEGNLVT ELVYVHSKLL
IADDNTVIIG SANINDRSML GKRDSEMAVI VQDTETVPSV MDGKEYQAGH FALGLRLQCF
RVVLGYLSGP SEDIQDPVSD KFFKEVWVST AARNATIYDK VFRCLPNDEV HNLIQLRDFI
SKPILAKEDP IRAEEELKKI RGFLVQFPFY FLSEENLLPS VGTKEAMVPT EVWT
//
