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Phospholipase D1 (PLD 1) (hPLD1) (EC 3.1.4.4) (Choline phosphatase 1) (Phosphatidylcholine-hydrolyzing phospholipase D1)

 PLD1_HUMAN              Reviewed;        1074 AA.
Q13393;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
22-NOV-2017, entry version 178.
RecName: Full=Phospholipase D1;
Short=PLD 1;
Short=hPLD1;
EC=3.1.4.4;
AltName: Full=Choline phosphatase 1;
AltName: Full=Phosphatidylcholine-hydrolyzing phospholipase D1;
Name=PLD1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PLD1A).
PubMed=8530346; DOI=10.1074/jbc.270.50.29640;
Hammond S.M., Altshuller Y.M., Sung T.-C., Rudge S.A., Rose K.,
Engebrecht J., Morris A.J., Frohman M.A.;
"Human ADP-ribosylation factor-activated phosphatidylcholine-specific
phospholipase D defines a new and highly conserved gene family.";
J. Biol. Chem. 270:29640-29643(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PLD1A AND PLD1B).
PubMed=9013646; DOI=10.1074/jbc.272.6.3860;
Hammond S.M., Jenco J.M., Nakashima S., Cadwallader K., Gu Q.-M.,
Cook S., Nozawa Y., Prestwich G.D., Frohman M.A., Morris A.J.;
"Characterization of two alternately spliced forms of phospholipase
D1. Activation of the purified enzymes by phosphatidylinositol 4,5-
bisphosphate, ADP-ribosylation factor, and Rho family monomeric GTP-
binding proteins and protein kinase C-alpha.";
J. Biol. Chem. 272:3860-3868(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PLD1A; PLD1B AND PLD1C).
TISSUE=Brain, Cervix carcinoma, Chondrocyte, and Skeletal muscle;
PubMed=9761774;
Steed P.M., Clark K.L., Boyar W.C., Lasala D.J.;
"Characterization of human PLD2 and the analysis of PLD isoform splice
variants.";
FASEB J. 12:1309-1317(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PLD1A).
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 739-1074 (ISOFORM PLD1D).
Hughes W.E., Parker P.J.;
"A novel human phospholipase D1 splice variant displays conserved
regulation in vitro but altered localisation in vivo.";
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[6]
TISSUE SPECIFICITY.
PubMed=9582313; DOI=10.1074/jbc.273.21.12846;
Lopez I., Arnold R.S., Lambeth J.D.;
"Cloning and initial characterization of a human phospholipase D2
(hPLD2). ADP-ribosylation factor regulates hPLD2.";
J. Biol. Chem. 273:12846-12852(1998).
[7]
INTERACTION WITH PIP5K1B.
PubMed=11032811; DOI=10.1093/emboj/19.20.5440;
Divecha N., Roefs M., Halstead J.R., D'Andrea S., Fernandez-Borga M.,
Oomen L., Saqib K.M., Wakelam M.J.O., D'Santos C.;
"Interaction of the type Ialpha PIPkinase with phospholipase D: a role
for the local generation of phosphatidylinositol 4, 5-bisphosphate in
the regulation of PLD2 activity.";
EMBO J. 19:5440-5449(2000).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-561 AND SER-629, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[13]
INVOLVEMENT IN CVDD, AND VARIANT CVDD PRO-442.
PubMed=27799408; DOI=10.1136/jmedgenet-2016-104259;
Ta-Shma A., Zhang K., Salimova E., Zernecke A., Sieiro-Mosti D.,
Stegner D., Furtado M., Shaag A., Perles Z., Nieswandt B., Rein A.J.,
Rosenthal N., Neiman A.M., Elpeleg O.;
"Congenital valvular defects associated with deleterious mutations in
the PLD1 gene.";
J. Med. Genet. 54:278-286(2017).
-!- FUNCTION: Implicated as a critical step in numerous cellular
pathways, including signal transduction, membrane trafficking, and
the regulation of mitosis. May be involved in the regulation of
perinuclear intravesicular membrane traffic (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: A phosphatidylcholine + H(2)O = choline + a
phosphatidate.
