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Q9Z0Y2 (PA21B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·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
PLA2-Ib
Phosphatidylcholine 2-acylhydrolase 1B
Gene names
Name:Pla2g1b
Synonyms:Pla2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length146 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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.

Catalytic activity

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subunit structure

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

Subcellular location

Secreted. Note: secreted from pancreatic acinar cells in its inactive form By similarity.

Post-translational modification

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

Sequence similarities

Belongs to the phospholipase A2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515 By similarity
Propeptide16 – 227Activation peptide By similarity
PRO_0000022741
Chain23 – 146124Phospholipase A2
PRO_0000022742

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 By similarity
Disulfide bond49 ↔ 146 By similarity
Disulfide bond51 ↔ 67 By similarity
Disulfide bond66 ↔ 127 By similarity
Disulfide bond73 ↔ 120 By similarity
Disulfide bond83 ↔ 113 By similarity
Disulfide bond106 ↔ 118 By similarity

Experimental info

Sequence conflict521G → S in BAB26212. Ref.6
Sequence conflict581T → P in BAB26212. Ref.6
Sequence conflict78 – 792KK → EN in BAB26212. Ref.6
Sequence conflict871I → R in BAB26212. Ref.6
Sequence conflict951Y → F in BAB26212. Ref.6
Sequence conflict1021S → G in BAB26212. Ref.6
Sequence conflict1221R → S in BAB25608. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q9Z0Y2 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 59500C68845B7C81

FASTA14616,290
        10         20         30         40         50         60 
MKLLLLAALL TAGAAAHSIS PRAVWQFRNM IKCTIPGSDP LKDYNNYGCY CGLGGWGTPV 

        70         80         90        100        110        120 
DDLDRCCQTH DHCYSQAKKL ESCKFLIDNP YTNTYSYSCS GSEITCSAKN NKCEDFICNC 

       130        140 
DREAAICFSK VPYNKEYKNL DTGKFC 

« Hide

References

« Hide 'large scale' references
[1]"Isolation, characterization and chromosomal localization of mouse sPLA2-Ib gene."
Mandal A.K., Zhang Z., Mukherjee A.B.
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: 129/SvJ.
[2]"Both group IB and group IIA secreted phospholipases A2 are natural ligands of the mouse 180-kDa M-type receptor."
Cupillard L., Mulherkar R., Gomez N., Kadam S., Valentin E., Lazdunski M., Lambeau G.
J. Biol. Chem. 274:7043-7051(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Low molecular weight group IIA and group V phospholipase A(2) enzymes have different intracellular locations in mouse bone marrow-derived mast cells."
Bingham C.O. III, Fijneman R.J.A., Friend D.S., Goddeau R.P., Rogers R.A., Austen K.F., Arm J.P.
J. Biol. Chem. 274:31476-31484(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Lung.
[4]"Molecular structure and tissue-specific expression of the mouse pancreatic phospholipase A2 gene."
Richmond B.L., Hui D.Y.
Gene 244:65-72(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"Role of sPLA2-I in colorectal tumorigenesis."
Mandal A.K., Zhang Z., Popescu N., Mukherjee A.B.
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: 129/SvJ.
Tissue: Pancreas.
[6]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Pancreas, Small intestine, Stomach and Tongue.
[7]"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].
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF094611 Genomic DNA. Translation: AAF02298.1.
AF097637 mRNA. Translation: AAD19896.1.
AF162712 mRNA. Translation: AAD45806.1.
AF187852 mRNA. Translation: AAF44297.1.
AF094610 mRNA. Translation: AAG27064.1.
AK028104 mRNA. Translation: BAC25749.1.
AK028134 mRNA. Translation: BAC25763.1.
AK008936 mRNA. Translation: BAB25978.1.
AK007730 mRNA. Translation: BAB25218.1.
AK007797 mRNA. Translation: BAB25263.1.
AK008664 mRNA. Translation: BAB25819.1.
AK008668 mRNA. Translation: BAB25822.1.
AK008841 mRNA. Translation: BAB25922.1.
AK008934 mRNA. Translation: BAB25976.1.
AK008331 mRNA. Translation: BAB25608.1.
AK009314 mRNA. Translation: BAB26212.1.
BC145908 mRNA. Translation: AAI45909.1.
BC145910 mRNA. Translation: AAI45911.1.
CCDSCCDS19592.1.
RefSeqNP_035237.1. NM_011107.1.
XP_006530261.1. XM_006530198.1.
UniGeneMm.20190.

3D structure databases

ProteinModelPortalQ9Z0Y2.
SMRQ9Z0Y2. Positions 23-141.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBQ9Z0Y2.
ChEMBLCHEMBL4378.

PTM databases

PhosphoSiteQ9Z0Y2.

Proteomic databases

MaxQBQ9Z0Y2.
PRIDEQ9Z0Y2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031495; ENSMUSP00000031495; ENSMUSG00000029522.
GeneID18778.
KEGGmmu:18778.
UCSCuc008zdx.1. mouse.

Organism-specific databases

CTD5319.
MGIMGI:101842. Pla2g1b.

Phylogenomic databases

eggNOGNOG290764.
GeneTreeENSGT00710000106605.
HOGENOMHOG000231749.
HOVERGENHBG008137.
InParanoidA6H6K5.
KOK01047.
OMATHDHCYS.
OrthoDBEOG7N63PF.
PhylomeDBQ9Z0Y2.
TreeFamTF319283.

Gene expression databases

ArrayExpressQ9Z0Y2.
BgeeQ9Z0Y2.
CleanExMM_PLA2G1B.
GenevestigatorQ9Z0Y2.

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. mouse.
NextBio295023.
PROQ9Z0Y2.
SOURCESearch...

Entry information

Entry namePA21B_MOUSE
AccessionPrimary (citable) accession number: Q9Z0Y2
Secondary accession number(s): A6H6K5, Q9D7E2, Q9D884
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot