Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P04054 (PA21B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phospholipase A2

EC=3.1.1.4
Alternative name(s):
Group IB phospholipase A2
Phosphatidylcholine 2-acylhydrolase 1B
Gene names
Name:PLA2G1B
Synonyms:PLA2, PLA2A, PPLA2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length148 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.9

Catalytic activity

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subunit structure

Monomer or homodimer By similarity. The inactive pro-form is a homotrimer. Ref.9

Subcellular location

Secreted. Note: secreted from pancreatic acinar cells in its inactive form. Ref.9

Post-translational modification

Activated by trypsin cleavage in the duodenum. Can also be activated by thrombin or autocatalytically.

Sequence similarities

Belongs to the phospholipase A2 family.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   PTMAutocatalytic cleavage
Disulfide bond
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament organization

Traceable author statement PubMed 9886417. Source: ProtInc

activation of MAPK activity

Inferred from sequence or structural similarity PubMed 15528384PubMed 16005851. Source: BHF-UCL

activation of phospholipase A2 activity

Traceable author statement PubMed 17981679. Source: BHF-UCL

arachidonic acid secretion

Traceable author statement PubMed 12423354. Source: BHF-UCL

cellular response to insulin stimulus

Inferred from sequence or structural similarity PubMed 1918029. Source: BHF-UCL

fatty acid biosynthetic process

Inferred from direct assay PubMed 1918029. Source: BHF-UCL

glucose transport

Inferred from sequence or structural similarity PubMed 1918029. Source: BHF-UCL

glycerophospholipid biosynthetic process

Traceable author statement. Source: Reactome

interleukin-8 production

Inferred from sequence or structural similarity PubMed 15528384. Source: BHF-UCL

intracellular signal transduction

Inferred from sequence or structural similarity PubMed 15528384. Source: BHF-UCL

leukotriene biosynthetic process

Inferred from sequence or structural similarity PubMed 16005851. Source: BHF-UCL

multicellular organismal lipid catabolic process

Inferred from direct assay Ref.7. Source: BHF-UCL

neutrophil chemotaxis

Inferred from sequence or structural similarity PubMed 16005851. Source: BHF-UCL

neutrophil mediated immunity

Inferred from sequence or structural similarity PubMed 16005851. Source: BHF-UCL

phosphatidic acid biosynthetic process

Traceable author statement. Source: Reactome

phosphatidylcholine acyl-chain remodeling

Traceable author statement. Source: Reactome

phosphatidylcholine metabolic process

Inferred from direct assay Ref.7. Source: BHF-UCL

phosphatidylethanolamine acyl-chain remodeling

Traceable author statement. Source: Reactome

phosphatidylglycerol acyl-chain remodeling

Traceable author statement. Source: Reactome

phosphatidylinositol acyl-chain remodeling

Traceable author statement. Source: Reactome

phosphatidylserine acyl-chain remodeling

Traceable author statement. Source: Reactome

phospholipid metabolic process

Traceable author statement. Source: Reactome

positive regulation of DNA replication

Inferred from direct assay PubMed 1918029. Source: BHF-UCL

positive regulation of NF-kappaB transcription factor activity

Inferred from sequence or structural similarity PubMed 15528384. Source: BHF-UCL

positive regulation of calcium ion transport into cytosol

Inferred from sequence or structural similarity PubMed 15528384. Source: BHF-UCL

positive regulation of fibroblast proliferation

Inferred by curator PubMed 1918029. Source: BHF-UCL

positive regulation of immune response

Inferred from sequence or structural similarity PubMed 16005851. Source: BHF-UCL

positive regulation of protein secretion

Traceable author statement PubMed 17981679. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity PubMed 15528384. Source: BHF-UCL

signal transduction

Traceable author statement PubMed 9886417. Source: ProtInc

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcell surface

Inferred from direct assay PubMed 1918029. Source: BHF-UCL

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay Ref.7. Source: BHF-UCL

secretory granule

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionbile acid binding

Inferred from sequence or structural similarity Ref.7. Source: BHF-UCL

calcium ion binding

Inferred from direct assay Ref.7. Source: BHF-UCL

calcium-dependent phospholipase A2 activity

Inferred from direct assay Ref.7. Source: BHF-UCL

phospholipase A2 activity

Inferred from direct assay PubMed 1918029. Source: BHF-UCL

receptor binding

Inferred from physical interaction PubMed 7721806. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515 Ref.7
Propeptide16 – 227Activation peptide Ref.7
PRO_0000022739
Chain23 – 148126Phospholipase A2 Ref.1
PRO_0000022740

Sites

Active site701 By similarity
Active site1211 By similarity
Metal binding501Calcium; via carbonyl oxygen By similarity
Metal binding521Calcium; via carbonyl oxygen By similarity
Metal binding541Calcium; via carbonyl oxygen By similarity
Metal binding711Calcium By similarity

Amino acid modifications

Disulfide bond33 ↔ 99 Ref.9
Disulfide bond49 ↔ 146 Ref.9
Disulfide bond51 ↔ 67 Ref.9
Disulfide bond66 ↔ 127 Ref.9
Disulfide bond73 ↔ 120 Ref.9
Disulfide bond83 ↔ 113 Ref.9
Disulfide bond106 ↔ 118 Ref.9

Natural variations

Natural variant161D → A.
Corresponds to variant rs5632 [ dbSNP | Ensembl ].
VAR_011911
Natural variant891N → K.
Corresponds to variant rs5636 [ dbSNP | Ensembl ].
VAR_011913
Natural variant891N → T.
Corresponds to variant rs5635 [ dbSNP | Ensembl ].
VAR_011912

Experimental info

Sequence conflict1441Missing AA sequence Ref.8

Secondary structure

.......................... 148
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04054 [UniParc].

