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Protein

Group XV phospholipase A2

Gene

PLA2G15

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has transacylase and calcium-independent phospholipase A2 activity (PubMed:20410020, PubMed:23958596). Catalyzes the formation of 1-O-acyl-N-acetylsphingosine and the concomitant release of a lyso-phospholipid (PubMed:11790796, PubMed:25727495). 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. Required for normal phospholipid degradation in alveolar and peritoneal macrophages and in spleen (By similarity). May have weak lysophospholipase activity (PubMed:10092508).By similarity5 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei46 – 461Substrate; via amide nitrogenCombined sources1 Publication
Active sitei198 – 1981Acyl-ester intermediateSequence analysisCombined sources1 Publication
Binding sitei199 – 1991Substrate; via amide nitrogenCombined sources1 Publication
Active sitei360 – 3601Charge relay system1 Publication
Active sitei392 – 3921Charge relay system1 Publication

GO - Molecular functioni

  • calcium-independent phospholipase A2 activity Source: UniProtKB
  • lysophospholipase activity Source: ProtInc
  • O-acyltransferase activity Source: UniProtKB
  • phospholipid binding Source: ProtInc

GO - Biological processi

  • ceramide metabolic process Source: UniProtKB
  • fatty acid catabolic process Source: ProtInc
  • 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 degradation, Lipid metabolism

Protein family/group databases

ESTHERihuman-PLA2G15. PC-sterol_acyltransferase.

Names & Taxonomyi

Protein namesi
Recommended name:
Group XV phospholipase A2 (EC:2.3.1.-4 Publications)
Alternative name(s):
1-O-acylceramide synthase1 Publication
Short name:
ACS
LCAT-like lysophospholipase1 Publication
Short name:
LLPL1 Publication
Lysophospholipase 3
Lysosomal phospholipase A22 Publications
Short name:
LPLA22 Publications
Gene namesi
Name:PLA2G15
Synonyms:LYPLA3
ORF Names:UNQ341/PRO540
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:17163. PLA2G15.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Lysosome, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi46 – 461D → A: Decreases phospholipase and transacetylase activity. Has no effect on association with membranes. 1 Publication
Mutagenesisi83 – 831L → S: No effect on phospholipase activity. Strongly decreases transacetylase activity and association with membranes. 1 Publication
Mutagenesisi85 – 851V → S: No effect on phospholipase activity. Strongly decreases transacetylase activity and association with membranes. 1 Publication
Mutagenesisi99 – 991N → A: Loss of glycosylation site. Leads to retention in the endoplasmic reticulum and nearly abolishes the production of the mature, active enzyme. 1 Publication
Mutagenesisi198 – 1981S → A: Abolishes phospholipase and transacetylase activity. Abolishes association with membranes. 1 Publication
Mutagenesisi235 – 2351K → A: No effect on phospholipase activity. Abolishes transacetylase activity. Has no effect on association with membranes. 1 Publication
Mutagenesisi273 – 2731N → A: Loss of glycosylation site. Mildly reduces production of the mature, active enzyme. 1 Publication
Mutagenesisi289 – 2891N → A: Loss of glycosylation site. Mildly reduces production of the mature, active enzyme. 1 Publication
Mutagenesisi362 – 3621T → A: No effect on phospholipase activity. Strongly decreases transacetylase activity and abolishes association with membranes. 1 Publication
Mutagenesisi398 – 3981N → A: Loss of glycosylation site. Slightly reduces production of the mature, active enzyme. 1 Publication

Organism-specific databases

PharmGKBiPA164724567.

Chemistry

ChEMBLiCHEMBL4986.

Polymorphism and mutation databases

BioMutaiPLA2G15.
DMDMi44888104.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 33332 PublicationsAdd
BLAST
Chaini34 – 412379Group XV phospholipase A2PRO_0000017808Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi65 ↔ 89Combined sources1 Publication
Glycosylationi99 – 991N-linked (GlcNAc...)Sequence analysisCombined sources1 Publication
Glycosylationi273 – 2731N-linked (GlcNAc...)Sequence analysisCombined sources1 Publication
Glycosylationi289 – 2891N-linked (GlcNAc...)Sequence analysisCombined sources1 Publication
Glycosylationi398 – 3981N-linked (GlcNAc...)Sequence analysisCombined sources1 Publication

Post-translational modificationi

N-glycosylated (PubMed:11790796, PubMed:23958596). N-glycosylation is important for maturation of the enzyme and normal subcellular location (PubMed:23958596).2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ8NCC3.
MaxQBiQ8NCC3.
PaxDbiQ8NCC3.
PeptideAtlasiQ8NCC3.
PRIDEiQ8NCC3.

PTM databases

iPTMnetiQ8NCC3.
PhosphoSiteiQ8NCC3.

