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Group XV phospholipase A2 (EC 2.3.1.-) (1-O-acylceramide synthase) (ACS) (LCAT-like lysophospholipase) (LLPL) (Lysophospholipase 3) (Lysosomal phospholipase A2) (LPLA2)

 PAG15_HUMAN             Reviewed;         412 AA.
Q8NCC3; B3KMF3; B4DUD1; Q53GZ1; Q9NPQ6; Q9UG04; Q9Y2B3;
01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2004, sequence version 2.
27-SEP-2017, entry version 139.
RecName: Full=Group XV phospholipase A2;
EC=2.3.1.- {ECO:0000269|PubMed:11790796, ECO:0000269|PubMed:20410020, ECO:0000269|PubMed:23958596, ECO:0000269|PubMed:25727495};
AltName: Full=1-O-acylceramide synthase {ECO:0000303|PubMed:11790796};
Short=ACS;
AltName: Full=LCAT-like lysophospholipase {ECO:0000303|PubMed:10092508};
Short=LLPL {ECO:0000303|PubMed:10092508};
AltName: Full=Lysophospholipase 3;
AltName: Full=Lysosomal phospholipase A2 {ECO:0000303|PubMed:11790796, ECO:0000303|PubMed:23958596};
Short=LPLA2 {ECO:0000303|PubMed:11790796, ECO:0000303|PubMed:23958596};
Flags: Precursor;
Name=PLA2G15; Synonyms=LYPLA3; ORFNames=UNQ341/PRO540;
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 1), PROTEIN SEQUENCE OF 34-43,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND FUNCTION.
TISSUE=Heart, and Kidney;
PubMed=10092508; DOI=10.1006/bbrc.1999.0411;
Taniyama Y., Shibata S., Kita S., Horikoshi K., Shirafuji H.,
Sumino Y., Fujino M.;
"Cloning and expression of a novel lysophospholipase which
structurally resembles lecithin cholesterol acyltransferase.";
Biochem. Biophys. Res. Commun. 257:50-56(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Teratocarcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Liver;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Colon;
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).
[9]
PROTEIN SEQUENCE OF 34-48.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 221-412 (ISOFORM 1).
The European IMAGE consortium;
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[11]
GLYCOSYLATION, FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=11790796; DOI=10.1074/jbc.M111977200;
Hiraoka M., Abe A., Shayman J.A.;
"Cloning and characterization of a lysosomal phospholipase A2, 1-O-
acylceramide synthase.";
J. Biol. Chem. 277:10090-10099(2002).
[12]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION, AND CATALYTIC
ACTIVITY.
PubMed=20410020; DOI=10.1194/jlr.D007146;
Abe A., Kelly R., Shayman J.A.;
"The measurement of lysosomal phospholipase A2 activity in plasma.";
J. Lipid Res. 51:2464-2470(2010).
[13]
GLYCOSYLATION, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF ASN-99; ASN-273; ASN-289 AND ASN-398.
PubMed=23958596; DOI=10.1194/jlr.M041640;
Hiraoka M., Okamoto K., Ohguro H., Abe A.;
"Role of N-glycosylation of human lysosomal phospholipase A2 for the
formation of catalytically active enzyme.";
J. Lipid Res. 54:3098-3105(2013).
[14]
X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 34-412 IN COMPLEX WITH
SYNTHETIC INHIBITOR, CATALYTIC ACTIVITY, FUNCTION, ACTIVE SITE,
SUBCELLULAR LOCATION, DISULFIDE BOND, MUTAGENESIS OF ASP-46; LEU-83;
VAL-85; SER-198; LYS-235 AND THR-362, AND GLYCOSYLATION AT ASN-99;
ASN-273; ASN-289 AND ASN-398.
PubMed=25727495; DOI=10.1038/ncomms7250;
Glukhova A., Hinkovska-Galcheva V., Kelly R., Abe A., Shayman J.A.,
Tesmer J.J.;
"Structure and function of lysosomal phospholipase A2 and
lecithin:cholesterol acyltransferase.";
Nat. Commun. 6:6250-6250(2015).
-!- FUNCTION: Has transacylase and calcium-independent phospholipase
A2 activity (PubMed:20410020, PubMed:23958596). Catalyzes the
formation of 1-O-acyl-N-acetylsphingosine and the concomitant
release of a lyso-phospholipid (PubMed:11790796, PubMed:25727495).
