ID A0A2Y9L3K3_ENHLU Unreviewed; 933 AA.
AC A0A2Y9L3K3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN Name=LOC111161193 {ECO:0000313|RefSeq:XP_022380476.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022380476.1};
RN [1] {ECO:0000313|RefSeq:XP_022380476.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022380476.1};
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_022380476.1; XM_022524768.1.
DR AlphaFoldDB; A0A2Y9L3K3; -.
DR STRING; 391180.A0A2Y9L3K3; -.
DR KEGG; elk:111161193; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000248482; 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; 2.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
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:SF121; PHOSPHOLIPASE D2; 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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000248482}.
FT DOMAIN 65..195
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 437..464
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 751..778
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..494
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 933 AA; 105833 MW; CA7CCCB903ED36D6 CRC64;
MAATPASLFP SGGDLDSSQL HMEPDELDTL KEGEDPADRM HPFLAIYDLQ PLKMRPLVFA
PGVPVTAQVV GTERYTSGSK VGTCTLYSVR LTHGAFTWTT KKKFRHFQEL HRDLLRHKVL
MSLLPLARFG AAHPPAREAA DREIPSLPRV APEGSSRHAS SKQKYLENYL NRLLTMSFYR
NYHAMTEFLE VSRLSFIPDL GSKGLEGVIR KRSGGHRVPG LTCCGRDQVC YRWSKRWLVV
KDSFLLYMCL ETGAISFVQL FDPGFEVRVG KRSTEARYGV RIDTSHRSLI LKCGSYRQAR
WWGQEITELA QGPGRDFIQL HRHDSYAPPR PGTLARWFVN GAGYFAAVAD AILQAQEEIF
ITDWWLSPEI YLKRPAHSDD WRLDIMLKRK AEEGVRVSVL LFKEVELALG INSGYSKRAL
MLLHHNIKVM RHPDQVTLWA HHEKLLVVDQ VVAFLGGLDL AYGRWDDLHY RLTDLGDPSR
PAAPKPPPPG SDSPGSPDLS QNQLFWLGKD YSNLITKDWV QLDRPFEDFI DRETMPRMPW
RDVGVAVHGL PARDLARHFI QRWNFTKMTK AKYKTPMYPY LLPKSTSTAD QLPFTLPGGQ
CTTVQVLRSV DRWSAGTLEN SILNAYLHTI RESQHFLYIE NQFFISCSDG RTVFNKVGDE
IVDRILKAHK HGQCFRVYVL LPLLPGFQGD ITTGGGNSIQ AILHFTYRTL CRGEYSILHR
LKAAMGTAWR DYMSICGLRT HGELGGHPVS ELIYIHSKML IADDRTVIIG SANINDRSLL
GKRDSELAVL IQDTEMEPSL MDGREYQAGR FALSLRKHCF SVILGADARP DLDLQDPVCD
DFFQLWQDTA ENNANIYEQI FRCLPSNATR SLRALREYVA AEPLATVSPP LARSELTQVQ
GHLVHFPLKF LEEENLLPPL GSKEGMMPLE VWT
//