-!- ENZYME REGULATION: Stimulated by phosphatidylinositol 4,5-
bisphosphate and phosphatidylinositol 3,4,5-trisphosphate,
activated by the phosphokinase C-alpha, by the ADP-ribosylation
factor-1 (ARF-1), and to a lesser extent by GTP-binding proteins:
RHO A, RAC-1 and CDC42. Inhibited by oleate.
-!- SUBUNIT: Interacts with PIP5K1B. {ECO:0000269|PubMed:11032811}.
-!- INTERACTION:
P23528:CFL1; NbExp=4; IntAct=EBI-2827556, EBI-352733;
Q15382:RHEB; NbExp=2; IntAct=EBI-2827556, EBI-1055287;
-!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}.
Endoplasmic reticulum membrane {ECO:0000250}; Lipid-anchor
{ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus
membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic
side {ECO:0000250}. Late endosome membrane {ECO:0000250}; Lipid-
anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=PLD1A;
IsoId=Q13393-1; Sequence=Displayed;
Name=PLD1B;
IsoId=Q13393-2; Sequence=VSP_005020;
Name=PLD1C;
IsoId=Q13393-3; Sequence=VSP_005018, VSP_005019;
Name=PLD1D;
IsoId=Q13393-4; Sequence=VSP_005021, VSP_005022;
-!- TISSUE SPECIFICITY: Expressed abundantly in the pancreas and heart
and at high levels in brain, placenta, spleen, uterus and small
intestine. {ECO:0000269|PubMed:9582313}.
-!- DISEASE: Cardiac valvular defect, developmental (CVDD)
[MIM:212093]: An autosomal recessive form of congenital heart
defects, characterized by valvular malformations involving the
pulmonic, tricuspid and mitral valves.
{ECO:0000269|PubMed:27799408}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the phospholipase D family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Phospholipase D entry;
URL="https://en.wikipedia.org/wiki/Phospholipase_D";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PLD1ID43716ch3q26.html";
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EMBL; U38545; AAB49031.1; -; mRNA.
EMBL; BC068976; AAH68976.1; -; mRNA.
EMBL; AJ276230; CAB76564.1; -; mRNA.
CCDS; CCDS3216.1; -. [Q13393-1]
CCDS; CCDS46957.1; -. [Q13393-2]
RefSeq; NP_002653.1; NM_002662.4. [Q13393-1]
RefSeq; XP_005247590.1; XM_005247533.2. [Q13393-1]
RefSeq; XP_005247591.1; XM_005247534.2. [Q13393-2]
RefSeq; XP_011511199.1; XM_011512897.1. [Q13393-4]
UniGene; Hs.382865; -.
UniGene; Hs.732969; -.
ProteinModelPortal; Q13393; -.
SMR; Q13393; -.
BioGrid; 111353; 44.
CORUM; Q13393; -.
DIP; DIP-40821N; -.
IntAct; Q13393; 17.
MINT; MINT-141519; -.
STRING; 9606.ENSP00000342793; -.
BindingDB; Q13393; -.
ChEMBL; CHEMBL2536; -.
DrugBank; DB00122; Choline.
DrugBank; DB05301; LAX-101.
DrugBank; DB09031; Miltefosine.
GuidetoPHARMACOLOGY; 1433; -.
SwissLipids; SLP:000000149; -.
iPTMnet; Q13393; -.
PhosphoSitePlus; Q13393; -.
SwissPalm; Q13393; -.
BioMuta; PLD1; -.
DMDM; 2499703; -.
EPD; Q13393; -.
MaxQB; Q13393; -.
PaxDb; Q13393; -.
PeptideAtlas; Q13393; -.
PRIDE; Q13393; -.
TopDownProteomics; Q13393-2; -. [Q13393-2]
DNASU; 5337; -.
