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Protein

Group XV phospholipase A2

Gene

Pla2g15

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

Functioni

Has transacylase and calcium-independent phospholipase A2 activity. Catalyzes the formation of 1-O-acyl-N-acetylsphingosine and the concomitant release of a lyso-phospholipid (PubMed:11790796, PubMed:16106046, PubMed:16880524, PubMed:19017977, PubMed:20410020). Has high activity with 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) and 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC), catalyzing the transfer of oleic acid to N-acetyl-sphingosine (PubMed:16880524). Required for normal phospholipid degradation in alveolar and peritoneal macrophages and in spleen (PubMed:16880524, PubMed:19017977).5 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei46 – 461Substrate; via amide nitrogenBy similarity
Active sitei198 – 1981Acyl-ester intermediateSequence analysis2 Publications
Binding sitei199 – 1991Substrate; via amide nitrogenBy similarity
Active sitei360 – 3601Charge relay systemBy similarity1 Publication
Active sitei392 – 3921Charge relay systemBy similarity1 Publication

GO - Molecular functioni

  • calcium-independent phospholipase A2 activity Source: MGI
  • O-acyltransferase activity Source: UniProtKB

GO - Biological processi

  • ceramide metabolic process Source: UniProtKB
  • fatty acid metabolic process Source: UniProtKB-KW
  • glycerophospholipid metabolic process Source: UniProtKB
  • phosphatidylcholine catabolic process Source: UniProtKB
  • phosphatidylethanolamine catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Hydrolase, Transferase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Protein family/group databases

ESTHERimouse-C87498. PC-sterol_acyltransferase.

Chemistry

SwissLipidsiSLP:000000352.

Names & Taxonomyi

Protein namesi
Recommended name:
Group XV phospholipase A2 (EC:2.3.1.-5 Publications)
Alternative name(s):
1-O-acylceramide synthase1 Publication
Short name:
ACS
LCAT-like lysophospholipase
Short name:
LLPL
Lysophospholipase 3
Lysosomal phospholipase A22 Publications
Short name:
LPLA21 Publication
Gene namesi
Name:Pla2g15
Synonyms:Lypla3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:2178076. Pla2g15.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • extracellular space Source: UniProtKB
  • lysosome Source: UniProtKB
  • membrane Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Membrane, Secreted

Pathology & Biotechi

Disruption phenotypei

Mice are born at the expected Mendelian rate, are viable and fertile. They display strongly reduced transacylase activity in lung alveolar macrophages and in peritoneal macrophages, leading to the accumulation of phospholipids with phosphatidylethanolamine and phosphatidylcholine headgroups. Mice display higher numers of alveolar macrophages in the lung, together with a mononuclear cell infiltrate in airways and blood vessels. Alveolar nmacrophages are larger than normal and present lamellar inclusion bodies, indicative of cellular phospholipidosis. Besides, mutant mice display splenomegaly.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi65 – 651C → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi89 – 891C → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi198 – 1981S → A: Abolishes enzyme activity. 2 Publications
Mutagenesisi360 – 3601D → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi392 – 3921H → A: Abolishes enzyme activity. 1 Publication

Chemistry

ChEMBLiCHEMBL3259497.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3333By similarityAdd
BLAST
Chaini34 – 412379Group XV phospholipase A2PRO_0000017809Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi65 ↔ 89By similarity1 Publication
Glycosylationi99 – 991N-linked (GlcNAc...)Sequence analysis
Glycosylationi273 – 2731N-linked (GlcNAc...)Sequence analysis
Glycosylationi289 – 2891N-linked (GlcNAc...)Sequence analysis
Glycosylationi398 – 3981N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

N-glycosylated (PubMed:11790796). N-glycosylation is important for maturation of the enzyme and normal subcellular location (By similarity).By similarity1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ8VEB4.
MaxQBiQ8VEB4.
PaxDbiQ8VEB4.
PRIDEiQ8VEB4.

PTM databases

PhosphoSiteiQ8VEB4.

Expressioni

Tissue specificityi

Detected in blood plasma (PubMed:20410020). Detected in alveolar macrophages (at protein level) (PubMed:16106046, PubMed:16880524, PubMed:19017977). Detected in heart, liver, spleen, kidney, thymus, brain and lung (PubMed:16880524).4 Publications

Gene expression databases

BgeeiQ8VEB4.
GenevisibleiQ8VEB4. MM.

Interactioni

Protein-protein interaction databases

IntActiQ8VEB4. 1 interaction.
MINTiMINT-4100834.
STRINGi10090.ENSMUSP00000034377.

Structurei

3D structure databases

ProteinModelPortaliQ8VEB4.
SMRiQ8VEB4. Positions 36-412.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2369. Eukaryota.
ENOG410Y9CF. LUCA.
GeneTreeiENSGT00390000004902.
HOGENOMiHOG000238654.
InParanoidiQ8VEB4.
KOiK06129.
OMAiEMIEEMH.
OrthoDBiEOG73BVD0.
PhylomeDBiQ8VEB4.
TreeFamiTF313258.

Family and domain databases

Gene3Di3.40.50.1820. 3 hits.
InterProiIPR029058. AB_hydrolase.
IPR003386. LACT/PDAT_acylTrfase.
[Graphical view]
PfamiPF02450. LCAT. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 2 hits.

Sequencei

Sequence statusi: Complete.

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

Q8VEB4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDRHLCTCRE TQLRSGLLLP LFLLMMLADL TLPAQRHPPV VLVPGDLGNQ
60 70 80 90 100
LEAKLDKPKV VHYLCSKKTD SYFTLWLNLE LLLPVIIDCW IDNIRLVYNR
110 120 130 140 150
TSRATQFPDG VDVRVPGFGE TFSMEFLDPS KRNVGSYFYT MVESLVGWGY
160 170 180 190 200
TRGEDVRGAP YDWRRAPNEN GPYFLALREM IEEMYQMYGG PVVLVAHSMG
210 220 230 240 250
NVYMLYFLQR QPQVWKDKYI HAFVSLGAPW GGVAKTLRVL ASGDNNRIPV
260 270 280 290 300
IGPLKIREQQ RSAVSTSWLL PYNHTWSHEK VFVYTPTTNY TLRDYHRFFR
310 320 330 340 350
DIGFEDGWFM RQDTEGLVEA MTPPGVELHC LYGTGVPTPN SFYYESFPDR
360 370 380 390 400
DPKICFGDGD GTVNLESVLQ CQAWQSRQEH RVSLQELPGS EHIEMLANAT
410
TLAYLKRVLL EP
Length:412
Mass (Da):47,307
Last modified:March 1, 2002 - v1
Checksum:i6544369410C46C9A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti342 – 3421F → S in BAE32987 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF468958 mRNA. Translation: AAL78651.1.
AY179884 Genomic DNA. Translation: AAO49009.1.
AK085194 mRNA. Translation: BAC39387.1.
AK155004 mRNA. Translation: BAE32987.1.
AK163111 mRNA. Translation: BAE37197.1.
AK170814 mRNA. Translation: BAE42046.1.
BC019373 mRNA. Translation: AAH19373.1.
CCDSiCCDS22630.1.
RefSeqiNP_598553.1. NM_133792.2.
UniGeneiMm.284770.

Genome annotation databases

EnsembliENSMUST00000034377; ENSMUSP00000034377; ENSMUSG00000031903.
GeneIDi192654.
KEGGimmu:192654.
UCSCiuc009nfj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF468958 mRNA. Translation: AAL78651.1.
AY179884 Genomic DNA. Translation: AAO49009.1.
AK085194 mRNA. Translation: BAC39387.1.
AK155004 mRNA. Translation: BAE32987.1.
AK163111 mRNA. Translation: BAE37197.1.
AK170814 mRNA. Translation: BAE42046.1.
BC019373 mRNA. Translation: AAH19373.1.
CCDSiCCDS22630.1.
RefSeqiNP_598553.1. NM_133792.2.
UniGeneiMm.284770.

3D structure databases

ProteinModelPortaliQ8VEB4.
SMRiQ8VEB4. Positions 36-412.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8VEB4. 1 interaction.
MINTiMINT-4100834.
STRINGi10090.ENSMUSP00000034377.

Chemistry

ChEMBLiCHEMBL3259497.
SwissLipidsiSLP:000000352.

Protein family/group databases

ESTHERimouse-C87498. PC-sterol_acyltransferase.

PTM databases

PhosphoSiteiQ8VEB4.

Proteomic databases

EPDiQ8VEB4.
MaxQBiQ8VEB4.
PaxDbiQ8VEB4.
PRIDEiQ8VEB4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034377; ENSMUSP00000034377; ENSMUSG00000031903.
GeneIDi192654.
KEGGimmu:192654.
UCSCiuc009nfj.1. mouse.

Organism-specific databases

CTDi23659.
MGIiMGI:2178076. Pla2g15.

Phylogenomic databases

eggNOGiKOG2369. Eukaryota.
ENOG410Y9CF. LUCA.
GeneTreeiENSGT00390000004902.
HOGENOMiHOG000238654.
InParanoidiQ8VEB4.
KOiK06129.
OMAiEMIEEMH.
OrthoDBiEOG73BVD0.
PhylomeDBiQ8VEB4.
TreeFamiTF313258.

Miscellaneous databases

ChiTaRSiPla2g15. mouse.
PROiQ8VEB4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VEB4.
GenevisibleiQ8VEB4. MM.

Family and domain databases

Gene3Di3.40.50.1820. 3 hits.
InterProiIPR029058. AB_hydrolase.
IPR003386. LACT/PDAT_acylTrfase.
[Graphical view]
PfamiPF02450. LCAT. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of a lysosomal phospholipase A2, 1-O-acylceramide synthase."
    Hiraoka M., Abe A., Shayman J.A.
    J. Biol. Chem. 277:10090-10099(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF SER-198, GLYCOSYLATION.
    Strain: 129/Sv and C57BL/6.
    Tissue: Kidney.
  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 and NOD.
    Tissue: Dendritic cell and Embryonic stomach.
  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: FVB/N.
    Tissue: Mammary tumor.
  4. "Structure and function of lysosomal phospholipase A2: identification of the catalytic triad and the role of cysteine residues."
    Hiraoka M., Abe A., Shayman J.A.
    J. Lipid Res. 46:2441-2447(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, DISULFIDE BOND, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-65; CYS-89; SER-198; ASP-360 AND HIS-392.
  5. Cited for: DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
  6. "The secretion and uptake of lysosomal phospholipase A2 by alveolar macrophages."
    Abe A., Kelly R., Kollmeyer J., Hiraoka M., Lu Y., Shayman J.A.
    J. Immunol. 181:7873-7881(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Liver, Lung and Spleen.
  8. "The measurement of lysosomal phospholipase A2 activity in plasma."
    Abe A., Kelly R., Shayman J.A.
    J. Lipid Res. 51:2464-2470(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION, CATALYTIC ACTIVITY.

Entry informationi

Entry nameiPAG15_MOUSE
AccessioniPrimary (citable) accession number: Q8VEB4
Secondary accession number(s): Q3TCB1, Q3U303
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: March 1, 2002
Last modified: June 8, 2016
This is version 116 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.