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Phospholipase A2 (EC 3.1.1.4) (Group IB phospholipase A2) (Phosphatidylcholine 2-acylhydrolase 1B)

 PA21B_HUMAN             Reviewed;         148 AA.
P04054; B2R4H5; Q3KPI1;
01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 3.
20-JUN-2018, entry version 184.
RecName: Full=Phospholipase A2;
EC=3.1.1.4;
AltName: Full=Group IB phospholipase A2;
AltName: Full=Phosphatidylcholine 2-acylhydrolase 1B;
Flags: Precursor;
Name=PLA2G1B; Synonyms=PLA2, PLA2A, PPLA2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
TISSUE=Lung;
PubMed=3028739; DOI=10.1089/dna.1.1986.5.519;
Seilhamer J.J., Randall T.L., Yamanaka M., Johnson L.K.;
"Pancreatic phospholipase A2: isolation of the human gene and cDNAs
from porcine pancreas and human lung.";
DNA 5:519-527(1986).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Urinary bladder;
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).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[5]
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[7]
PROTEIN SEQUENCE OF 16-22.
TISSUE=Pancreas;
PubMed=7060561; DOI=10.1111/j.1432-1033.1982.tb05855.x;
Grataroli R., Dijkman R., Dutilh C.E., van der Ouderaa F.,
de Haas G.H., Figarella C.;
"Studies on prophospholipase A2 and its enzyme from human pancreatic
juice. Catalytic properties and sequence of the N-terminal region.";
Eur. J. Biochem. 122:111-117(1982).
[8]
PROTEIN SEQUENCE OF 23-148.
TISSUE=Pancreas;
PubMed=6349696; DOI=10.1016/0167-4838(83)90126-7;
Verheij H.M., Westerman J., Sternby B., de Haas G.H.;
"The complete primary structure of phospholipase A2 from human
pancreas.";
Biochim. Biophys. Acta 747:93-99(1983).
[9]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 16-148, DISULFIDE BONDS,
SUBUNIT, AUTOPROTEOLYTIC CLEAVAGE, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=19297324; DOI=10.1074/jbc.M808029200;
Xu W., Yi L., Feng Y., Chen L., Liu J.;
"Structural insight into the activation mechanism of human pancreatic
prophospholipase A2.";
J. Biol. Chem. 284:16659-16666(2009).
-!- FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-
acyl groups in 3-sn-phosphoglycerides, this releases
glycerophospholipids and arachidonic acid that serve as the
precursors of signal molecules. {ECO:0000269|PubMed:19297324}.
-!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1-
acylglycerophosphocholine + a carboxylate. {ECO:0000255|PROSITE-
ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
-!- SUBUNIT: Monomer or homodimer (By similarity). The inactive pro-
form is a homotrimer. {ECO:0000250, ECO:0000269|PubMed:19297324}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19297324}.
Note=secreted from pancreatic acinar cells in its inactive form.
-!- PTM: Activated by trypsin cleavage in the duodenum. Can also be
activated by thrombin or autocatalytically.
-!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS SNPs;
URL="http://egp.gs.washington.edu/data/pla2g1b/";
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EMBL; M21056; AAA60107.1; -; Genomic_DNA.
EMBL; M22970; AAA60107.1; JOINED; Genomic_DNA.
EMBL; M21054; AAA36450.1; -; mRNA.
EMBL; AK311830; BAG34772.1; -; mRNA.
EMBL; AY438977; AAR05441.1; -; Genomic_DNA.
EMBL; AC003982; AAB95635.1; -; Genomic_DNA.
EMBL; CH471054; EAW98184.1; -; Genomic_DNA.
EMBL; BC106725; AAI06726.1; -; mRNA.
EMBL; BC106726; AAI06727.1; -; mRNA.
CCDS; CCDS9195.1; -.
PIR; C25793; PSHU.
RefSeq; NP_000919.1; NM_000928.2.
UniGene; Hs.992; -.
PDB; 1YSK; Model; -; A=23-146.
PDB; 3ELO; X-ray; 1.55 A; A=16-148.
PDBsum; 1YSK; -.
PDBsum; 3ELO; -.
ProteinModelPortal; P04054; -.
SMR; P04054; -.
BioGrid; 111336; 2.
IntAct; P04054; 1.
STRING; 9606.ENSP00000312286; -.
BindingDB; P04054; -.
ChEMBL; CHEMBL4426; -.
DrugBank; DB07836; 1-DECYL-3-TRIFLUORO ETHYL-SN-GLYCERO-2-PHOSPHOMETHANOL.
DrugBank; DB03565; 1-O-Octyl-2-Heptylphosphonyl-Sn-Glycero-3-Phosphoethanolamine.
DrugBank; DB02659; Cholic Acid.
DrugBank; DB02938; Heptanoic Acid.