Has high activity with 1-palmitoyl-2-oleoyl-sn-glycero-3-
phosphocholine (POPC) and 1,2-dioleoyl-sn-glycero-3-phosphocholine
(DOPC), catalyzing the transfer of oleic acid to N-acetyl-
sphingosine. Required for normal phospholipid degradation in
alveolar and peritoneal macrophages and in spleen (By similarity).
May have weak lysophospholipase activity (PubMed:10092508).
{ECO:0000250|UniProtKB:Q8VEB4, ECO:0000269|PubMed:10092508,
ECO:0000269|PubMed:11790796, ECO:0000269|PubMed:20410020,
ECO:0000269|PubMed:23958596, ECO:0000269|PubMed:25727495}.
-!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:23958596}.
Secreted {ECO:0000269|PubMed:10092508,
ECO:0000269|PubMed:20410020}. Membrane
{ECO:0000269|PubMed:25727495}; Peripheral membrane protein
{ECO:0000269|PubMed:25727495}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8NCC3-1; Sequence=Displayed;
Name=2;
IsoId=Q8NCC3-2; Sequence=VSP_056689, VSP_056690;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Detected in blood plasma (at protein level)
(PubMed:10092508, PubMed:20410020). Ubiquitous. Highly expressed
in heart, placenta, skeletal muscle, kidney and pancreas. Detected
at lower levels in spleen, thymus, prostate, testis, ovary, small
intestine, colon and peripheral blood leukocytes
(PubMed:10092508). {ECO:0000269|PubMed:10092508,
ECO:0000269|PubMed:20410020}.
-!- PTM: N-glycosylated (PubMed:11790796, PubMed:23958596). N-
glycosylation is important for maturation of the enzyme and normal
subcellular location (PubMed:23958596).
{ECO:0000269|PubMed:11790796, ECO:0000269|PubMed:23958596}.
-!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAB53675.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AB017494; BAA76877.1; -; mRNA.
EMBL; AY358425; AAQ88791.1; -; mRNA.
EMBL; AK001705; BAG50965.1; -; mRNA.
EMBL; AK074828; BAC11233.1; -; mRNA.
EMBL; AK300596; BAG62293.1; -; mRNA.
EMBL; AK222790; BAD96510.1; -; mRNA.
EMBL; AL110209; CAB53675.1; ALT_INIT; mRNA.
EMBL; AC020978; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471092; EAW83217.1; -; Genomic_DNA.
EMBL; BC011640; AAH11640.2; -; mRNA.
EMBL; BC062605; AAH62605.1; -; mRNA.
EMBL; AL389957; CAB97531.1; -; mRNA.
CCDS; CCDS10864.1; -. [Q8NCC3-1]
PIR; T14755; T14755.
RefSeq; NP_036452.1; NM_012320.3. [Q8NCC3-1]
UniGene; Hs.632199; -.
PDB; 4X90; X-ray; 1.84 A; A/B/C/D=34-412.
PDB; 4X91; X-ray; 2.30 A; A/B/C/D=34-412.
PDB; 4X92; X-ray; 3.00 A; A=34-412.
PDB; 4X93; X-ray; 2.60 A; A/B=34-412.
PDB; 4X94; X-ray; 2.70 A; A=34-412.
PDB; 4X95; X-ray; 3.08 A; A/B=34-412.
PDB; 4X97; X-ray; 2.65 A; A/B/C/D=34-412.
PDBsum; 4X90; -.
PDBsum; 4X91; -.
PDBsum; 4X92; -.
PDBsum; 4X93; -.
PDBsum; 4X94; -.
PDBsum; 4X95; -.
PDBsum; 4X97; -.
ProteinModelPortal; Q8NCC3; -.
SMR; Q8NCC3; -.
BioGrid; 117181; 4.
IntAct; Q8NCC3; 2.
MINT; MINT-1403291; -.
STRING; 9606.ENSP00000219345; -.
BindingDB; Q8NCC3; -.
ChEMBL; CHEMBL4986; -.
ESTHER; human-PLA2G15; PC-sterol_acyltransferase.
iPTMnet; Q8NCC3; -.
