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Q9Z0Y2

- PA21B_MOUSE

UniProt

Q9Z0Y2 - PA21B_MOUSE

Protein

Phospholipase A2

Gene

Pla2g1b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
  1. 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

    Binds 1 calcium 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. fatty acid biosynthetic process Source: Ensembl
    2. multicellular organismal lipid catabolic process Source: Ensembl
    3. phosphatidylcholine metabolic process Source: Ensembl
    4. phospholipid catabolic process Source: MGI
    5. positive regulation of DNA replication Source: Ensembl

    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

    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

    ArrayExpressiQ9Z0Y2.
    BgeeiQ9Z0Y2.
    CleanExiMM_PLA2G1B.
    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.
    GeneTreeiENSGT00710000106605.
    HOGENOMiHOG000231749.
    HOVERGENiHBG008137.
    InParanoidiA6H6K5.
    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

    MKLLLLAALL TAGAAAHSIS PRAVWQFRNM IKCTIPGSDP LKDYNNYGCY    50
    CGLGGWGTPV DDLDRCCQTH DHCYSQAKKL ESCKFLIDNP YTNTYSYSCS 100
    GSEITCSAKN NKCEDFICNC DREAAICFSK VPYNKEYKNL DTGKFC 146
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 ENSGT00710000106605.
    HOGENOMi HOG000231749.
    HOVERGENi HBG008137.
    InParanoidi A6H6K5.
    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

    ArrayExpressi Q9Z0Y2.
    Bgeei Q9Z0Y2.
    CleanExi MM_PLA2G1B.
    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

    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: October 1, 2014
    This is version 132 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