ID A0A3Q2G0U3_CYPVA Unreviewed; 966 AA.
AC A0A3Q2G0U3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000015180.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000015180.1}
RP IDENTIFICATION.
RG Ensembl;
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 AlphaFoldDB; A0A3Q2G0U3; -.
DR Ensembl; ENSCVAT00000023196.1; ENSCVAP00000015180.1; ENSCVAG00000018834.1.
DR GeneTree; ENSGT00940000155015; -.
DR OMA; ILYWAHH; -.
DR Proteomes; UP000265020; Unplaced.
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; 2.
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; 3.
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:UP000265020}.
FT DOMAIN 56..189
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 196..305
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 436..463
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 783..810
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 121..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 966 AA; 111152 MW; A43F675F4ADD4DE5 CRC64;
MLGKDQPTTT SDTYDGDCRI PFSAVYGTVG FREANARVYL PTVPITAKIL EVERFTTAQD
RFNLSQHRSV NKSLPAVFKI EMKHGEFTWL VKRKEKHFLE LHREMRTYKT LMRIPLPSRS
HTVRRKTMRK SEVREMPSLP RGGGDDLVRD EQVSSRRRQL EDYLNTLLKM AMYRKYHHTM
EFIDVSQLSF IHDLGPKGLE GMIYKRSGGH RIPGMNCCGQ GQACYRWSKR WLVVKDSFLL
YMKPDSGAIS FVVLVDKEFS IKMDSKDTET QHGVRIDSLS RTLVFKCTSY RHARWWGQSI
ESFVRSHGKA FLREHRFGSF AQEQENVPAK WYVNGKTYME DVADALEEAK EEIFITDWWL
SPEIFLKRPV VEGNRWRLDC ILKRKAQMGV RIFVMLYKEV ELALGINSGY SKRTLMHLHP
NIKVMRHPDH VSSSVYLWAH HEKIVVIDQS VAFVGGIDLA YGRWDDTEHR LTDVGSVTRS
VALEQVSVST GDGVSQSNGR GTPPADSMEL PKLKGVGRSR MVRFSLYRHL QKHTMQHVDS
VSSVDSTDSG SVKSLKTGVG ELQGNTRFWH GKDYCNFVYK DWIQLEKPFD DFIDRYTTPR
MPWHDIASVV HGRGARDVAR HFIQRWNFTK IMKPKYRSLS YPFLLPKSHS TADELKYQVP
GKVKHLCGCY RFNQFFISCA DNRTVYNKIG DAIIERIIRA HKEGKKYRVY VVTPLLPGFE
GDITTGGGNA IQAVMHFNYR TMIRGEHSII SQLKKEMDDQ WMNYISFAGL RTHAELEGRL
VTELIYVHSK MLIADDNTVI IGSANINDRS MLGKRDSEVA VIVEDCEKVA SVMDGQEYQA
GSYALELRLE CFRTILGGHT DSSIDLSDPV SDRFYKEVWM TTAGRNATIY EKVFRCLPSS
LVRNMSELEQ FQSKPGLAQT DKTRAQEELR KIRGFLVQFP LDFLSEHNLM PSVGTKEAMV
PTEIWT
//
