P04054 (PA21B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	148 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Lipid degradation Lipid metabolism
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase
PTM	Autocatalytic cleavage Disulfide bond Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	actin 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 glucose transport Inferred from sequence or structural similarity PubMed 1918029. Source: BHF-UCL interleukin-8 production Inferred from sequence or structural similarity PubMed 15528384. Source: BHF-UCL intracellular protein kinase cascade 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 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 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
Cellular_component	extracellular space Inferred from direct assay Ref.7. Source: BHF-UCL secretory granule Inferred from electronic annotation. Source: Compara
Molecular_function	bile 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 cell surface binding Inferred from direct assay PubMed 1918029. Source: BHF-UCL receptor binding Inferred from direct assay PubMed 1918029. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 15

15

Ref.7

Propeptide

16 – 22

7

Activation peptide Ref.7

PRO_0000022739

Chain

23 – 148

126

Phospholipase A2 Ref.1

PRO_0000022740

Sites

Active site

70

1

By similarity

Active site

121

1

By similarity

Metal binding

50

1

Calcium; via carbonyl oxygen By similarity

Metal binding

52

1

Calcium; via carbonyl oxygen By similarity

Metal binding

54

1

Calcium; via carbonyl oxygen By similarity

Metal binding

71

1

Calcium By similarity

Amino acid modifications

Disulfide bond

33 ↔ 99

Ref.9

Disulfide bond

49 ↔ 146

Ref.9

Disulfide bond

51 ↔ 67

Ref.9

Disulfide bond

66 ↔ 127

Ref.9

Disulfide bond

73 ↔ 120

Ref.9

Disulfide bond

83 ↔ 113

Ref.9

Disulfide bond

106 ↔ 118

Ref.9

Natural variations

Natural variant

16

1

D → A.
Corresponds to variant rs5632 [ dbSNP | Ensembl ].

VAR_011911

Natural variant

89

1

N → K.
Corresponds to variant rs5636 [ dbSNP | Ensembl ].

VAR_011913

Natural variant

89

1

N → T.
Corresponds to variant rs5635 [ dbSNP | Ensembl ].

VAR_011912

Experimental info

Sequence conflict

144

1

Missing AA sequence Ref.8

Secondary structure

1

.

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148

Helix Strand Turn

Details...

Helix

21 – 23

3

Helix

25 – 30

6

Helix

31 – 33

3

Helix

40 – 44

5

Beta strand

45 – 47

3

Turn

48 – 50

3

Beta strand

51 – 54

4

Helix

62 – 77

16

Helix

81 – 83

3

Turn

84 – 87

4

Beta strand

97 – 100

4

Beta strand

103 – 106

4

Helix

112 – 130

19

Helix

135 – 137

3

Helix

142 – 145

4

Sequences

	Sequence		Length	Mass (Da)
	P04054 [UniParc]. Last modified February 1, 1991. Version 3. Checksum: C8E38B2B64AEE8CB	FASTA	148	16,360
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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

NIEHS SNPs

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.

IPI

IPI00021792.

PIR

PSHU. C25793.

RefSeq

NP_000919.1. NM_000928.2.

UniGene

Hs.992.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YSK	model	-	A	23-146	[»]
3ELO	X-ray	1.55	A	16-148	[»]

ProteinModelPortal

P04054.

ModBase

Search...

Protein-protein interaction databases

IntAct

P04054. 1 interaction.

STRING

9606.ENSP00000312286.

PTM databases

PhosphoSite

P04054.

Polymorphism databases

DMDM

129404.

Proteomic databases

PaxDb

P04054.

PRIDE

P04054.

Protocols and materials databases

DNASU

5319.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000308366; ENSP00000312286; ENSG00000170890.

GeneID

5319.

KEGG

hsa:5319.

UCSC

uc001tyd.3. human.

Organism-specific databases

CTD

5319.

GeneCards

GC12M120759.

HGNC

HGNC:9030. PLA2G1B.

HPA

CAB022329.

MIM

172410. gene.

neXtProt

NX_P04054.

PharmGKB

PA33361.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG290764.

HOGENOM

HOG000231749.

HOVERGEN

HBG008137.

InParanoid

P04054.

KO

K01047.

OMA

NKECEAF.

OrthoDB

EOG4GHZQJ.

PhylomeDB

P04054.

Enzyme and pathway databases

Pathway_Interaction_DB

fcer1pathway. Fc-epsilon receptor I signaling in mast cells.

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

P04054.

Bgee

P04054.

CleanEx

HS_PLA2G1B.

Genevestigator

P04054.

GermOnline

ENSG00000170890. Homo sapiens.

Family and domain databases

Gene3D

1.20.90.10. 1 hit.

InterPro

IPR001211. PLipase_A2.
IPR013090. PLipase_A2_AS.
IPR016090. PLipase_A2_dom.
[Graphical view]

PANTHER

PTHR11716. PTHR11716. 1 hit.

Pfam

PF00068. Phospholip_A2_1. 1 hit.
[Graphical view]

PRINTS

PR00389. PHPHLIPASEA2.

SMART

SM00085. PA2c. 1 hit.
[Graphical view]

SUPFAM

SSF48619. PhospholipaseA2. 1 hit.

PROSITE

PS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P04054.

ChEMBL

CHEMBL4426.

ChiTaRS

PLA2G1B. human.

EvolutionaryTrace

P04054.

GenomeRNAi

5319.

NextBio

20578.

SOURCE

Search...

Entry information

Entry name

PA21B_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 143 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.