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Phospholipase D3 (PLD 3) (EC 3.1.4.4) (Choline phosphatase 3) (HindIII K4L homolog) (Hu-K4) (Phosphatidylcholine-hydrolyzing phospholipase D3)

 PLD3_HUMAN              Reviewed;         490 AA.
Q8IV08; Q92853; Q9BW87;
20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
27-SEP-2017, entry version 128.
RecName: Full=Phospholipase D3;
Short=PLD 3;
EC=3.1.4.4;
AltName: Full=Choline phosphatase 3;
AltName: Full=HindIII K4L homolog;
AltName: Full=Hu-K4;
AltName: Full=Phosphatidylcholine-hydrolyzing phospholipase D3;
Name=PLD3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Mammary gland;
PubMed=9140189; DOI=10.1016/S0168-1702(96)01422-0;
Cao J.X., Koop B.F., Upton C.;
"A human homolog of the vaccinia virus HindIII K4L gene is a member of
the phospholipase D superfamily.";
Virus Res. 48:11-18(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Colon, and Lung;
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).
[3]
SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY, AND GLYCOSYLATION.
PubMed=15794758; DOI=10.1111/j.1742-4658.2005.04601.x;
Munck A., Boehm C., Seibel N.M., Hashemol Hosseini Z., Hampe W.;
"Hu-K4 is a ubiquitously expressed type 2 transmembrane protein
associated with the endoplasmic reticulum.";
FEBS J. 272:1718-1726(2005).
[4]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-97 AND ASN-132.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[6]
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).
[7]
FUNCTION, POSSIBLE INVOLVEMENT IN ALZHEIMER DISEASE, VARIANT MET-232,
TISSUE SPECIFICITY, AND INTERACTION WITH APP.
PubMed=24336208; DOI=10.1038/nature12825;
UK Brain Expression Consortium;
Cruchaga C., Karch C.M., Jin S.C., Benitez B.A., Cai Y., Guerreiro R.,
Harari O., Norton J., Budde J., Bertelsen S., Jeng A.T., Cooper B.,
Skorupa T., Carrell D., Levitch D., Hsu S., Choi J., Ryten M.,
Hardy J., Ryten M., Trabzuni D., Weale M.E., Ramasamy A., Smith C.,
Sassi C., Bras J., Gibbs J.R., Hernandez D.G., Lupton M.K., Powell J.,
Forabosco P., Ridge P.G., Corcoran C.D., Tschanz J.T., Norton M.C.,
Munger R.G., Schmutz C., Leary M., Demirci F.Y., Bamne M.N., Wang X.,
Lopez O.L., Ganguli M., Medway C., Turton J., Lord J., Braae A.,
Barber I., Brown K., Passmore P., Craig D., Johnston J.,
McGuinness B., Todd S., Heun R., Kolsch H., Kehoe P.G., Hooper N.M.,
Vardy E.R., Mann D.M., Pickering-Brown S., Brown K., Kalsheker N.,
Lowe J., Morgan K., David Smith A., Wilcock G., Warden D., Holmes C.,
Pastor P., Lorenzo-Betancor O., Brkanac Z., Scott E., Topol E.,
Morgan K., Rogaeva E., Singleton A.B., Hardy J., Kamboh M.I.,
St George-Hyslop P., Cairns N., Morris J.C., Kauwe J.S., Goate A.M.;
"Rare coding variants in the phospholipase D3 gene confer risk for
Alzheimer's disease.";
Nature 505:550-554(2014).
[8]
LACK OF INVOLVEMENT IN ALZHEIMER DISEASE, AND VARIANTS SER-63; ALA-76;
MET-159; CYS-162; SER-173; GLY-175; CYS-188; HIS-222; MET-232;
GLN-242; GLY-249; CYS-272; SER-284; VAL-293; LEU-297; TYR-300;
PRO-308; ILE-358; ALA-426 AND ARG-429.
PubMed=26411346; DOI=10.1002/humu.22908;
Belgium Neurology (BELNEU) Consortium and the European Early-Onset Dementia (EU EOD) Consortium;
Cacace R., Van den Bossche T., Engelborghs S., Geerts N., Laureys A.,
Dillen L., Graff C., Thonberg H., Chiang H.H., Pastor P.,
Ortega-Cubero S., Pastor M.A., Diehl-Schmid J., Alexopoulos P.,
Benussi L., Ghidoni R., Binetti G., Nacmias B., Sorbi S.,
Sanchez-Valle R., Llado A., Gelpi E., Almeida M.R., Santana I.,
Tsolaki M., Koutroumani M., Clarimon J., Lleo A., Fortea J.,
de Mendonca A., Martins M., Borroni B., Padovani A., Matej R.,
Rohan Z., Vandenbulcke M., Vandenberghe R., De Deyn P.P., Cras P.,
van der Zee J., Sleegers K., Van Broeckhoven C.;
"Rare variants in PLD3 do not affect risk for early-onset Alzheimer
disease in a European consortium cohort.";
Hum. Mutat. 36:1226-1235(2015).
[9]
LACK OF INVOLVEMENT IN ALZHEIMER DISEASE.
PubMed=25832408; DOI=10.1038/nature14036;
Lambert J.C., Grenier-Boley B., Bellenguez C., Pasquier F.,
Campion D., Dartigues J.F., Berr C., Tzourio C., Amouyel P.;
"PLD3 and sporadic Alzheimer's disease risk.";
Nature 520:E1-E1(2015).
[10]
LACK OF INVOLVEMENT IN ALZHEIMER DISEASE, AND VARIANT MET-232.
PubMed=25832410; DOI=10.1038/nature14038;
van der Lee S.J., Holstege H., Wong T.H., Jakobsdottir J., Bis J.C.,
Chouraki V., van Rooij J.G., Grove M.L., Smith A.V., Amin N.,
Choi S.H., Beiser A.S., Garcia M.E., van Ijcken W.F., Pijnenburg Y.A.,
Louwersheimer E., Brouwer R.W., van den Hout M.C., Oole E.,
Eirkisdottir G., Levy D., Rotter J.I., Emilsson V., O'Donnell C.J.,
Aspelund T., Uitterlinden A.G., Launer L.J., Hofman A., Boerwinkle E.,
Psaty B.M., DeStefano A.L., Scheltens P., Seshadri S.,
van Swieten J.C., Gudnason V., van der Flier W.M., Ikram M.A.,
van Duijn C.M.;
"PLD3 variants in population studies.";
Nature 520:E2-E3(2015).
[11]
LACK OF INVOLVEMENT IN ALZHEIMER DISEASE, AND VARIANT MET-232.
PubMed=25832411; DOI=10.1038/nature14039;
Heilmann S., Drichel D., Clarimon J., Fernandez V., Lacour A.,
Wagner H., Thelen M., Hernandez I., Fortea J., Alegret M., Blesa R.,
Mauleon A., Roca M.R., Kornhuber J., Peters O., Heun R., Froelich L.,
Huell M., Heneka M.T., Ruether E., Riedel-Heller S., Scherer M.,
Wiltfang J., Jessen F., Becker T., Tarraga L., Boada M., Maier W.,
Lleo A., Ruiz A., Noethen M.M., Ramirez A.;
"PLD3 in non-familial Alzheimer's disease.";
Nature 520:E3-E5(2015).
[12]
LACK OF INVOLVEMENT IN ALZHEIMER DISEASE.
PubMed=25832413; DOI=10.1038/nature14040;
Hooli B.V., Lill C.M., Mullin K., Qiao D., Lange C., Bertram L.,
Tanzi R.E.;
"PLD3 gene variants and Alzheimer's disease.";
Nature 520:E7-E8(2015).
[13]
POSSIBLE INVOLVEMENT IN ALZHEIMER DISEASE.
PubMed=25832409; DOI=10.1038/nature14041;
Cruchaga C., Goate A.M.;
"Cruchaga & Goate reply.";
Nature 520:E10-E10(2015).
[14]
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).
-!- FUNCTION: May be involved in APP processing.
{ECO:0000305|PubMed:24336208}.
-!- CATALYTIC ACTIVITY: A phosphatidylcholine + H(2)O = choline + a
phosphatidate.
-!- SUBUNIT: Interacts with APP. {ECO:0000269|PubMed:24336208}.
-!- INTERACTION:
P19838:NFKB1; NbExp=2; IntAct=EBI-2689908, EBI-300010;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:15794758}; Single-pass type II membrane
protein {ECO:0000269|PubMed:15794758}.
-!- TISSUE SPECIFICITY: Widely expressed. In the brain, high levels of
expression are detected in the frontal, temporal and occipital
cortices and hippocampus. Expressed at low level in corpus
callosum. {ECO:0000269|PubMed:15794758,
ECO:0000269|PubMed:24336208}.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:15794758,
ECO:0000269|PubMed:19159218}.
-!- DISEASE: Note=Genetic variants in PLD3 have been suggested to be
associated with an increased risk for Alzheimer disease
(PubMed:24336208, PubMed:25832409). Further studies, however, did
not support PLD3 involvement in this disease (PubMed:25832408,
PubMed:25832411, PubMed:25832413, PubMed:25832410,
PubMed:26411346). {ECO:0000269|PubMed:24336208,
ECO:0000269|PubMed:25832408, ECO:0000269|PubMed:25832409,
ECO:0000269|PubMed:25832410, ECO:0000269|PubMed:25832411,
ECO:0000269|PubMed:25832413, ECO:0000269|PubMed:26411346}.
-!- SIMILARITY: Belongs to the phospholipase D family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB16799.1; Type=Frameshift; Positions=52; Evidence={ECO:0000305};
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EMBL; U60644; AAB16799.1; ALT_FRAME; mRNA.
EMBL; BC000553; AAH00553.2; -; mRNA.
EMBL; BC036327; AAH36327.1; -; mRNA.
EMBL; BC096820; AAH96820.1; -; mRNA.
CCDS; CCDS33027.1; -.
RefSeq; NP_001026866.1; NM_001031696.3.
RefSeq; NP_001278240.1; NM_001291311.1.
RefSeq; NP_036400.2; NM_012268.3.
RefSeq; XP_005258761.1; XM_005258704.1.
RefSeq; XP_005258764.1; XM_005258707.4.
RefSeq; XP_005258765.1; XM_005258708.3.
RefSeq; XP_005258766.1; XM_005258709.4.
RefSeq; XP_005258767.1; XM_005258710.4.
RefSeq; XP_006723185.1; XM_006723122.1.
RefSeq; XP_011524994.1; XM_011526692.1.
RefSeq; XP_011524995.1; XM_011526693.1.
RefSeq; XP_016882035.1; XM_017026546.1.
RefSeq; XP_016882036.1; XM_017026547.1.
RefSeq; XP_016882037.1; XM_017026548.1.
RefSeq; XP_016882038.1; XM_017026549.1.
UniGene; Hs.257008; -.
ProteinModelPortal; Q8IV08; -.
SMR; Q8IV08; -.
BioGrid; 117173; 25.
IntAct; Q8IV08; 24.
STRING; 9606.ENSP00000348901; -.
iPTMnet; Q8IV08; -.
PhosphoSitePlus; Q8IV08; -.
BioMuta; PLD3; -.
DMDM; 74750647; -.
EPD; Q8IV08; -.
MaxQB; Q8IV08; -.
PaxDb; Q8IV08; -.
PeptideAtlas; Q8IV08; -.
PRIDE; Q8IV08; -.
TopDownProteomics; Q8IV08; -.
DNASU; 23646; -.
Ensembl; ENST00000356508; ENSP00000348901; ENSG00000105223.
Ensembl; ENST00000409281; ENSP00000387022; ENSG00000105223.
