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Database: UniProt
Entry: A0A9J8BVD0_CYPCA
LinkDB: A0A9J8BVD0_CYPCA
Original site: A0A9J8BVD0_CYPCA 
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
//
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