ID A0A3P8Y5M6_ESOLU Unreviewed; 1035 AA.
AC A0A3P8Y5M6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN Name=PLD1 {ECO:0000313|Ensembl:ENSELUP00000011320.2};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000011320.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000011320.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000011320.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A3P8Y5M6; -.
DR STRING; 8010.ENSELUP00000011320; -.
DR Ensembl; ENSELUT00000000659.2; ENSELUP00000011320.2; ENSELUG00000011706.2.
DR GeneTree; ENSGT00940000155015; -.
DR Proteomes; UP000265140; LG21.
DR Bgee; ENSELUG00000011706; Expressed in head kidney and 14 other cell types or tissues.
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: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 CDD; cd01254; PH_PLD; 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:UP000265140}.
FT DOMAIN 85..218
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 225..334
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 465..492
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 852..879
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 1035 AA; 118697 MW; 3408210681A29572 CRC64;
MHHPSNPTSS TLHLVAADMS EIMENLDTRE LDLADGEYDT TDSKPPEERQ GFASIYNTVG
FKEAEGKVFL SSPITAKILA VERFTSAQDR FNITTQRSVN KSLPAVFKIE LRHGEFVWVV
KRKEKHFMEL HRELLRYKTF MRIPLPSRSH TVKRHSVYKS EIRAMPNLPR GGGDELVREE
QVSSRRKALE DYLNKLLKMP MYKNYHATME FIDVSQLSFI HDLGPKGLEG MVHKRSGGHR
IPGLNCCGHS KMCYRWSKRW LVVKDSFLLY MKPDTGSISF VLLVDKEFSI KMDSKDTETQ
HGVRIDTLSR SLVLKFNSYR HARWWGQAIE GFVKKHGSAF LTDHRFGSFA SPKHNIPAKW
YVNGKTYMED VADALEESKE EIFITDWWLS PEIFMKRPVV EGNRWRLDYI LRRKAQQGVR
IFVMLYKEVE LALGINSEYS KRTLMHLHPN VKVMRHPDHV SSSVYLWAHH EKIVVIDQSV
AFVGGIDLAY GRWDDREHRL TDVGSVTRSV ALEQVEGPPL NNGLAPSNGH GAASMVTDSM
DQPKLKGQGR IRRSRFSLKR HLQKHVLAHA DSDSVESLEE KTGSVQSLQT EVGGVGELVG
NTRFWHGKDY CNFVYKDWIQ LDKPFDDFID RHTHPRMPWH DMGSVVHGTA ARDVARHFIQ
RWNFCKIMKP KYRSLSYPYL LPKSHTTAGE IRYQVPGCIP ANVQILRSAS DWSAGIKYPE
ESIHNAYVHA IKASQHYIYI ENQFFISCAD NKHVFNKIGD AIAERIIKAY REGKRFRVYV
VTPLLPGFEG DINTGGGSAI QAVMHYNYRT MIRGDCSITS QLKREMDDQW MNYISFAGLR
THAELEGRLV TELIYVHSKM LIVDDNTVII GSANINDRSM LGKRDSEVAV VVEDSETVAS
VMDGQKYQAG RYALTLRLEC FRTILGAHND LTIDVSDPVS DHFYKDIWMT TCARNATIYQ
KVFRCLPSSD VRSILELEGY LAKPGLERED PTRAHEELKK IRGFLVQFPL YFLSEQNLLP
PIGSKEAMVP MEVWT
//