DrugBank; DB03633; Lpc-Ether.
DrugBank; DB02448; N-Tridecanoic Acid.
DrugBank; DB04552; Niflumic Acid.
DrugBank; DB02795; P-Anisic Acid.
DrugBank; DB07657; PHOSPHONIC ACID 2-DODECANOYLAMINO-HEXYL ESTER PROPYL ESTER.
DrugBank; DB03587; Pyruvoyl Group.
DrugBank; DB00795; Sulfasalazine.
GuidetoPHARMACOLOGY; 1416; -.
SwissLipids; SLP:000001083; -.
BioMuta; PLA2G1B; -.
DMDM; 129404; -.
PaxDb; P04054; -.
PeptideAtlas; P04054; -.
PRIDE; P04054; -.
ProteomicsDB; 51641; -.
DNASU; 5319; -.
Ensembl; ENST00000308366; ENSP00000312286; ENSG00000170890.
GeneID; 5319; -.
KEGG; hsa:5319; -.
UCSC; uc001tyd.3; human.
CTD; 5319; -.
DisGeNET; 5319; -.
EuPathDB; HostDB:ENSG00000170890.13; -.
GeneCards; PLA2G1B; -.
HGNC; HGNC:9030; PLA2G1B.
HPA; CAB022329; -.
HPA; HPA047822; -.
HPA; HPA060803; -.
MIM; 172410; gene.
neXtProt; NX_P04054; -.
OpenTargets; ENSG00000170890; -.
PharmGKB; PA33361; -.
eggNOG; KOG4087; Eukaryota.
eggNOG; ENOG411283D; LUCA.
GeneTree; ENSGT00760000119160; -.
HOGENOM; HOG000231749; -.
HOVERGEN; HBG008137; -.
InParanoid; P04054; -.
KO; K01047; -.
OMA; WQFRKMI; -.
OrthoDB; EOG091G0UZ3; -.
PhylomeDB; P04054; -.
TreeFam; TF319283; -.
Reactome; R-HSA-1482788; Acyl chain remodelling of PC.
Reactome; R-HSA-1482801; Acyl chain remodelling of PS.
Reactome; R-HSA-1482839; Acyl chain remodelling of PE.
Reactome; R-HSA-1482922; Acyl chain remodelling of PI.
Reactome; R-HSA-1482925; Acyl chain remodelling of PG.
Reactome; R-HSA-1483166; Synthesis of PA.
SIGNOR; P04054; -.
ChiTaRS; PLA2G1B; human.
EvolutionaryTrace; P04054; -.
GeneWiki; PLA2G1B; -.
GenomeRNAi; 5319; -.
PRO; PR:P04054; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000170890; -.
CleanEx; HS_PLA2G1B; -.
ExpressionAtlas; P04054; baseline and differential.
Genevisible; P04054; HS.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0030141; C:secretory granule; IEA:Ensembl.
GO; GO:0032052; F:bile acid binding; ISS:BHF-UCL.
GO; GO:0005509; F:calcium ion binding; IDA:BHF-UCL.
GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IDA:BHF-UCL.
GO; GO:0004623; F:phospholipase A2 activity; IDA:BHF-UCL.
GO; GO:0102567; F:phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine); IEA:UniProtKB-EC.
GO; GO:0102568; F:phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine); IEA:UniProtKB-EC.
GO; GO:0005102; F:signaling receptor binding; IDA:BHF-UCL.
GO; GO:0007015; P:actin filament organization; TAS:ProtInc.
GO; GO:0000187; P:activation of MAPK activity; ISS:BHF-UCL.
GO; GO:0032431; P:activation of phospholipase A2 activity; TAS:BHF-UCL.
GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
GO; GO:0050482; P:arachidonic acid secretion; TAS:BHF-UCL.
GO; GO:0032869; P:cellular response to insulin stimulus; ISS:BHF-UCL.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
GO; GO:0006633; P:fatty acid biosynthetic process; IDA:BHF-UCL.
GO; GO:0002227; P:innate immune response in mucosa; IDA:UniProtKB.
GO; GO:0032637; P:interleukin-8 production; ISS:BHF-UCL.
GO; GO:0035556; P:intracellular signal transduction; ISS:BHF-UCL.
GO; GO:0019370; P:leukotriene biosynthetic process; ISS:BHF-UCL.
GO; GO:0016042; P:lipid catabolic process; IDA:BHF-UCL.
GO; GO:0030593; P:neutrophil chemotaxis; ISS:BHF-UCL.
GO; GO:0002446; P:neutrophil mediated immunity; ISS:BHF-UCL.
GO; GO:0006654; P:phosphatidic acid biosynthetic process; TAS:Reactome.
GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; TAS:Reactome.