PhosphoSitePlus; Q8NCC3; -.
BioMuta; PLA2G15; -.
DMDM; 44888104; -.
EPD; Q8NCC3; -.
MaxQB; Q8NCC3; -.
PaxDb; Q8NCC3; -.
PeptideAtlas; Q8NCC3; -.
PRIDE; Q8NCC3; -.
DNASU; 23659; -.
Ensembl; ENST00000219345; ENSP00000219345; ENSG00000103066. [Q8NCC3-1]
Ensembl; ENST00000413021; ENSP00000394197; ENSG00000103066. [Q8NCC3-2]
GeneID; 23659; -.
KEGG; hsa:23659; -.
UCSC; uc002evr.4; human. [Q8NCC3-1]
CTD; 23659; -.
DisGeNET; 23659; -.
EuPathDB; HostDB:ENSG00000103066.12; -.
GeneCards; PLA2G15; -.
HGNC; HGNC:17163; PLA2G15.
HPA; HPA041702; -.
HPA; HPA041727; -.
MIM; 609362; gene.
neXtProt; NX_Q8NCC3; -.
OpenTargets; ENSG00000103066; -.
PharmGKB; PA164724567; -.
eggNOG; KOG2369; Eukaryota.
eggNOG; ENOG410Y9CF; LUCA.
GeneTree; ENSGT00390000004902; -.
HOGENOM; HOG000238654; -.
InParanoid; Q8NCC3; -.
KO; K06129; -.
OMA; IPGWGDP; -.
OrthoDB; EOG091G07S3; -.
PhylomeDB; Q8NCC3; -.
TreeFam; TF313258; -.
Reactome; R-HSA-1483115; Hydrolysis of LPC.
ChiTaRS; PLA2G15; human.
GeneWiki; LYPLA3_(gene); -.
GenomeRNAi; 23659; -.
PRO; PR:Q8NCC3; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000103066; -.
CleanEx; HS_PLA2G15; -.
ExpressionAtlas; Q8NCC3; baseline and differential.
Genevisible; Q8NCC3; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005764; C:lysosome; ISS:UniProtKB.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0047499; F:calcium-independent phospholipase A2 activity; ISS:UniProtKB.
GO; GO:0004622; F:lysophospholipase activity; TAS:ProtInc.
GO; GO:0008374; F:O-acyltransferase activity; IDA:UniProtKB.
GO; GO:0005543; F:phospholipid binding; TAS:ProtInc.
GO; GO:0006672; P:ceramide metabolic process; IDA:UniProtKB.
GO; GO:0009062; P:fatty acid catabolic process; TAS:ProtInc.
GO; GO:0006650; P:glycerophospholipid metabolic process; IDA:UniProtKB.
GO; GO:0034638; P:phosphatidylcholine catabolic process; ISS:UniProtKB.
GO; GO:0046338; P:phosphatidylethanolamine catabolic process; ISS:UniProtKB.
GO; GO:0006644; P:phospholipid metabolic process; TAS:Reactome.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR003386; LACT/PDAT_acylTrfase.
Pfam; PF02450; LCAT; 2.
SUPFAM; SSF53474; SSF53474; 2.
1: Evidence at protein level;
3D-structure; Acyltransferase; Alternative splicing;
Complete proteome; Direct protein sequencing; Disulfide bond;
Fatty acid metabolism; Glycoprotein; Hydrolase; Lipid degradation;
Lipid metabolism; Lysosome; Membrane; Reference proteome; Secreted;
Signal; Transferase.
SIGNAL 1 33 {ECO:0000269|PubMed:10092508,
ECO:0000269|PubMed:15340161}.
CHAIN 34 412 Group XV phospholipase A2.
/FTId=PRO_0000017808.
ACT_SITE 198 198 Acyl-ester intermediate.
{ECO:0000244|PDB:4X97, ECO:0000255,
ECO:0000269|PubMed:25727495}.
ACT_SITE 360 360 Charge relay system.
{ECO:0000305|PubMed:25727495}.
ACT_SITE 392 392 Charge relay system.
{ECO:0000305|PubMed:25727495}.
BINDING 46 46 Substrate; via amide nitrogen.
{ECO:0000244|PDB:4X97,
ECO:0000305|PubMed:25727495}.
BINDING 199 199 Substrate; via amide nitrogen.
{ECO:0000244|PDB:4X95,
ECO:0000305|PubMed:25727495}.
CARBOHYD 99 99 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4X90,
ECO:0000244|PDB:4X91,
ECO:0000244|PDB:4X92,
ECO:0000244|PDB:4X93,
ECO:0000244|PDB:4X94,
ECO:0000244|PDB:4X95,
ECO:0000244|PDB:4X97, ECO:0000255,
ECO:0000269|PubMed:25727495}.
CARBOHYD 273 273 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4X90,
ECO:0000244|PDB:4X91,
ECO:0000244|PDB:4X92,
ECO:0000244|PDB:4X93,
ECO:0000244|PDB:4X94,
ECO:0000244|PDB:4X95,
ECO:0000244|PDB:4X97, ECO:0000255,
ECO:0000269|PubMed:25727495}.
CARBOHYD 289 289 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4X90,
ECO:0000244|PDB:4X91,
ECO:0000244|PDB:4X92,
ECO:0000244|PDB:4X93,
ECO:0000244|PDB:4X94,
ECO:0000244|PDB:4X95,
ECO:0000244|PDB:4X97, ECO:0000255,
ECO:0000269|PubMed:25727495}.
CARBOHYD 398 398 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4X90,
ECO:0000244|PDB:4X91,
ECO:0000244|PDB:4X92,
ECO:0000244|PDB:4X93,
ECO:0000244|PDB:4X94,
ECO:0000244|PDB:4X95,
ECO:0000244|PDB:4X97, ECO:0000255,
ECO:0000269|PubMed:25727495}.
DISULFID 65 89 {ECO:0000244|PDB:4X90,
ECO:0000244|PDB:4X91,
ECO:0000244|PDB:4X92,
ECO:0000244|PDB:4X93,
ECO:0000244|PDB:4X94,
ECO:0000244|PDB:4X95,
ECO:0000244|PDB:4X97,
ECO:0000269|PubMed:25727495}.
VAR_SEQ 43 114 VPGDLGNQLEAKLDKPTVVHYLCSKKTESYFTIWLNLELLL
PVIIDCWIDNIRLVYNKTSRATQFPDGVDVR -> GWFTTK
HPGPPSFLMVWMYVSLALGRPSHWSSWTPAKAAWVPISTPW
WRALWAGATHGVRMSEGLPMTGAEP (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056689.
VAR_SEQ 115 208 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056690.
MUTAGEN 46 46 D->A: Decreases phospholipase and
transacetylase activity. Has no effect on
association with membranes.
{ECO:0000269|PubMed:25727495}.
MUTAGEN 83 83 L->S: No effect on phospholipase
activity. Strongly decreases
transacetylase activity and association
with membranes.
{ECO:0000269|PubMed:25727495}.
MUTAGEN 85 85 V->S: No effect on phospholipase
activity. Strongly decreases
transacetylase activity and association
with membranes.
{ECO:0000269|PubMed:25727495}.
MUTAGEN 99 99 N->A: Loss of glycosylation site. Leads
to retention in the endoplasmic reticulum
and nearly abolishes the production of
the mature, active enzyme.
{ECO:0000269|PubMed:23958596}.
MUTAGEN 198 198 S->A: Abolishes phospholipase and
transacetylase activity. Abolishes
association with membranes.
{ECO:0000269|PubMed:25727495}.
MUTAGEN 235 235 K->A: No effect on phospholipase
activity. Abolishes transacetylase
activity. Has no effect on association
with membranes.
{ECO:0000269|PubMed:25727495}.
MUTAGEN 273 273 N->A: Loss of glycosylation site. Mildly
reduces production of the mature, active
enzyme. {ECO:0000269|PubMed:23958596}.
MUTAGEN 289 289 N->A: Loss of glycosylation site. Mildly
reduces production of the mature, active
enzyme. {ECO:0000269|PubMed:23958596}.
MUTAGEN 362 362 T->A: No effect on phospholipase
activity. Strongly decreases
transacetylase activity and abolishes
association with membranes.
{ECO:0000269|PubMed:25727495}.
MUTAGEN 398 398 N->A: Loss of glycosylation site.
Slightly reduces production of the
mature, active enzyme.