Ensembl; ENST00000409419; ENSP00000386293; ENSG00000105223.
Ensembl; ENST00000409587; ENSP00000387050; ENSG00000105223.
Ensembl; ENST00000409735; ENSP00000386938; ENSG00000105223.
GeneID; 23646; -.
KEGG; hsa:23646; -.
UCSC; uc002onj.5; human.
CTD; 23646; -.
DisGeNET; 23646; -.
EuPathDB; HostDB:ENSG00000105223.19; -.
GeneCards; PLD3; -.
HGNC; HGNC:17158; PLD3.
HPA; CAB020812; -.
HPA; HPA012800; -.
MalaCards; PLD3; -.
MIM; 615698; gene.
neXtProt; NX_Q8IV08; -.
OpenTargets; ENSG00000105223; -.
PharmGKB; PA134887482; -.
eggNOG; KOG3603; Eukaryota.
eggNOG; ENOG410XQZ4; LUCA.
GeneTree; ENSGT00390000009798; -.
HOGENOM; HOG000293407; -.
HOVERGEN; HBG052880; -.
InParanoid; Q8IV08; -.
KO; K16860; -.
OMA; THFIPNT; -.
OrthoDB; EOG091G07LR; -.
PhylomeDB; Q8IV08; -.
TreeFam; TF313378; -.
Reactome; R-HSA-1483148; Synthesis of PG.
Reactome; R-HSA-2029485; Role of phospholipids in phagocytosis.
ChiTaRS; PLD3; human.
GenomeRNAi; 23646; -.
PRO; PR:Q8IV08; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000105223; -.
CleanEx; HS_PLD3; -.
ExpressionAtlas; Q8IV08; baseline and differential.
Genevisible; Q8IV08; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
GO; GO:0004630; F:phospholipase D activity; TAS:ProtInc.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
InterPro; IPR032803; PLDc_3.
InterPro; IPR001736; PLipase_D/transphosphatidylase.
Pfam; PF00614; PLDc; 1.
Pfam; PF13918; PLDc_3; 1.
SMART; SM00155; PLDc; 2.
PROSITE; PS50035; PLD; 2.
1: Evidence at protein level;
Complete proteome; Endoplasmic reticulum; Glycoprotein; Hydrolase;
Lipid degradation; Lipid metabolism; Membrane; Polymorphism;
Reference proteome; Repeat; Signal-anchor; Transmembrane;
Transmembrane helix.
CHAIN 1 490 Phospholipase D3.
/FTId=PRO_0000280326.
TOPO_DOM 1 38 Cytoplasmic. {ECO:0000255}.
TRANSMEM 39 59 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 60 490 Lumenal. {ECO:0000255}.
DOMAIN 196 223 PLD phosphodiesterase 1.
{ECO:0000255|PROSITE-ProRule:PRU00153}.
DOMAIN 411 437 PLD phosphodiesterase 2.
{ECO:0000255|PROSITE-ProRule:PRU00153}.
ACT_SITE 201 201 {ECO:0000255|PROSITE-ProRule:PRU00153}.
ACT_SITE 203 203 {ECO:0000255|PROSITE-ProRule:PRU00153}.
ACT_SITE 208 208 {ECO:0000255|PROSITE-ProRule:PRU00153}.
CARBOHYD 97 97 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 132 132 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
VARIANT 63 63 G -> S (in dbSNP:rs142070038).
{ECO:0000269|PubMed:26411346}.
/FTId=VAR_075905.
VARIANT 76 76 P -> A (in dbSNP:rs138674695).
{ECO:0000269|PubMed:26411346}.
/FTId=VAR_075906.
VARIANT 159 159 V -> M (in dbSNP:rs374184677).
{ECO:0000269|PubMed:26411346}.
/FTId=VAR_075907.
VARIANT 162 162 R -> C. {ECO:0000269|PubMed:26411346}.
/FTId=VAR_075908.
VARIANT 173 173 P -> S. {ECO:0000269|PubMed:26411346}.