Ensembl; ENST00000351298; ENSP00000342793; ENSG00000075651. [Q13393-1]
Ensembl; ENST00000356327; ENSP00000348681; ENSG00000075651. [Q13393-2]
GeneID; 5337; -.
KEGG; hsa:5337; -.
UCSC; uc003fhs.4; human. [Q13393-1]
CTD; 5337; -.
DisGeNET; 5337; -.
EuPathDB; HostDB:ENSG00000075651.15; -.
GeneCards; PLD1; -.
HGNC; HGNC:9067; PLD1.
HPA; CAB004527; -.
HPA; HPA042396; -.
MIM; 212093; phenotype.
MIM; 602382; gene.
neXtProt; NX_Q13393; -.
OpenTargets; ENSG00000075651; -.
PharmGKB; PA164742228; -.
eggNOG; KOG1329; Eukaryota.
eggNOG; COG1502; LUCA.
GeneTree; ENSGT00390000008356; -.
HOGENOM; HOG000246972; -.
HOVERGEN; HBG006650; -.
InParanoid; Q13393; -.
KO; K01115; -.
OMA; RDFINKP; -.
OrthoDB; EOG091G017Y; -.
PhylomeDB; Q13393; -.
TreeFam; TF300589; -.
BioCyc; MetaCyc:HS01185-MONOMER; -.
BRENDA; 3.1.4.4; 2681.
Reactome; R-HSA-1483148; Synthesis of PG.
Reactome; R-HSA-1483166; Synthesis of PA.
Reactome; R-HSA-2029485; Role of phospholipids in phagocytosis.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SignaLink; Q13393; -.
SIGNOR; Q13393; -.
ChiTaRS; PLD1; human.
GeneWiki; Phospholipase_D1; -.
GenomeRNAi; 5337; -.
PRO; PR:Q13393; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000075651; -.
CleanEx; HS_PLD1; -.
ExpressionAtlas; Q13393; baseline and differential.
Genevisible; Q13393; HS.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0030139; C:endocytic vesicle; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0005768; C:endosome; IDA:MGI.
GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
GO; GO:0004630; F:phospholipase D activity; TAS:Reactome.
GO; GO:0048870; P:cell motility; IBA:GO_Central.
GO; GO:0006935; P:chemotaxis; TAS:ProtInc.
GO; GO:0048017; P:inositol lipid-mediated signaling; IEA:InterPro.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0006654; P:phosphatidic acid biosynthetic process; TAS:Reactome.
GO; GO:0007265; P:Ras protein signal transduction; TAS:ProtInc.
GO; GO:0032534; P:regulation of microvillus assembly; IMP:UniProtKB.
GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:ProtInc.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 3.30.1520.10; -; 1.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR001683; Phox.
InterPro; IPR025202; PLD-like_dom.
InterPro; IPR001736; PLipase_D/transphosphatidylase.
InterPro; IPR016555; PLipase_D_euk.
InterPro; IPR015679; PLipase_D_fam.
InterPro; IPR036871; PX_dom_sf.
PANTHER; PTHR18896; PTHR18896; 1.
Pfam; PF00169; PH; 1.
Pfam; PF00614; PLDc; 1.
Pfam; PF13091; PLDc_2; 1.
Pfam; PF00787; PX; 1.
PIRSF; PIRSF009376; Phospholipase_D_euk; 1.
SMART; SM00233; PH; 1.
SMART; SM00155; PLDc; 2.
SMART; SM00312; PX; 1.
SUPFAM; SSF50729; SSF50729; 1.
SUPFAM; SSF64268; SSF64268; 1.
PROSITE; PS50035; PLD; 2.
PROSITE; PS50195; PX; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Disease mutation;
Endoplasmic reticulum; Endosome; Golgi apparatus; Hydrolase;
Lipid degradation; Lipid metabolism; Lipoprotein; Membrane; Palmitate;
Phosphoprotein; Polymorphism; Reference proteome; Repeat.
