Reviewed, UniProtKB/Swiss-Prot P04054 (PA21B_HUMAN)

Names and origin

Protein names

Recommended name:
    Phospholipase A2
    EC=3.1.1.4
Alternative name(s):
    Phosphatidylcholine 2-acylhydrolase
    Group IB phospholipase A2

Gene names

Name:	PLA2G1B
Synonyms:	PLA2, PLA2A, PPLA2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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.
Catalytic activity	Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.
Cofactor	Binds 1 calcium ion per subunit By similarity.
Subcellular location	Secreted.
Sequence similarities	Belongs to the phospholipase A2 family.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	actin filament organization Traceable author statement. Source: ProtInc activation of MAPK activity Inferred from sequence or structural similarity. Source: UniProtKB activation of phospholipase A2 activity Traceable author statement. Source: UniProtKB arachidonic acid secretion Traceable author statement. Source: UniProtKB cellular response to insulin stimulus Inferred from sequence or structural similarity. Source: UniProtKB glucose transport Inferred from sequence or structural similarity. Source: UniProtKB interleukin-8 production Inferred from sequence or structural similarity. Source: UniProtKB leukotriene biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB multicellular organismal lipid catabolic process Ref.7 Inferred from direct assay. Source: UniProtKB neutrophil chemotaxis Inferred from sequence or structural similarity. Source: UniProtKB neutrophil mediated immunity Inferred from sequence or structural similarity. Source: UniProtKB phosphatidylcholine metabolic process Ref.7 Inferred from direct assay. Source: UniProtKB positive regulation of DNA replication Inferred from direct assay. Source: UniProtKB positive regulation of NF-kappaB transcription factor activity Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of calcium ion transport into cytosol Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of fibroblast proliferation Inferred by curator. Source: UniProtKB positive regulation of immune response Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of protein secretion Traceable author statement. Source: UniProtKB positive regulation of specific transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	extracellular space Ref.7 Inferred from direct assay. Source: UniProtKB
Molecular function	bile acid binding Ref.7 Inferred from sequence or structural similarity. Source: UniProtKB calcium ion binding Ref.7 Inferred from direct assay. Source: UniProtKB calcium-dependent phospholipase A2 activity Ref.7 Inferred from direct assay. Source: UniProtKB cell surface binding Inferred from direct assay. Source: UniProtKB receptor binding Inferred from direct assay. Source: UniProtKB
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.8		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
	Disulfide bond	49 ↔ 146
	Disulfide bond	51 ↔ 67
	Disulfide bond	66 ↔ 127
	Disulfide bond	73 ↔ 120
	Disulfide bond	83 ↔ 113
	Disulfide bond	106 ↔ 118
Natural variations
	Natural variant	16	1	D → A: dbSNP rs5632.		VAR_011911
	Natural variant	89	1	N → K: dbSNP rs5636.		VAR_011913
	Natural variant	89	1	N → T: dbSNP rs5635.		VAR_011912
Experimental info
	Sequence conflict	144	1	Missing AA sequence Ref.8

Sequences

	Sequence		Length	Mass (Da)
	P04054-1 [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: 3028739] [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: 14702039] [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: 16541075] [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: 15489334] [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: 7060561] [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: 6349696] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-148. Tissue: Pancreas.
+	Additional computationally mapped references.

Web resources

NIEHS SNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

UniGene

Hs.992

3D structure databases

PDBPDBe

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

ModBase

Search...

PTM databases

PhosphoSite

P04054.

Proteomic databases

PRIDE

P04054.

Genome annotation databases

Ensembl

ENSG00000170890. Homo sapiens. [Contig view]

GeneID

5319.

KEGG

hsa:5319.

UCSC

uc001tyd.1. human.

Organism-specific databases

GeneCards

GC12M119244.

H-InvDB

HIX0011060.

HGNC

HGNC:9030. PLA2G1B.

MIM

172410. gene.

PharmGKB

PA33361.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P04054.

HOVERGEN

P04054.

OMA

P04054. AKKLDSC.

Enzyme and pathway databases

BRENDA

3.1.1.4. 247.

Pathway_Interaction_DB

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

Gene expression databases

ArrayExpress

P04054.

Bgee

P04054.

CleanEx

HS_PLA2G1B.

GermOnline

ENSG00000170890. Homo sapiens.

Family and domain databases

InterPro

IPR016090. Phospholipase_A2.
IPR013090. Phospholipase_A2_AS.
IPR001211. Phospholipase_A2_euk.
[Graphical view]

Gene3D

G3DSA:1.20.90.10. Phospholipase_A2. 1 hit.

PANTHER

PTHR11716. Phospholipase_A2. 1 hit.

Pfam

PF00068. Phospholip_A2_1. 1 hit.
[Graphical view]

PRINTS

PR00389. PHPHLIPASEA2.

ProDom

PD000303. PhospholipaseA2. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00085. PA2c. 1 hit.
[Graphical view]

PROSITE

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

ProtoNet

Search...

Other Resources

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:	July 7, 2009
This is version 100 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)