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Q9EPR2

- PG12A_MOUSE

UniProt

Q9EPR2 - PG12A_MOUSE

Protein

Group XIIA secretory phospholipase A2

Gene

Pla2g12a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 2 (16 Apr 2002)
      Previous versions | rss
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    Functioni

    PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Does not exhibit detectable activity toward sn-2-arachidonoyl- or linoleoyl-phosphatidylcholine or -phosphatidylethanolamine By similarity.By similarity

    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 bindingi91 – 911Calcium; via carbonyl oxygenBy similarity
    Metal bindingi93 – 931Calcium; via carbonyl oxygenBy similarity
    Metal bindingi95 – 951Calcium; via carbonyl oxygenBy similarity
    Active sitei113 – 1131PROSITE-ProRule annotation
    Metal bindingi114 – 1141CalciumBy similarity
    Active sitei128 – 1281PROSITE-ProRule annotation

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. phospholipase A2 activity Source: MGI

    GO - Biological processi

    1. lipid catabolic process Source: MGI
    2. phospholipid metabolic process Source: InterPro

    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:
    Group XIIA secretory phospholipase A2 (EC:3.1.1.4)
    Short name:
    GXII sPLA2
    Short name:
    sPLA2-XII
    Alternative name(s):
    Phosphatidylcholine 2-acylhydrolase 12A
    Gene namesi
    Name:Pla2g12a
    Synonyms:Pla2g12
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:1913600. Pla2g12a.

    Subcellular locationi

    Secreted. Cytoplasm By similarity

    GO - Cellular componenti

    1. endoplasmic reticulum Source: MGI
    2. extracellular region Source: UniProtKB-SubCell
    3. Golgi apparatus Source: MGI
    4. intracellular Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence AnalysisAdd
    BLAST
    Chaini26 – 192167Group XIIA secretory phospholipase A2PRO_0000022771Add
    BLAST

    Proteomic databases

    PaxDbiQ9EPR2.
    PRIDEiQ9EPR2.

    PTM databases

    PhosphoSiteiQ9EPR2.

    Expressioni

    Gene expression databases

    BgeeiQ9EPR2.
    CleanExiMM_PLA2G12A.
    GenevestigatoriQ9EPR2.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9EPR2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the phospholipase A2 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG68062.
    GeneTreeiENSGT00390000008798.
    HOGENOMiHOG000247019.
    HOVERGENiHBG053577.
    InParanoidiQ9EPR2.
    KOiK01047.
    OMAiKICRNVQ.
    OrthoDBiEOG7J1818.
    PhylomeDBiQ9EPR2.
    TreeFamiTF323302.

    Family and domain databases

    Gene3Di1.20.90.10. 1 hit.
    InterProiIPR013090. PLipase_A2_AS.
    IPR016090. PLipase_A2_dom.
    IPR010711. PLipase_A2_secretory_G12.
    [Graphical view]
    PANTHERiPTHR12824. PTHR12824. 1 hit.
    PfamiPF06951. PLA2G12. 1 hit.
    [Graphical view]
    SUPFAMiSSF48619. SSF48619. 1 hit.
    PROSITEiPS00118. PA2_HIS. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9EPR2-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MVTPRPAPAR SPALLLLLLL ATARGQEQDQ TTDWRATLKT IRNGIHKIDT    50
    YLNAALDLLG GEDGLCQYKC SDGSKPVPRY GYKPSPPNGC GSPLFGVHLN 100
    IGIPSLTKCC NQHDRCYETC GKSKNDCDEE FQYCLSKICR DVQKTLGLSQ 150
    NVQACETTVE LLFDSVIHLG CKPYLDSQRA ACWCRYEEKT DL 192
    Length:192
    Mass (Da):21,319
    Last modified:April 16, 2002 - v2
    Checksum:i670ACE8F6AB6FCA2
    GO
    Isoform 2 (identifier: Q9EPR2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-73: MVTPRPAPAR...GLCQYKCSDG → MKDYHSGPGKYWEPFAFPVGCSGTEEEEGLRIGR

    Show »
    Length:153
    Mass (Da):17,199
    Checksum:iC9021DB502233080
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti11 – 111S → G in AAG23336. (PubMed:11278438)Curated
    Sequence conflicti173 – 1731P → H in BAB26094. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7373MVTPR…KCSDG → MKDYHSGPGKYWEPFAFPVG CSGTEEEEGLRIGR in isoform 2. CuratedVSP_004509Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY007381 mRNA. Translation: AAG23336.1.
    AY007382 mRNA. Translation: AAG23337.1.
    AK003183 mRNA. No translation available.
    AK009133 mRNA. Translation: BAB26094.1.
    AK010011 mRNA. Translation: BAB26641.1.
    AK010174 mRNA. Translation: BAB26747.1.
    AK163693 mRNA. Translation: BAE37460.1.
    BC051117 mRNA. Translation: AAH51117.1.
    CCDSiCCDS17836.1. [Q9EPR2-1]
    CCDS17837.1. [Q9EPR2-2]
    RefSeqiNP_075685.2. NM_023196.4. [Q9EPR2-1]
    NP_904359.1. NM_183423.3. [Q9EPR2-2]
    UniGeneiMm.151951.