/FTId=VAR_075909.
VARIANT 175 175 A -> G. {ECO:0000269|PubMed:26411346}.
/FTId=VAR_075910.
VARIANT 188 188 R -> C. {ECO:0000269|PubMed:26411346}.
/FTId=VAR_075911.
VARIANT 222 222 R -> H (in dbSNP:rs765630414).
{ECO:0000269|PubMed:26411346}.
/FTId=VAR_075912.
VARIANT 232 232 V -> M (found in Alzheimer disease
patients at higher frequency compared to
controls; unknown pathological
significance; dbSNP:rs145999145).
{ECO:0000269|PubMed:24336208,
ECO:0000269|PubMed:25832410,
ECO:0000269|PubMed:25832411,
ECO:0000269|PubMed:26411346}.
/FTId=VAR_071186.
VARIANT 242 242 R -> Q (in dbSNP:rs757965784).
{ECO:0000269|PubMed:26411346}.
/FTId=VAR_075913.
VARIANT 249 249 E -> G (in dbSNP:rs746715924).
{ECO:0000269|PubMed:26411346}.
/FTId=VAR_075914.
VARIANT 272 272 R -> C (in dbSNP:rs144312764).
{ECO:0000269|PubMed:26411346}.
/FTId=VAR_075915.
VARIANT 284 284 N -> S (in dbSNP:rs200274020).
{ECO:0000269|PubMed:26411346}.
/FTId=VAR_075916.
VARIANT 293 293 A -> V (in dbSNP:rs368737000).
{ECO:0000269|PubMed:26411346}.
/FTId=VAR_075917.
VARIANT 297 297 P -> L. {ECO:0000269|PubMed:26411346}.
/FTId=VAR_075918.
VARIANT 300 300 C -> Y (in dbSNP:rs146083475).
{ECO:0000269|PubMed:26411346}.
/FTId=VAR_075919.
VARIANT 308 308 L -> P (in dbSNP:rs537053537).
{ECO:0000269|PubMed:26411346}.
/FTId=VAR_075920.
VARIANT 358 358 V -> I (in dbSNP:rs370488565).
{ECO:0000269|PubMed:26411346}.
/FTId=VAR_075921.
VARIANT 426 426 T -> A (in dbSNP:rs745463234).
{ECO:0000269|PubMed:26411346}.
/FTId=VAR_075922.
VARIANT 429 429 G -> R. {ECO:0000269|PubMed:26411346}.
/FTId=VAR_075923.
CONFLICT 473 473 S -> I (in Ref. 1; AAB16799).
{ECO:0000305}.
SEQUENCE 490 AA; 54705 MW; 444EC4D02F5610F1 CRC64;
MKPKLMYQEL KVPAEEPANE LPMNEIEAWK AAEKKARWVL LVLILAVVGF GALMTQLFLW
EYGDLHLFGP NQRPAPCYDP CEAVLVESIP EGLDFPNAST GNPSTSQAWL GLLAGAHSSL
DIASFYWTLT NNDTHTQEPS AQQGEEVLRQ LQTLAPKGVN VRIAVSKPSG PQPQADLQAL
LQSGAQVRMV DMQKLTHGVL HTKFWVVDQT HFYLGSANMD WRSLTQVKEL GVVMYNCSCL
ARDLTKIFEA YWFLGQAGSS IPSTWPRFYD TRYNQETPME ICLNGTPALA YLASAPPPLC
PSGRTPDLKA LLNVVDNARS FIYVAVMNYL PTLEFSHPHR FWPAIDDGLR RATYERGVKV
RLLISCWGHS EPSMRAFLLS LAALRDNHTH SDIQVKLFVV PADEAQARIP YARVNHNKYM
VTERATYIGT SNWSGNYFTE TAGTSLLVTQ NGRGGLRSQL EAIFLRDWDS PYSHDLDTSA
DSVGNACRLL


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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 1 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 0.002 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


 

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