Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9Z0Y2

- PA21B_MOUSE

UniProt

Q9Z0Y2 - PA21B_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Phospholipase A2

Gene

Pla2g1b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

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 activityi

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.PROSITE-ProRule annotation

Cofactori

Ca2+By similarityNote: Binds 1 Ca(2+) ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi50 – 501Calcium; via carbonyl oxygenBy similarity
Metal bindingi52 – 521Calcium; via carbonyl oxygenBy similarity
Metal bindingi54 – 541Calcium; via carbonyl oxygenBy similarity
Active sitei70 – 701By similarity
Metal bindingi71 – 711CalciumBy similarity
Active sitei121 – 1211By similarity

GO - Molecular functioni

  1. calcium-dependent phospholipase A2 activity Source: Ensembl
  2. calcium ion binding Source: InterPro
  3. phospholipase A2 activity Source: MGI
  4. receptor binding Source: MGI

GO - Biological processi

  1. antibacterial humoral response Source: Ensembl
  2. defense response to Gram-positive bacterium Source: Ensembl
  3. fatty acid biosynthetic process Source: Ensembl
  4. innate immune response in mucosa Source: Ensembl
  5. multicellular organismal lipid catabolic process Source: Ensembl
  6. phosphatidylcholine metabolic process Source: Ensembl
  7. phospholipid catabolic process Source: MGI
  8. positive regulation of DNA replication Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_188640. Synthesis of PA.
REACT_199024. Acyl chain remodelling of PI.
REACT_199027. Acyl chain remodelling of PE.
REACT_199030. Acyl chain remodelling of PS.
REACT_199038. Acyl chain remodelling of PC.
REACT_199039. Acyl chain remodelling of PG.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholipase A2 (EC:3.1.1.4)
Alternative name(s):
Group IB phospholipase A2
PLA2-Ib
Phosphatidylcholine 2-acylhydrolase 1B
Gene namesi
Name:Pla2g1b
Synonyms:Pla2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:101842. Pla2g1b.

Subcellular locationi

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

GO - Cellular componenti

  1. cell surface Source: Ensembl
  2. extracellular region Source: MGI
  3. extracellular space Source: Ensembl
  4. secretory granule Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515By similarityAdd
BLAST
Propeptidei16 – 227Activation peptideBy similarityPRO_0000022741
Chaini23 – 146124Phospholipase A2PRO_0000022742Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi33 ↔ 99By similarity
Disulfide bondi49 ↔ 146By similarity
Disulfide bondi51 ↔ 67By similarity
Disulfide bondi66 ↔ 127By similarity
Disulfide bondi73 ↔ 120By similarity
Disulfide bondi83 ↔ 113By similarity
Disulfide bondi106 ↔ 118By similarity

Post-translational modificationi

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

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Zymogen

Proteomic databases

MaxQBiQ9Z0Y2.
PRIDEiQ9Z0Y2.

PTM databases

PhosphoSiteiQ9Z0Y2.

Expressioni

Gene expression databases

BgeeiQ9Z0Y2.
CleanExiMM_PLA2G1B.
ExpressionAtlasiQ9Z0Y2. baseline and differential.
GenevestigatoriQ9Z0Y2.

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ9Z0Y2.
SMRiQ9Z0Y2. Positions 23-141.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the phospholipase A2 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG290764.
GeneTreeiENSGT00760000119160.
HOGENOMiHOG000231749.
HOVERGENiHBG008137.
InParanoidiQ9Z0Y2.
KOiK01047.
OMAiTHDHCYS.
OrthoDBiEOG7N63PF.
PhylomeDBiQ9Z0Y2.
TreeFamiTF319283.