    Genome annotation databases

    EnsembliENSMUST00000029629; ENSMUSP00000029629; ENSMUSG00000027999. [Q9EPR2-1]
    ENSMUST00000061165; ENSMUSP00000053651; ENSMUSG00000027999. [Q9EPR2-2]
    GeneIDi66350.
    KEGGimmu:66350.
    UCSCiuc008rip.2. mouse. [Q9EPR2-2]
    uc012cxt.1. mouse. [Q9EPR2-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY007381 mRNA. Translation: AAG23336.1 .
    AY007382 mRNA. Translation: AAG23337.1 .
    AK003183 mRNA. No translation available.
    AK009133 mRNA. Translation: BAB26094.1 .
    AK010011 mRNA. Translation: BAB26641.1 .
    AK010174 mRNA. Translation: BAB26747.1 .
    AK163693 mRNA. Translation: BAE37460.1 .
    BC051117 mRNA. Translation: AAH51117.1 .
    CCDSi CCDS17836.1. [Q9EPR2-1 ]
    CCDS17837.1. [Q9EPR2-2 ]
    RefSeqi NP_075685.2. NM_023196.4. [Q9EPR2-1 ]
    NP_904359.1. NM_183423.3. [Q9EPR2-2 ]
    UniGenei Mm.151951.

    3D structure databases

    ProteinModelPortali Q9EPR2.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q9EPR2.

    Proteomic databases

    PaxDbi Q9EPR2.
    PRIDEi Q9EPR2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000029629 ; ENSMUSP00000029629 ; ENSMUSG00000027999 . [Q9EPR2-1 ]
    ENSMUST00000061165 ; ENSMUSP00000053651 ; ENSMUSG00000027999 . [Q9EPR2-2 ]
    GeneIDi 66350.
    KEGGi mmu:66350.
    UCSCi uc008rip.2. mouse. [Q9EPR2-2 ]
    uc012cxt.1. mouse. [Q9EPR2-1 ]

    Organism-specific databases

    CTDi 81579.
    MGIi MGI:1913600. Pla2g12a.

    Phylogenomic databases

    eggNOGi NOG68062.
    GeneTreei ENSGT00390000008798.
    HOGENOMi HOG000247019.
    HOVERGENi HBG053577.
    InParanoidi Q9EPR2.
    KOi K01047.
    OMAi KICRNVQ.
    OrthoDBi EOG7J1818.
    PhylomeDBi Q9EPR2.
    TreeFami TF323302.

    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

    NextBioi 321399.
    PROi Q9EPR2.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9EPR2.
    CleanExi MM_PLA2G12A.
    Genevestigatori Q9EPR2.

    Family and domain databases

    Gene3Di 1.20.90.10. 1 hit.
    InterProi IPR013090. PLipase_A2_AS.
    IPR016090. PLipase_A2_dom.
    IPR010711. PLipase_A2_secretory_G12.
    [Graphical view ]
    PANTHERi PTHR12824. PTHR12824. 1 hit.
    Pfami PF06951. PLA2G12. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48619. SSF48619. 1 hit.
    PROSITEi PS00118. PA2_HIS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel group of phospholipase A2s preferentially expressed in type 2 helper T cells."
      Ho I.C., Arm J.P., Bingham C.O. III, Choi A., Austen K.F., Glimcher L.H.
      J. Biol. Chem. 276:18321-18326(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: AKR.
    2. "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: Cerebellum, Embryo and Tongue.
    3. "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] (ISOFORM 1).
      Tissue: Olfactory epithelium.

    Entry informationi

    Entry nameiPG12A_MOUSE
    AccessioniPrimary (citable) accession number: Q9EPR2
    Secondary accession number(s): Q3TQC4
    , Q9CQR3, Q9CTL1, Q9D7L3, Q9EPR1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 16, 2002
    Last sequence update: April 16, 2002
    Last modified: October 1, 2014
    This is version 113 of the entry and version 2 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