CHAIN 1 1074 Phospholipase D1.
/FTId=PRO_0000218802.
DOMAIN 81 212 PX. {ECO:0000255|PROSITE-
ProRule:PRU00147}.
DOMAIN 219 328 PH.
DOMAIN 459 486 PLD phosphodiesterase 1.
{ECO:0000255|PROSITE-ProRule:PRU00153}.
DOMAIN 891 918 PLD phosphodiesterase 2.
{ECO:0000255|PROSITE-ProRule:PRU00153}.
REGION 463 928 Catalytic.
MOD_RES 499 499 Phosphoserine.
{ECO:0000250|UniProtKB:P70496}.
MOD_RES 561 561 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 629 629 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:23186163}.
LIPID 240 240 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 241 241 S-palmitoyl cysteine. {ECO:0000250}.
VAR_SEQ 514 597 PAAMESMESLRLKDKNEPVQNLPIQKSIDDVDSKLKGIGKP
RKFSKFSLYKQLHRHHLHDADSISSIDSTSSYFNHYRSHHN
LI -> IPGPSVVYRQVWESCMGKPDSGMERTTAISSSKTG
FNLINLLLISLTGTPRPGCPGMTLPLQSTGRRLVMWHVTSS
SAGTSQKL (in isoform PLD1C).
{ECO:0000303|PubMed:9761774}.
/FTId=VSP_005018.
VAR_SEQ 585 623 SYFNHYRSHHNLIHGLKPHFKLFHPSSESEQGLTRPHAD
-> N (in isoform PLD1B).
{ECO:0000303|PubMed:9013646,
ECO:0000303|PubMed:9761774}.
/FTId=VSP_005020.
VAR_SEQ 598 1074 Missing (in isoform PLD1C).
{ECO:0000303|PubMed:9761774}.
/FTId=VSP_005019.
VAR_SEQ 962 971 VVLGYLDDPS -> SKMTPGVEDP (in isoform
PLD1D). {ECO:0000303|Ref.5}.
/FTId=VSP_005021.
VAR_SEQ 972 1074 Missing (in isoform PLD1D).
{ECO:0000303|Ref.5}.
/FTId=VSP_005022.
VARIANT 49 49 P -> A (in dbSNP:rs9819927).
/FTId=VAR_034387.
VARIANT 442 442 H -> P (in CVDD; dbSNP:rs769669104).
{ECO:0000269|PubMed:27799408}.
/FTId=VAR_078985.
VARIANT 622 622 A -> S (in dbSNP:rs2290480).
/FTId=VAR_022056.
VARIANT 820 820 V -> M (in dbSNP:rs2287579).
/FTId=VAR_022057.
VARIANT 1024 1024 V -> I (in dbSNP:rs9827333).
/FTId=VAR_051703.
CONFLICT 832 832 S -> P (in Ref. 3; CAB76564).
{ECO:0000305}.
