ID A0A2D0R7H1_ICTPU Unreviewed; 899 AA.
AC A0A2D0R7H1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN Name=si:ch211-168k14.2 {ECO:0000313|RefSeq:XP_017325770.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017325770.1};
RN [1] {ECO:0000313|RefSeq:XP_017325770.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017325770.1};
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_017325770.1; XM_017470281.3.
DR AlphaFoldDB; A0A2D0R7H1; -.
DR GeneID; 108266656; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000221080; Chromosome 6.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd09138; PLDc_vPLD1_2_yPLD_like_1; 1.
DR CDD; cd06895; PX_PLD; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 3.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
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:SF202; PHOSPHOLIPASE; 1.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR Pfam; PF00614; PLDc; 1.
DR Pfam; PF00787; PX; 1.
DR PIRSF; PIRSF009376; Phospholipase_D_euk; 1.
DR SMART; SM00155; PLDc; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 3.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50035; PLD; 1.
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}; Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 865..890
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 75..210
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 457..484
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 494..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 899 AA; 102867 MW; 2C8F9F5B7F4C0F72 CRC64;
MAVCQKSFRL ERLESDTSGF SASLDHDDLQ DNSEELDVDR CDASLRESRT NPFQAIYSFL
PFKSLDCKVF LDDVPILVQV TEVDRVTYAR VLNPNLYTIE LRYGNFTWKI KRRFKHFQML
HQELLKFKAL LRIPLPSRIH SVKRRSFEGH SRSRTGHMPT LPRRPDALVR EEQLMSRKMR
LEDYLKNILK KTLYRNHPAT LEFLEVSQIS FIKELGPKGI EGMILKKSGG NTFPVCYWCG
SNSVCYRWSK RWLVVKDSFV LYMKPKDGQV GTVILYDKGF HIQIGSEETG VRHGVTIENL
CRALTIKCST YRQARWWGHS IDEFVQRFGQ DFLRENRHGS FAPVRENTKA QWFVNAAGYF
DAIADALEGA KEEIFITAWW LSPEIFLKRP VVDGNTWRLD HVLKRKAEQG VKICVLLYKE
VEVILGLNSE YTKKTLTGLH SNIMVIRHPD HVPSTSLLWA HHEKSVVIDQ SLAFLGGIDL
AYGRWDDSQH RLTDVGSVRR SPQASPAVSP ELTRESVGVS EEDKALKFSS VMEEEVLGGE
AAGETCSVEE RAETSSNLTL PVSRSYVAAA EDKSSSEGTE FKHCNSRSSV SSRSLLVPEW
YSKSLFLRST DSYSMGLHHF HLLPHDTSSL RSHISSTELC GETRFWHGKD YCNFILKDWV
KLNKPFDDFI DRYKTPRMPW HDVGVVVHGK AARDIARHFI QRWNFTKLVK KRSGATCYPC
LVPKSLCEPS KPPEPWGKHT QANVQVLRSV CQWSIGTKVH EESIHLAYIS AIQNSKHFIY
IENQFFISCS DKTIRNSIGD ALTERILRAY REKKKFRVYV VMPLLPGFEG DISSGGGQAI
KAIMHFNYRT TCRGEHSIID RLKCWLTAGS TTSLSVVYAL MLIWMAVWLL SSSMCTASS
//