Last modified February 1, 1991. Version 3.
Checksum: C8E38B2B64AEE8CB

FASTA14816,360
        10         20         30         40         50         60 
MKLLVLAVLL TVAAADSGIS PRAVWQFRKM IKCVIPGSDP FLEYNNYGCY CGLGGSGTPV 

        70         80         90        100        110        120 
DELDKCCQTH DNCYDQAKKL DSCKFLLDNP YTHTYSYSCS GSAITCSSKN KECEAFICNC 

       130        140 
DRNAAICFSK APYNKAHKNL DTKKYCQS 

« Hide

References

« Hide 'large scale' references
[1]"Pancreatic phospholipase A2: isolation of the human gene and cDNAs from porcine pancreas and human lung."
Seilhamer J.J., Randall T.L., Yamanaka M., Johnson L.K.
DNA 5:519-527(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Tissue: Lung.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Urinary bladder.
[3]NIEHS SNPs program
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"The finished DNA sequence of human chromosome 12."
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. expand/collapse author list , 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.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]"Studies on prophospholipase A2 and its enzyme from human pancreatic juice. Catalytic properties and sequence of the N-terminal region."
Grataroli R., Dijkman R., Dutilh C.E., van der Ouderaa F., de Haas G.H., Figarella C.
Eur. J. Biochem. 122:111-117(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 16-22.
Tissue: Pancreas.
[8]"The complete primary structure of phospholipase A2 from human pancreas."
Verheij H.M., Westerman J., Sternby B., de Haas G.H.
Biochim. Biophys. Acta 747:93-99(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 23-148.
Tissue: Pancreas.
[9]"Structural insight into the activation mechanism of human pancreatic prophospholipase A2."
Xu W., Yi L., Feng Y., Chen L., Liu J.
J. Biol. Chem. 284:16659-16666(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 16-148, DISULFIDE BONDS, SUBUNIT, AUTOPROTEOLYTIC CLEAVAGE, SUBCELLULAR LOCATION, FUNCTION.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M21056, M22970 Genomic DNA. Translation: AAA60107.1.
M21054 mRNA. Translation: AAA36450.1.
AK311830 mRNA. Translation: BAG34772.1.
AY438977 Genomic DNA. Translation: AAR05441.1.
AC003982 Genomic DNA. Translation: AAB95635.1.
CH471054 Genomic DNA. Translation: EAW98184.1.
BC106725 mRNA. Translation: AAI06726.1.
BC106726 mRNA. Translation: AAI06727.1.
PIRPSHU. C25793.
RefSeqNP_000919.1. NM_000928.2.
UniGeneHs.992.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YSKmodel-A23-146[»]
3ELOX-ray1.55A16-148[»]
ProteinModelPortalP04054.
SMRP04054. Positions 16-148.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111336. 2 interactions.
IntActP04054. 1 interaction.
STRING9606.ENSP00000312286.

Chemistry

BindingDBP04054.
ChEMBLCHEMBL4426.

PTM databases

PhosphoSiteP04054.

Polymorphism databases

DMDM129404.

Proteomic databases

PaxDbP04054.
PRIDEP04054.

Protocols and materials databases

DNASU5319.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000308366; ENSP00000312286; ENSG00000170890.
GeneID5319.
KEGGhsa:5319.
UCSCuc001tyd.3. human.

Organism-specific databases

CTD5319.
GeneCardsGC12M120759.
HGNCHGNC:9030. PLA2G1B.
HPAHPA047822.
HPA060803.
MIM172410. gene.
neXtProtNX_P04054.
PharmGKBPA33361.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG290764.
HOGENOMHOG000231749.
HOVERGENHBG008137.
InParanoidP04054.
KOK01047.
OMADELDKCC.
OrthoDBEOG7N63PF.
PhylomeDBP04054.
TreeFamTF319283.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP04054.
BgeeP04054.
CleanExHS_PLA2G1B.
GenevestigatorP04054.

Family and domain databases

Gene3D1.20.90.10. 1 hit.
InterProIPR001211. PLipase_A2.
IPR013090. PLipase_A2_AS.
IPR016090. PLipase_A2_dom.
[Graphical view]
PANTHERPTHR11716. PTHR11716. 1 hit.
PfamPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSPR00389. PHPHLIPASEA2.
SMARTSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMSSF48619. SSF48619. 1 hit.
PROSITEPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPLA2G1B. human.
EvolutionaryTraceP04054.
GeneWikiPLA2G1B.
GenomeRNAi5319.
NextBio20578.
PROP04054.
SOURCESearch...

Entry information

Entry namePA21B_HUMAN
AccessionPrimary (citable) accession number: P04054
Secondary accession number(s): B2R4H5, Q3KPI1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: February 1, 1991
Last modified: April 16, 2014
This is version 151 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM