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Q8K1N1 (PLPL8_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 84. 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:
Calcium-independent phospholipase A2-gamma

EC=3.1.1.5
Alternative name(s):
Intracellular membrane-associated calcium-independent phospholipase A2 gamma
Short name=iPLA2-gamma
Patatin-like phospholipase domain-containing protein 8
Gene names
Name:Pnpla8
Synonyms:Ipla22, Ipla2g
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length776 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Calcium-independent phospholipase A2, which catalyzes the hydrolysis of the sn-2 position of glycerophospholipids, PtdSer and to a lower extent PtdCho. Cleaves membrane phospholipids By similarity.

Catalytic activity

2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate.

Enzyme regulation

Inhibited by E-6-bromomethylene-3-1-naphthalenyl-2H-tetrahydropyran-2-one (BEL) By similarity.

Subcellular location

Endoplasmic reticulum membrane; Single-pass membrane protein By similarity. Golgi apparatus membrane; Single-pass membrane protein By similarity. Cytoplasmperinuclear region By similarity.

Sequence similarities

Contains 1 patatin domain.

Sequence caution

The sequence AAH19364.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB23417.1 differs from that shown. Reason: Erroneous termination at position 777. Translated as stop.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentCytoplasm
Endoplasmic reticulum
Golgi apparatus
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionHydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processarachidonic acid metabolic process

Inferred from electronic annotation. Source: Ensembl

arachidonic acid secretion

Inferred from electronic annotation. Source: Ensembl

cell death

Inferred from electronic annotation. Source: Ensembl

fatty acid metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

linoleic acid metabolic process

Inferred from electronic annotation. Source: Ensembl

phosphatidylcholine catabolic process

Inferred from electronic annotation. Source: Ensembl

phosphatidylethanolamine catabolic process

Inferred from electronic annotation. Source: Ensembl

prostaglandin biosynthetic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

peroxisomal membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functioncalcium-independent phospholipase A2 activity

Inferred from sequence or structural similarity. Source: UniProtKB

lysophospholipase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 776776Calcium-independent phospholipase A2-gamma
PRO_0000303215

Regions

Transmembrane469 – 48921Helical; Potential
Domain439 – 634196Patatin
Motif475 – 4795GXSXG By similarity

Amino acid modifications

Modified residue7301N6-succinyllysine Ref.4
Glycosylation41N-linked (GlcNAc...) Potential
Glycosylation1571N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict438 – 4414ILTI → DAWV in AAH19364. Ref.3
Sequence conflict7291M → I in BAE40365. Ref.2
Sequence conflict7491E → Q in BAE40365. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8K1N1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 1140CC8358B1E119

FASTA77687,381
        10         20         30         40         50         60 
MSINLTLDIY IYFLNNARSL CGKQRSKQLH FVCSKQYWRM NHVNVHREFH TSKKSCKWNR 

        70         80         90        100        110        120 
SEAHCSKHWH SPSNHGLHFG IVRLSTSAPK GLTKVSIHMS RIKSTLNSVS KAIFGSQNEM 

       130        140        150        160        170        180 
VTRLAQFKPS SRILRKVSDK GWLKQKNVKQ AVESLKNYSD KSAGKNSLAE QKSYFADKEE 

       190        200        210        220        230        240 
DSGKHSLFHY TYGITTRFGE SFSVLANHIN SYFKSKGKMS QTKEDKQLQD KPDLEERKSS 

       250        260        270        280        290        300 
SPGPDTVADR PDSESPLEVK DKLSSPTQMP EAHPVSAKQS IANFLSRPTE GVQALVGGYI 

       310        320        330        340        350        360 
GGLVPKLKSD PKSPPEEQEV SAKTEQAVNK DKKAEEKKRV LLQQEKIIAR VSIDNRTRAL 

       370        380        390        400        410        420 
VQALRRTADP KLCITRVEEL TFHLLEFPEG KGVAIKEKII PYLLRLRQVK DETLQAAVRE 

       430        440        450        460        470        480 
ILALIGYVDP VKGRGIRILT IDGGGTRGVV ALQTLRKLVE LTQKPIHQLF DYICGVSTGA 

       490        500        510        520        530        540 
ILAFMLGLFH MPLDECEELY RKLGSDVFTQ NVIVGTVKMS WSHAFYDSNT WEKILKDRIG 

       550        560        570        580        590        600 
SALMIETARN PACPKVAAIS TIVNRGQTPK AFVFRNYGHF PGTNSHYLGG CQYKMWQAIR 

       610        620        630        640        650        660 
ASSAAPGYFA EYALGSDLHQ DGGLLLNNPS ALALHECKCI WPDTPLECIV SLGTGRYESD 

       670        680        690        700        710        720 
VRNTSTYTSL KTKLSNVISS ATDTEEVHIM LDGLLPSDTY FRFNPVICEN IPLDESRDEK 

       730        740        750        760        770 
LDQLQLEGMK YIERNDQKMK KVAKILSQEK TTLQKINDWI KLKSDMYEGL PFFSKL 

« Hide

References

« Hide 'large scale' references
[1]"A novel intracellular membrane-bound calcium-independent phospholipase A(2)."
Tanaka H., Takeya R., Sumimoto H.
Biochem. Biophys. Res. Commun. 272:320-326(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: Egg, Kidney and Lung.
[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].
Strain: Czech II.
Tissue: Mammary tumor.
[4]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-730, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB044139 mRNA. Translation: BAB97200.1.
AK004621 mRNA. Translation: BAB23417.1. Sequence problems.
AK145776 mRNA. Translation: BAE26645.1.
AK163211 mRNA. Translation: BAE37236.1.
AK168475 mRNA. Translation: BAE40365.1.
BC019364 mRNA. Translation: AAH19364.1. Different initiation.
BC127056 mRNA. Translation: AAI27057.1.
CCDSCCDS36436.1.
RefSeqNP_080440.2. NM_026164.2.
UniGeneMm.54126.

3D structure databases

ProteinModelPortalQ8K1N1.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ8K1N1.

Proteomic databases

MaxQBQ8K1N1.
PaxDbQ8K1N1.
PRIDEQ8K1N1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000043082; ENSMUSP00000043286; ENSMUSG00000036257.
GeneID67452.
KEGGmmu:67452.
UCSCuc007nlp.1. mouse.

Organism-specific databases

CTD50640.
MGIMGI:1914702. Pnpla8.

Phylogenomic databases

eggNOGCOG3621.
GeneTreeENSGT00530000063645.
HOGENOMHOG000115579.
HOVERGENHBG102100.
InParanoidQ8K1N1.
KOK16815.
OMAKYDSKSQ.
PhylomeDBQ8K1N1.
TreeFamTF319230.

Gene expression databases

ArrayExpressQ8K1N1.
BgeeQ8K1N1.
CleanExMM_PNPLA8.
GenevestigatorQ8K1N1.

Family and domain databases

InterProIPR016035. Acyl_Trfase/lysoPLipase.
IPR002641. Patatin/PLipase_A2-rel.
[Graphical view]
PfamPF01734. Patatin. 1 hit.
[Graphical view]
SUPFAMSSF52151. SSF52151. 1 hit.
ProtoNetSearch...

Other

NextBio324606.
PROQ8K1N1.
SOURCESearch...

Entry information

Entry namePLPL8_MOUSE
AccessionPrimary (citable) accession number: Q8K1N1
Secondary accession number(s): Q3TH33, Q8VEC0, Q9DC20
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: October 1, 2002
Last modified: July 9, 2014
This is version 84 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