ID A0A9J8BVD0_CYPCA Unreviewed; 968 AA.
AC A0A9J8BVD0;
DT 28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 1.
DT 18-JUN-2025, entry version 12.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
OS Cyprinus carpio carpio.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Cyprinus.
OX NCBI_TaxID=630221 {ECO:0000313|Ensembl:ENSCCRP00000160573.1, ECO:0000313|Proteomes:UP001108240};
RN [1] {ECO:0000313|Ensembl:ENSCCRP00000160573.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) 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 -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000256|ARBA:ARBA00037868}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00037868}.
CC -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|ARBA:ARBA00008664, ECO:0000256|PIRNR:PIRNR009376}.
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DR Ensembl; ENSCCRT00000116327.1; ENSCCRP00000160573.1; ENSCCRG00000033262.2.
DR GeneTree; ENSGT00940000155015; -.
DR Proteomes; UP001108240; Unplaced.
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-UniRule.
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; 3.30.870.10:FF:000005; Phospholipase; 1.
DR FunFam; 3.30.870.10:FF:000018; Phospholipase; 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; 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 PIRSF; PIRSF009376; Phospholipase_D_euk; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00155; PLDc; 2.
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.
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:ARBA00023098};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP001108240};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 167..276
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 407..434
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 785..812
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 968 AA; 112043 MW; E321B2F4B5EAF49A CRC64;
RVLNMLPDMS DTVENLDTRD LGFSDAEDEP EEVDCEFNPS GASRIPFSAV YRTVGFKETE
AEVYLTAAPI TAKILDVERF TSAPGLFKIE LKHGNFTWIV KRKEKHFMEL HRELLRYKTL
MRIPLPTRRS DPYYLNKLLR MAMYRKYYAT TCFNLLHEIH FCSYKPVSFR EGIVYKRSGG
HRIPGMNCCG HNEVCYRWSK RWLIVKDSFL LYMKPDTGAI SFVLLVDNEF TIKMDSKNTD
TKHGLRIENL SRKLVLKFTS YRHARWWGQA IESFVRKHGK AFLRTHRFGS FAREEENIPS
KWYVNGKTYM EDVANALEEA KEEIFITDWW LSPEIFLKRP VVEGNRWRLD CILKRKAQQG
VRIFVMLYKE VELALGINSE YSKRTLKHLH PNIKVMRHPD HVSSSVYLWA HHEKIVVIDQ
SVAFVGGIDL AYGRWDDREH RLTDVGSVTR SVAQTMEQLA ILDCDFIRSM AGDSMDLPKL
KGIGRTRKTR FSLYHHIQRG LHHAESISSI DSTNSKRLFP DQTETDHSGS MHSLQTGVGE
LMGNTRFWHG KDYCNFVYKD WVRLDKPFDD FIDRYTTPRM PWHDISSVVH GKAARDVARH
FIQRWNFTKI MKPKYRSLSY PFLLPKSHST ANDLKYQVPD CVQTKVQVLR SAADWSAGIK
HHEESIHNAY IQVIAKSKHF IYIENQFFIS CADNKHVYNK IGDAIIERII RAHKEKKPFR
VYVVTPLLPG FEGDISTGGG SALQAQKKKT KKGQLRSDMD DQWMNYISIC GLRTHAELQG
RLVTELIYVH SKLLIADDNT VIIGSANIND RSMLGKRDSE VAVIFEDSET TPSVMDGQEY
QAGKFALQLR LECFKTILGA FDDPTIDVSD PISNGFYKDV WMSISGRNAT IYEKVFRCLP
SSLVRNKQEL MSFQFKPGLD KEDPVKAQEL LKKIRGFLIQ FPLEFLCEEN LMPSVGTKEA
MVPTEIWT
//