ID A0A1S2ZE28_ERIEU Unreviewed; 1069 AA.
AC A0A1S2ZE28;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN Name=PLD1 {ECO:0000313|RefSeq:XP_007517972.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007517972.1};
RN [1] {ECO:0000313|RefSeq:XP_007517972.1}
RP IDENTIFICATION.
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_007517972.1; XM_007517910.2.
DR AlphaFoldDB; A0A1S2ZE28; -.
DR STRING; 9365.ENSEEUP00000009316; -.
DR CTD; 5337; -.
DR eggNOG; KOG1329; Eukaryota.
DR InParanoid; A0A1S2ZE28; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000079721; 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 CDD; cd09842; PLDc_vPLD1_1; 1.
DR CDD; cd09844; PLDc_vPLD1_2; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
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:UP000079721}.
FT DOMAIN 81..212
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 219..328
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 459..486
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 886..913
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 149..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1069 AA; 122606 MW; 6800F3522AC97D8C CRC64;
MSLKQGPQVN TAALQRIAAD MSHLIENLDT RELHFEGDEV EYDLPPGEAK AQEGNIPFSA
IYETQGFKEL NLKTYLSGCP IMARVLGVER FTSASKAHSI NLYTIELTHG EFKWQVKRKF
KHFEEFHREL LKYKAFIRIP IPTKRHTFRR QHVKEEPREM PSLPRASENM NREEQFLGKR
KQLEDYLTKL LKMPMYKNYH ATTEFLDISQ LSFIHDLGPK GIEGMIMKRS GGHRIPGLNC
CGHGSACYRW SKRWLVVKDS FLLYMKPDNG AIAFVLLVDK EFRIKVGKKE TETKYGLRID
NLSRTLILKC NSYRHARLWG GAIEEFIQKH GSNFLKDHRF GSFAAVQENT LAKWYVNARG
YFEDVANAME EAQEEIFITD WWLSPEIFLK RPVVEGNRWR LDCILKRKAQ QGVRIFVMLY
KEVELALGIN SEYSKRTLMR LHPNIKVMRH PDHVSSTVYL WAHHEKLVVV DQSLAFVGGI
DLAYGRWDDH EHRLTDVGSV KRVAMGPSLS AETIGSLESL SLKDDSSKPL PTLKGVDGVD
SKLRGIGKPS KFSKFSLYQQ LHRHHLRTAE SVSSIDSVSS YGYHCRSRQS LIHGFKPHLR
LFHSPSASEQ GLCDPTGDAS SIHSVQTGIG DLHGETRFWH GKDYCNFVFK DWVQLDKPFA
DFIDRHSTPR MPWHDIASAV HGKAARDVAR HFIQRWNFTK IMKSKYRSLS YPFLLPKSQT
TAHELKYQVP GSVLANVQLL RSATDWSAGI KYHEESIHTA YVSVIENSKH YIYIENQFFI
SCADDKVVFN KVGDAIAQRI LKAHRENQRY RVYVVIPLLP GFEGDISTGG GNALQAIMHF
NYRTMCRGEN SILGQLKAEL GNQWINYISF CGLRTHAELE GNLVTELIYV HSKLLIADDN
TVIIGSANIN DRSLLGRRDS EMAIIVQDTE TVPSRMDSED YQAGRFAQGL RLQCFRLVLG
YLSEPSEDIQ DPVSDKFFKE VWVSTAARNA TIYDKVFRCL PSDEVHNLMQ LRDFISKPIL
AKEDPVRAEE ELRKIRGFLV QFPFYFLAEE SLLPSVGTKE AMVPMEVWT
//
