ID A0A3Q0GD75_ALLSI Unreviewed; 1062 AA.
AC A0A3Q0GD75;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-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|RefSeq:XP_025057559.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_025057559.1};
RN [1] {ECO:0000313|RefSeq:XP_025057559.1}
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_025057559.1; XM_025201774.1.
DR AlphaFoldDB; A0A3Q0GD75; -.
DR Proteomes; UP000189705; 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; cd07296; PX_PLD1; 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; 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; PF00787; PX; 1.
DR PIRSF; PIRSF009376; Phospholipase_D_euk; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00155; PLDc; 1.
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; 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};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Reference proteome {ECO:0000313|Proteomes:UP000189705}.
FT DOMAIN 79..211
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 458..485
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 148..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1062 AA; 122560 MW; 63CBA1B1ED1AECB9 CRC64;
MSLKREKPVD TSTLKKIAAD MSNIIESLDT RELHFEGEEV DSDVLNEPKT PAGIPFSTIY
NTQGFKEPHI QTFLTGCPIR VRVLEVERFT STTKVPSPNV YTIELTHGEF TWQVKRKFKH
FQEFHRELLR YKAFIRIPIP IRSHTVRRQS IKRGETRQMP SLPRTSENMV REEHFSSRRK
QLEDYLTKIL KMPMYRNYHG TMEFIGVSQL SFIHDLGPKG IEGMIMKRSG GHRIPGLNCC
GQGSVCYRWS KRWLVVKDSF LLYMKPDSGA IAFVLLVDKE FKIKIGKKET ETKYGLQIDN
LSRSLILKCN SYRHARWWGQ GIEEFIQKNG QNFLKDHRFG SYAAVREKTL AKWYVNAKWY
FEDVANAMEA AKEEIFITDW WLSPEIFMKR PVVEGNRWRL DCILKRKAQQ GVKIFVMLYK
EVELALGINS EYSKRTLMRL HPNIKVMRHP DHVSSSVYLW AHHEKLVIID QSVAFIGGID
LAYGRWDDDE HRLTDVGSVK RISGTKSTMN LAAAAESTEA LALKPYTDSP GDRKSLDDAL
DSSRLKGIGK ARKFARFSIY RQLHKHGIHH SDSVSSIDSE SSYCNPSRSQ QNLIQSLKPH
LKMFHHHTES RQGLAESEKD KGSIRSLKTG VGELFGETRF WHGKDYCNFV FKDWVQLDKP
FADFIDRHTT PRMPWHDIAS VVHGKAARDI ARHFIQRWNF AKIMKPKYRS LSYPFLLPKS
QQTANELKYQ VPESVLATVQ IPMLFLPYPQ ELDLLSNFLS KEYKVPSSCF SLFVRQVLRS
AADWSAGIKY HEESIHAAYV NVIENSKHFI YIENQFFISC ADDRVVSNKI GDAIAQRILK
AHRENKRFRV YVVIPLLPGF EGDILTGGGN ALQAIMHFNY RTMCRGDRSI LGQLKTESSA
NINDRSLLGK RDSEMAILVQ DTETVPSMMD GEDYRAGKFA QSLRLRCFRV VLGCSTNQNV
DLLDPVCDRF FKEMWVSTAA RNATIFDKVF RCLPSDEVNN LVQLRDFINR PILANEDPVK
AAEELKKIHG FLVQFPFRFL EEENLLPSVG TKESMVPMEV WT
//
