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Q9EPR2 (PG12A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Group XIIA secretory phospholipase A2

Short name=GXII sPLA2
Short name=sPLA2-XII
EC=3.1.1.4
Alternative name(s):
Phosphatidylcholine 2-acylhydrolase 12A
Gene names
Name:Pla2g12a
Synonyms:Pla2g12
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length192 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. Does not exhibit detectable activity toward sn-2-arachidonoyl- or linoleoyl-phosphatidylcholine or -phosphatidylethanolamine By similarity.

Catalytic activity

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subcellular location

Secreted. Cytoplasm By similarity.

Sequence similarities

Belongs to the phospholipase A2 family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9EPR2-1)

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.
Isoform 2 (identifier: Q9EPR2-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 192167Group XIIA secretory phospholipase A2
PRO_0000022771

Sites

Active site1131 By similarity
Active site1281 By similarity
Metal binding911Calcium; via carbonyl oxygen By similarity
Metal binding931Calcium; via carbonyl oxygen By similarity
Metal binding951Calcium; via carbonyl oxygen By similarity
Metal binding1141Calcium By similarity

Natural variations

Alternative sequence1 – 7373MVTPR…KCSDG → MKDYHSGPGKYWEPFAFPVG CSGTEEEEGLRIGR in isoform 2.
VSP_004509

Experimental info

Sequence conflict111S → G in AAG23336. Ref.1
Sequence conflict1731P → H in BAB26094. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 16, 2002. Version 2.
Checksum: 670ACE8F6AB6FCA2

FASTA19221,319
        10         20         30         40         50         60 
MVTPRPAPAR SPALLLLLLL ATARGQEQDQ TTDWRATLKT IRNGIHKIDT YLNAALDLLG 

        70         80         90        100        110        120 
GEDGLCQYKC SDGSKPVPRY GYKPSPPNGC GSPLFGVHLN IGIPSLTKCC NQHDRCYETC 

       130        140        150        160        170        180 
GKSKNDCDEE FQYCLSKICR DVQKTLGLSQ NVQACETTVE LLFDSVIHLG CKPYLDSQRA 

       190 
ACWCRYEEKT DL 

« Hide

Isoform 2 [UniParc].

Checksum: C9021DB502233080
Show »

FASTA15317,199

References

« Hide 'large scale' references
[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. 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: 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS17836.1. [Q9EPR2-1]
CCDS17837.1. [Q9EPR2-2]
RefSeqNP_075685.2. NM_023196.4. [Q9EPR2-1]
NP_904359.1. NM_183423.3. [Q9EPR2-2]
UniGeneMm.151951.

3D structure databases

ProteinModelPortalQ9EPR2.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ9EPR2.

Proteomic databases

PaxDbQ9EPR2.
PRIDEQ9EPR2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029629; ENSMUSP00000029629; ENSMUSG00000027999. [Q9EPR2-1]
ENSMUST00000061165; ENSMUSP00000053651; ENSMUSG00000027999. [Q9EPR2-2]
GeneID66350.
KEGGmmu:66350.
UCSCuc008rip.2. mouse. [Q9EPR2-2]
uc012cxt.1. mouse. [Q9EPR2-1]

Organism-specific databases

CTD81579.
MGIMGI:1913600. Pla2g12a.

Phylogenomic databases

eggNOGNOG68062.
GeneTreeENSGT00390000008798.
HOGENOMHOG000247019.
HOVERGENHBG053577.
InParanoidQ9EPR2.
KOK01047.
OMAKICRNVQ.
OrthoDBEOG7J1818.
PhylomeDBQ9EPR2.
TreeFamTF323302.

Gene expression databases

BgeeQ9EPR2.
CleanExMM_PLA2G12A.
GenevestigatorQ9EPR2.

Family and domain databases

Gene3D1.20.90.10. 1 hit.
InterProIPR013090. PLipase_A2_AS.
IPR016090. PLipase_A2_dom.
IPR010711. PLipase_A2_secretory_G12.
[Graphical view]
PANTHERPTHR12824. PTHR12824. 1 hit.
PfamPF06951. PLA2G12. 1 hit.
[Graphical view]
SUPFAMSSF48619. SSF48619. 1 hit.
PROSITEPS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio321399.
PROQ9EPR2.
SOURCESearch...

Entry information

Entry namePG12A_MOUSE
AccessionPrimary (citable) accession number: Q9EPR2
Secondary accession number(s): Q3TQC4 expand/collapse secondary AC list , Q9CQR3, Q9CTL1, Q9D7L3, Q9EPR1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: April 16, 2002
Last modified: July 9, 2014
This is version 111 of the entry and version 2 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