SEQUENCE 1074 AA; 124184 MW; 734F285790A0BF7A CRC64;
MSLKNEPRVN TSALQKIAAD MSNIIENLDT RELHFEGEEV DYDVSPSDPK IQEVYIPFSA
IYNTQGFKEP NIQTYLSGCP IKAQVLEVER FTSTTRVPSI NLYTIELTHG EFKWQVKRKF
KHFQEFHREL LKYKAFIRIP IPTRRHTFRR QNVREEPREM PSLPRSSENM IREEQFLGRR
KQLEDYLTKI LKMPMYRNYH ATTEFLDISQ LSFIHDLGPK GIEGMIMKRS GGHRIPGLNC
CGQGRACYRW SKRWLIVKDS FLLYMKPDSG AIAFVLLVDK EFKIKVGKKE TETKYGIRID
NLSRTLILKC NSYRHARWWG GAIEEFIQKH GTNFLKDHRF GSYAAIQENA LAKWYVNAKG
YFEDVANAME EANEEIFITD WWLSPEIFLK RPVVEGNRWR LDCILKRKAQ QGVRIFIMLY
KEVELALGIN SEYTKRTLMR LHPNIKVMRH PDHVSSTVYL WAHHEKLVII DQSVAFVGGI
DLAYGRWDDN EHRLTDVGSV KRVTSGPSLG SLPPAAMESM ESLRLKDKNE PVQNLPIQKS
IDDVDSKLKG IGKPRKFSKF SLYKQLHRHH LHDADSISSI DSTSSYFNHY RSHHNLIHGL
KPHFKLFHPS SESEQGLTRP HADTGSIRSL QTGVGELHGE TRFWHGKDYC NFVFKDWVQL
DKPFADFIDR YSTPRMPWHD IASAVHGKAA RDVARHFIQR WNFTKIMKSK YRSLSYPFLL
PKSQTTAHEL RYQVPGSVHA NVQLLRSAAD WSAGIKYHEE SIHAAYVHVI ENSRHYIYIE
NQFFISCADD KVVFNKIGDA IAQRILKAHR ENQKYRVYVV IPLLPGFEGD ISTGGGNALQ
AIMHFNYRTM CRGENSILGQ LKAELGNQWI NYISFCGLRT HAELEGNLVT ELIYVHSKLL
IADDNTVIIG SANINDRSML GKRDSEMAVI VQDTETVPSV MDGKEYQAGR FARGLRLQCF
RVVLGYLDDP SEDIQDPVSD KFFKEVWVST AARNATIYDK VFRCLPNDEV HNLIQLRDFI
NKPVLAKEDP IRAEEELKKI RGFLVQFPFY FLSEESLLPS VGTKEAIVPM EVWT


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EIAAB31494 Homo sapiens,Human,Inactive choline phosphatase 5,Inactive phosphatidylcholine-hydrolyzing phospholipase D5,Inactive phospholipase D5,Inactive PLD 5,PLD5,PLDc
EIAAB31493 Inactive choline phosphatase 5,Inactive phosphatidylcholine-hydrolyzing phospholipase D5,Inactive phospholipase D5,Inactive PLD 5,Mouse,Mus musculus,Pld5
EIAAB29640 GIIC sPLA2,Group IIA phospholipase A2,Homo sapiens,Human,Non-pancreatic secretory phospholipase A2,NPS-PLA2,Phosphatidylcholine 2-acylhydrolase 2A,Phospholipase A2, membrane associated,PLA2B,PLA2G2A,P
EIAAB26364 C7orf18,Homo sapiens,Human,N-acyl phosphatidylethanolamine phospholipase D,N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D,NAPE-hydrolyzing phospholipase D,NAPEPLD,NAPE-PLD
EIAAB26366 Mbldc1,Mouse,Mus musculus,N-acyl phosphatidylethanolamine phospholipase D,N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D,NAPE-hydrolyzing phospholipase D,Napepld,NAPE-PLD
10-663-45314 Secreted Phospholipase A2-IIA (sPLA2-IIA) Human - EC 3.1.1.4; Phosphatidylcholine 2-acylhydrolase; Group IIA phospholipase A2; GIIC sPLA2; Non-pancreatic secretory phospholipase A2; NPS-PLA2 N_A 0.002 mg
10-663-45314 Secreted Phospholipase A2-IIA (sPLA2-IIA) Human - EC 3.1.1.4; Phosphatidylcholine 2-acylhydrolase; Group IIA phospholipase A2; GIIC sPLA2; Non-pancreatic secretory phospholipase A2; NPS-PLA2 N_A 0.01 mg
10-663-45314 Secreted Phospholipase A2-IIA (sPLA2-IIA) Human - EC 3.1.1.4; Phosphatidylcholine 2-acylhydrolase; Group IIA phospholipase A2; GIIC sPLA2; Non-pancreatic secretory phospholipase A2; NPS-PLA2 N_A 1 mg


 

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