ID A0A3Q3FP41_9LABR Unreviewed; 1038 AA.
AC A0A3Q3FP41;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN Name=PLD1 {ECO:0000313|Ensembl:ENSLBEP00000021254.1};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000021254.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000021254.1}
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; A0A3Q3FP41; -.
DR STRING; 56723.ENSLBEP00000021254; -.
DR Ensembl; ENSLBET00000022389.1; ENSLBEP00000021254.1; ENSLBEG00000016081.1.
DR GeneTree; ENSGT00940000155015; -.
DR InParanoid; A0A3Q3FP41; -.
DR Proteomes; UP000261660; 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; 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:UP000261660}.
FT DOMAIN 88..220
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 227..336
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 467..494
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 855..882
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 570..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..590
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1038 AA; 118577 MW; 844F59CF400EB2CA CRC64;
MLRQSDPNSS TLQLVANDMT DIMEKLDTHE LDLEDGEYDT TDTTTPGECA DHLPFTAIYK
TVGFKESRAQ VFLSSPITAK ILEVERFTSA QDRFNVTTQR SINKSMPAVF KIELKHGEFT
WLVKRKEKHF MDLHRELRTY KTFMKLPLPT RSHTVKRQSA AEGVRHMPTL HRGRGDELGR
EEQVSSRRKQ LEDYLNNLLK VPMYRNYHAT MEFIDVSQLS FIHDLGPKGL EGMVQKRSGG
HRVPGMNCCG RSKMCYHWSK RWLVVKDSFL LYMKPDSGAI SFVMLVDKEF SIKMDSRDTE
TKHGVRIDSL SRSLLLKCSS YRHARWWGQA IEGFVQKHGS AFLTDHRFGS FAREEVNIPA
KWYVNGKTYM EDVADALEAA KEEIFITDWW LSPEIFLKRP VVEGNRWRLD SILKRKAEQG
VHIFVILYKE VELALGINSG YSKRTLRHLH PNIKVMRNPD HVSSAVYLWA HHEKIIIVDQ
SVAFVGGIDL AYGRWDDREH RLTDVGSVTL SHLEQAEAVA PNMAAPANGS GGVSQRNGNG
VFTVTDSVDQ PKLKGQGRLK RTRFSIKRHL QKHGLASADS DSDLEDEAKS GSVRSLQTGV
GELFGNTRFW HGKDYCNFVH KDWIQLDKPF DDFIDRHTTP RMPWHDISSV VHGKAARDVA
RHFIQRWNFT KLVKPKYNSP SFPCLLPKSH TTAGEQRYQV PNCIPAKVQI LRSACDWSAG
IKYHEESIHN AYVHAIEKSE HFVYIENQFF ISCADNRQVF NKIGDTIAER IIKAYREGKR
YRVYVVTPLL PGFEGDINTG GGSAIQAVMH FNYSVCRDHS IISQLKREMG DNWMNYISIA
GLRTHAELEG KLVTELIYVH SKMLIADDNT VIIGSANIND RSMLGKRDSE VAVIVEDSEM
VTAVMDGQEY QAGKYALQLR LECFKMILGA HTDPSIDVSD PISDQFYKEV WMATCARNAT
IYQKVFRSLP SSDVRNIFEL EGFLAKPGLD KEDPNKAREE LKKIRGFLVQ FPLQFLCEQN
LLPPMGSKEA MVPMEVWT
//