Family and domain databases

Gene3Di1.20.90.10. 1 hit.
InterProiIPR001211. PLipase_A2.
IPR013090. PLipase_A2_AS.
IPR016090. PLipase_A2_dom.
[Graphical view]
PANTHERiPTHR11716. PTHR11716. 1 hit.
PfamiPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSiPR00389. PHPHLIPASEA2.
SMARTiSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMiSSF48619. SSF48619. 1 hit.
PROSITEiPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9Z0Y2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKLLLLAALL TAGAAAHSIS PRAVWQFRNM IKCTIPGSDP LKDYNNYGCY
60 70 80 90 100
CGLGGWGTPV DDLDRCCQTH DHCYSQAKKL ESCKFLIDNP YTNTYSYSCS
110 120 130 140
GSEITCSAKN NKCEDFICNC DREAAICFSK VPYNKEYKNL DTGKFC
Length:146
Mass (Da):16,290
Last modified:May 1, 1999 - v1
Checksum:i59500C68845B7C81
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti52 – 521G → S in BAB26212. (PubMed:16141072)Curated
Sequence conflicti58 – 581T → P in BAB26212. (PubMed:16141072)Curated
Sequence conflicti78 – 792KK → EN in BAB26212. (PubMed:16141072)Curated
Sequence conflicti87 – 871I → R in BAB26212. (PubMed:16141072)Curated
Sequence conflicti95 – 951Y → F in BAB26212. (PubMed:16141072)Curated
Sequence conflicti102 – 1021S → G in BAB26212. (PubMed:16141072)Curated
Sequence conflicti122 – 1221R → S in BAB25608. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19592.1.
RefSeqiNP_035237.1. NM_011107.1.
XP_006530261.1. XM_006530198.1.
UniGeneiMm.20190.

Genome annotation databases

EnsembliENSMUST00000031495; ENSMUSP00000031495; ENSMUSG00000029522.
GeneIDi18778.
KEGGimmu:18778.
UCSCiuc008zdx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS19592.1.
RefSeqi NP_035237.1. NM_011107.1.
XP_006530261.1. XM_006530198.1.
UniGenei Mm.20190.

3D structure databases

ProteinModelPortali Q9Z0Y2.
SMRi Q9Z0Y2. Positions 23-141.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi Q9Z0Y2.
ChEMBLi CHEMBL4378.

PTM databases

PhosphoSitei Q9Z0Y2.

Proteomic databases

MaxQBi Q9Z0Y2.
PRIDEi Q9Z0Y2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000031495 ; ENSMUSP00000031495 ; ENSMUSG00000029522 .
GeneIDi 18778.
KEGGi mmu:18778.
UCSCi uc008zdx.1. mouse.

Organism-specific databases

CTDi 5319.
MGIi MGI:101842. Pla2g1b.

Phylogenomic databases

eggNOGi NOG290764.
GeneTreei ENSGT00760000119160.
HOGENOMi HOG000231749.
HOVERGENi HBG008137.
InParanoidi Q9Z0Y2.
KOi K01047.
OMAi THDHCYS.
OrthoDBi EOG7N63PF.
PhylomeDBi Q9Z0Y2.
TreeFami TF319283.

Enzyme and pathway databases

Reactomei REACT_188640. Synthesis of PA.
REACT_199024. Acyl chain remodelling of PI.
REACT_199027. Acyl chain remodelling of PE.
REACT_199030. Acyl chain remodelling of PS.
REACT_199038. Acyl chain remodelling of PC.
REACT_199039. Acyl chain remodelling of PG.

Miscellaneous databases

ChiTaRSi Pla2g1b. mouse.
NextBioi 295023.
PROi Q9Z0Y2.
SOURCEi Search...

Gene expression databases

Bgeei Q9Z0Y2.
CleanExi MM_PLA2G1B.
ExpressionAtlasi Q9Z0Y2. baseline and differential.
Genevestigatori Q9Z0Y2.

Family and domain databases

Gene3Di 1.20.90.10. 1 hit.
InterProi IPR001211. PLipase_A2.
IPR013090. PLipase_A2_AS.
IPR016090. PLipase_A2_dom.
[Graphical view ]
PANTHERi PTHR11716. PTHR11716. 1 hit.
Pfami PF00068. Phospholip_A2_1. 1 hit.
[Graphical view ]
PRINTSi PR00389. PHPHLIPASEA2.
SMARTi SM00085. PA2c. 1 hit.
[Graphical view ]
SUPFAMi SSF48619. SSF48619. 1 hit.
PROSITEi PS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiPA21B_MOUSE
AccessioniPrimary (citable) accession number: Q9Z0Y2
Secondary accession number(s): A6H6K5, Q9D7E2, Q9D884
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1999
Last modified: November 26, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3