GO; GO:0046470; P:phosphatidylcholine metabolic process; IDA:BHF-UCL.
GO; GO:0036152; P:phosphatidylethanolamine acyl-chain remodeling; TAS:Reactome.
GO; GO:0036148; P:phosphatidylglycerol acyl-chain remodeling; TAS:Reactome.
GO; GO:0036149; P:phosphatidylinositol acyl-chain remodeling; TAS:Reactome.
GO; GO:0036150; P:phosphatidylserine acyl-chain remodeling; TAS:Reactome.
GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; ISS:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:BHF-UCL.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:BHF-UCL.
GO; GO:0050778; P:positive regulation of immune response; ISS:BHF-UCL.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:BHF-UCL.
GO; GO:0050714; P:positive regulation of protein secretion; TAS:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
GO; GO:0046324; P:regulation of glucose import; ISS:BHF-UCL.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
CDD; cd00125; PLA2c; 1.
Gene3D; 1.20.90.10; -; 1.
InterPro; IPR001211; PLipase_A2.
InterPro; IPR033112; PLipase_A2_Asp_AS.
InterPro; IPR016090; PLipase_A2_dom.
InterPro; IPR036444; PLipase_A2_dom_sf.
InterPro; IPR033113; PLipase_A2_His_AS.
PANTHER; PTHR11716; PTHR11716; 1.
Pfam; PF00068; Phospholip_A2_1; 1.
PRINTS; PR00389; PHPHLIPASEA2.
SMART; SM00085; PA2c; 1.
SUPFAM; SSF48619; SSF48619; 1.
PROSITE; PS00119; PA2_ASP; 1.
PROSITE; PS00118; PA2_HIS; 1.
1: Evidence at protein level;
3D-structure; Autocatalytic cleavage; Calcium; Complete proteome;
Direct protein sequencing; Disulfide bond; Hydrolase;
Lipid degradation; Lipid metabolism; Metal-binding; Polymorphism;
Reference proteome; Secreted; Signal; Zymogen.
SIGNAL 1 15 {ECO:0000269|PubMed:7060561}.
PROPEP 16 22 Activation peptide.
{ECO:0000269|PubMed:6349696}.
/FTId=PRO_0000022739.
CHAIN 23 148 Phospholipase A2.
{ECO:0000269|PubMed:3028739}.
/FTId=PRO_0000022740.
ACT_SITE 70 70 {ECO:0000250}.
ACT_SITE 121 121 {ECO:0000250}.
METAL 50 50 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 52 52 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 54 54 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 71 71 Calcium. {ECO:0000250}.
DISULFID 33 99 {ECO:0000269|PubMed:19297324}.
DISULFID 49 146 {ECO:0000269|PubMed:19297324}.
DISULFID 51 67 {ECO:0000269|PubMed:19297324}.
DISULFID 66 127 {ECO:0000269|PubMed:19297324}.
DISULFID 73 120 {ECO:0000269|PubMed:19297324}.
DISULFID 83 113 {ECO:0000269|PubMed:19297324}.
DISULFID 106 118 {ECO:0000269|PubMed:19297324}.
VARIANT 16 16 D -> A (in dbSNP:rs5632).
/FTId=VAR_011911.
VARIANT 89 89 N -> K (in dbSNP:rs5636).
/FTId=VAR_011913.
VARIANT 89 89 N -> T (in dbSNP:rs5635).
/FTId=VAR_011912.
CONFLICT 144 144 Missing (in Ref. 8; AA sequence).
{ECO:0000305}.
HELIX 21 23 {ECO:0000244|PDB:3ELO}.
HELIX 25 30 {ECO:0000244|PDB:3ELO}.
HELIX 31 33 {ECO:0000244|PDB:3ELO}.
HELIX 40 44 {ECO:0000244|PDB:3ELO}.
STRAND 45 47 {ECO:0000244|PDB:3ELO}.
TURN 48 50 {ECO:0000244|PDB:3ELO}.
STRAND 51 54 {ECO:0000244|PDB:3ELO}.
HELIX 62 77 {ECO:0000244|PDB:3ELO}.
HELIX 81 83 {ECO:0000244|PDB:3ELO}.
TURN 84 87 {ECO:0000244|PDB:3ELO}.
STRAND 97 100 {ECO:0000244|PDB:3ELO}.
STRAND 103 106 {ECO:0000244|PDB:3ELO}.
HELIX 112 130 {ECO:0000244|PDB:3ELO}.
HELIX 135 137 {ECO:0000244|PDB:3ELO}.
HELIX 142 145 {ECO:0000244|PDB:3ELO}.
SEQUENCE 148 AA; 16360 MW; C8E38B2B64AEE8CB CRC64;
MKLLVLAVLL TVAAADSGIS PRAVWQFRKM IKCVIPGSDP FLEYNNYGCY CGLGGSGTPV
DELDKCCQTH DNCYDQAKKL DSCKFLLDNP YTHTYSYSCS GSAITCSSKN KECEAFICNC
DRNAAICFSK APYNKAHKNL DTKKYCQS


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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
10-663-45343 Secreted Phospholipase A2-IB (sPLA2-IB) Human - EC 3.1.1.4; Phosphatidylcholine 2-acylhydrolase; Group IB phospholipase A2 N_A 1 mg
10-663-45343 Secreted Phospholipase A2-IB (sPLA2-IB) Human - EC 3.1.1.4; Phosphatidylcholine 2-acylhydrolase; Group IB phospholipase A2 N_A 0.01 mg
10-663-45343 Secreted Phospholipase A2-IB (sPLA2-IB) Human - EC 3.1.1.4; Phosphatidylcholine 2-acylhydrolase; Group IB phospholipase A2 N_A 0.002 mg
10-663-45001 Phospholipase A2 Bee Venom Protein (PA2-BVP) - EC 3.1.1.4; Phosphatidylcholine 2-acylhydrolase; Group IB phospholipase A2 N_A 1 mg
10-663-45001 Phospholipase A2 Bee Venom Protein (PA2-BVP) - EC 3.1.1.4; Phosphatidylcholine 2-acylhydrolase; Group IB phospholipase A2 N_A 0.1 mg
10-663-45001 Phospholipase A2 Bee Venom Protein (PA2-BVP) - EC 3.1.1.4; Phosphatidylcholine 2-acylhydrolase; Group IB phospholipase A2 N_A 0.5 mg
E0576b ELISA kit Bos taurus,Bovine,Group IB phospholipase A2,Phosphatidylcholine 2-acylhydrolase 1B,Phospholipase A2,PLA2G1B 96T
10-663-45346 Secreted Phospholipase A2-V (sPLA2-V) Human - EC 3.1.1.4; Phosphatidylcholine 2-acylhydrolase; PLA2-10; Group V phospholipase A2 N_A 0.002 mg
E0576r ELISA kit Group IB phospholipase A2,Phosphatidylcholine 2-acylhydrolase 1B,Phospholipase A2,Pla2g1b,Rat,Rattus norvegicus 96T
E0576b ELISA Bos taurus,Bovine,Group IB phospholipase A2,Phosphatidylcholine 2-acylhydrolase 1B,Phospholipase A2,PLA2G1B 96T
10-663-45346 Secreted Phospholipase A2-V (sPLA2-V) Human - EC 3.1.1.4; Phosphatidylcholine 2-acylhydrolase; PLA2-10; Group V phospholipase A2 N_A 0.01 mg
E0576r ELISA Group IB phospholipase A2,Phosphatidylcholine 2-acylhydrolase 1B,Phospholipase A2,Pla2g1b,Rat,Rattus norvegicus 96T
10-663-45346 Secreted Phospholipase A2-V (sPLA2-V) Human - EC 3.1.1.4; Phosphatidylcholine 2-acylhydrolase; PLA2-10; Group V phospholipase A2 N_A 1 mg
U0576r CLIA Group IB phospholipase A2,Phosphatidylcholine 2-acylhydrolase 1B,Phospholipase A2,Pla2g1b,Rat,Rattus norvegicus 96T
U0576b CLIA Bos taurus,Bovine,Group IB phospholipase A2,Phosphatidylcholine 2-acylhydrolase 1B,Phospholipase A2,PLA2G1B 96T
E0576Rb ELISA kit Group IB phospholipase A2,Oryctolagus cuniculus,Phosphatidylcholine 2-acylhydrolase 1B,Phospholipase A2,PLA2G1B,Rabbit 96T
E0576p ELISA kit Group IB phospholipase A2,Phosphatidylcholine 2-acylhydrolase 1B,Phospholipase A2, major isoenzyme,Pig,PLA2G1B,Sus scrofa 96T
E0576Rb ELISA Group IB phospholipase A2,Oryctolagus cuniculus,Phosphatidylcholine 2-acylhydrolase 1B,Phospholipase A2,PLA2G1B,Rabbit 96T
E0576p ELISA Group IB phospholipase A2,Phosphatidylcholine 2-acylhydrolase 1B,Phospholipase A2, major isoenzyme,Pig,PLA2G1B,Sus scrofa 96T
U0576p CLIA Group IB phospholipase A2,Phosphatidylcholine 2-acylhydrolase 1B,Phospholipase A2, major isoenzyme,Pig,PLA2G1B,Sus scrofa 96T
U0576Rb CLIA Group IB phospholipase A2,Oryctolagus cuniculus,Phosphatidylcholine 2-acylhydrolase 1B,Phospholipase A2,PLA2G1B,Rabbit 96T


 

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