{ECO:0000269|PubMed:23958596}.
CONFLICT 94 94 I -> T (in Ref. 4; BAD96510).
{ECO:0000305}.
CONFLICT 370 370 Q -> R (in Ref. 3; BAC11233).
{ECO:0000305}.
STRAND 40 43 {ECO:0000244|PDB:4X90}.
STRAND 51 56 {ECO:0000244|PDB:4X90}.
STRAND 73 77 {ECO:0000244|PDB:4X90}.
HELIX 79 82 {ECO:0000244|PDB:4X90}.
HELIX 86 94 {ECO:0000244|PDB:4X90}.
STRAND 97 99 {ECO:0000244|PDB:4X90}.
TURN 100 103 {ECO:0000244|PDB:4X90}.
STRAND 104 106 {ECO:0000244|PDB:4X90}.
STRAND 111 114 {ECO:0000244|PDB:4X90}.
HELIX 122 125 {ECO:0000244|PDB:4X90}.
STRAND 126 128 {ECO:0000244|PDB:4X90}.
HELIX 133 135 {ECO:0000244|PDB:4X90}.
STRAND 136 138 {ECO:0000244|PDB:4X90}.
HELIX 139 147 {ECO:0000244|PDB:4X90}.
TURN 153 155 {ECO:0000244|PDB:4X90}.
STRAND 156 158 {ECO:0000244|PDB:4X90}.
HELIX 167 169 {ECO:0000244|PDB:4X90}.
HELIX 171 188 {ECO:0000244|PDB:4X90}.
STRAND 192 197 {ECO:0000244|PDB:4X90}.
HELIX 200 209 {ECO:0000244|PDB:4X90}.
HELIX 213 219 {ECO:0000244|PDB:4X90}.
STRAND 220 227 {ECO:0000244|PDB:4X90}.
HELIX 235 242 {ECO:0000244|PDB:4X90}.
HELIX 253 262 {ECO:0000244|PDB:4X90}.
HELIX 264 268 {ECO:0000244|PDB:4X90}.
TURN 273 275 {ECO:0000244|PDB:4X90}.
STRAND 281 284 {ECO:0000244|PDB:4X90}.
STRAND 289 291 {ECO:0000244|PDB:4X90}.
HELIX 292 294 {ECO:0000244|PDB:4X95}.
HELIX 295 301 {ECO:0000244|PDB:4X90}.
HELIX 305 314 {ECO:0000244|PDB:4X90}.
STRAND 328 336 {ECO:0000244|PDB:4X90}.
STRAND 338 343 {ECO:0000244|PDB:4X90}.
TURN 347 349 {ECO:0000244|PDB:4X90}.
STRAND 353 364 {ECO:0000244|PDB:4X90}.
HELIX 365 367 {ECO:0000244|PDB:4X90}.
HELIX 368 374 {ECO:0000244|PDB:4X90}.
TURN 375 377 {ECO:0000244|PDB:4X90}.
STRAND 382 388 {ECO:0000244|PDB:4X90}.
HELIX 394 397 {ECO:0000244|PDB:4X90}.
HELIX 399 410 {ECO:0000244|PDB:4X90}.
SEQUENCE 412 AA; 46658 MW; 1FEA8A5783AF050A CRC64;
MGLHLRPYRV GLLPDGLLFL LLLLMLLADP ALPAGRHPPV VLVPGDLGNQ LEAKLDKPTV
VHYLCSKKTE SYFTIWLNLE LLLPVIIDCW IDNIRLVYNK TSRATQFPDG VDVRVPGFGK
TFSLEFLDPS KSSVGSYFHT MVESLVGWGY TRGEDVRGAP YDWRRAPNEN GPYFLALREM
IEEMYQLYGG PVVLVAHSMG NMYTLYFLQR QPQAWKDKYI RAFVSLGAPW GGVAKTLRVL
ASGDNNRIPV IGPLKIREQQ RSAVSTSWLL PYNYTWSPEK VFVQTPTINY TLRDYRKFFQ
DIGFEDGWLM RQDTEGLVEA TMPPGVQLHC LYGTGVPTPD SFYYESFPDR DPKICFGDGD
GTVNLKSALQ CQAWQSRQEH QVLLQELPGS EHIEMLANAT TLAYLKRVLL GP


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