Expressioni

Tissue specificityi

Detected in blood plasma (at protein level) (PubMed:10092508, PubMed:20410020). Ubiquitous. Highly expressed in heart, placenta, skeletal muscle, kidney and pancreas. Detected at lower levels in spleen, thymus, prostate, testis, ovary, small intestine, colon and peripheral blood leukocytes (PubMed:10092508).2 Publications

Gene expression databases

BgeeiENSG00000103066.
CleanExiHS_PLA2G15.
ExpressionAtlasiQ8NCC3. baseline and differential.
GenevisibleiQ8NCC3. HS.

Organism-specific databases

HPAiHPA041702.
HPA041727.

Interactioni

Protein-protein interaction databases

BioGridi117181. 2 interactions.
IntActiQ8NCC3. 2 interactions.
MINTiMINT-1403291.
STRINGi9606.ENSP00000219345.

Chemistry

BindingDBiQ8NCC3.

Structurei

Secondary structure

1
412
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi40 – 434Combined sources
Beta strandi51 – 566Combined sources
Beta strandi73 – 775Combined sources
Helixi79 – 824Combined sources
Helixi86 – 949Combined sources
Beta strandi97 – 993Combined sources
Turni100 – 1034Combined sources
Beta strandi104 – 1063Combined sources
Beta strandi111 – 1144Combined sources
Helixi122 – 1254Combined sources
Beta strandi126 – 1283Combined sources
Helixi133 – 1353Combined sources
Beta strandi136 – 1383Combined sources
Helixi139 – 1479Combined sources
Turni153 – 1553Combined sources
Beta strandi156 – 1583Combined sources
Helixi167 – 1693Combined sources
Helixi171 – 18818Combined sources
Beta strandi192 – 1976Combined sources
Helixi200 – 20910Combined sources
Helixi213 – 2197Combined sources
Beta strandi220 – 2278Combined sources
Helixi235 – 2428Combined sources
Helixi253 – 26210Combined sources
Helixi264 – 2685Combined sources
Turni273 – 2753Combined sources
Beta strandi281 – 2844Combined sources
Beta strandi289 – 2913Combined sources
Helixi292 – 2943Combined sources
Helixi295 – 3017Combined sources
Helixi305 – 31410Combined sources
Beta strandi328 – 3369Combined sources
Beta strandi338 – 3436Combined sources
Turni347 – 3493Combined sources
Beta strandi353 – 36412Combined sources
Helixi365 – 3673Combined sources
Helixi368 – 3747Combined sources
Turni375 – 3773Combined sources
Beta strandi382 – 3887Combined sources
Helixi394 – 3974Combined sources
Helixi399 – 41012Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4X90X-ray1.84A/B/C/D34-412[»]
4X91X-ray2.30A/B/C/D34-412[»]
4X92X-ray3.00A34-412[»]
4X93X-ray2.60A/B34-412[»]
4X94X-ray2.70A34-412[»]
4X95X-ray3.08A/B34-412[»]
4X97X-ray2.65A/B/C/D34-412[»]
ProteinModelPortaliQ8NCC3.
SMRiQ8NCC3. Positions 37-412.
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.
InParanoidiQ8NCC3.
KOiK06129.
OMAiEMIEEMH.
OrthoDBiEOG091G07S3.
PhylomeDBiQ8NCC3.
TreeFamiTF313258.

Family and domain databases

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

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. AlignAdd to basket

Isoform 1 (identifier: Q8NCC3-1) [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

        10         20         30         40         50
MGLHLRPYRV GLLPDGLLFL LLLLMLLADP ALPAGRHPPV VLVPGDLGNQ
60 70 80 90 100
LEAKLDKPTV VHYLCSKKTE SYFTIWLNLE LLLPVIIDCW IDNIRLVYNK
110 120 130 140 150
TSRATQFPDG VDVRVPGFGK TFSLEFLDPS KSSVGSYFHT MVESLVGWGY
160 170 180 190 200
TRGEDVRGAP YDWRRAPNEN GPYFLALREM IEEMYQLYGG PVVLVAHSMG
210 220 230 240 250
NMYTLYFLQR QPQAWKDKYI RAFVSLGAPW GGVAKTLRVL ASGDNNRIPV
260 270 280 290 300
IGPLKIREQQ RSAVSTSWLL PYNYTWSPEK VFVQTPTINY TLRDYRKFFQ
310 320 330 340 350
DIGFEDGWLM RQDTEGLVEA TMPPGVQLHC LYGTGVPTPD SFYYESFPDR
360 370 380 390 400
DPKICFGDGD GTVNLKSALQ CQAWQSRQEH QVLLQELPGS EHIEMLANAT
410
TLAYLKRVLL GP
Length:412
Mass (Da):46,658
Last modified:March 1, 2004 - v2
Checksum:i1FEA8A5783AF050A
GO
Isoform 2 (identifier: Q8NCC3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     43-114: VPGDLGNQLE...TQFPDGVDVR → GWFTTKHPGP...EGLPMTGAEP
     115-208: Missing.

Note: No experimental confirmation available.
Show »
Length:318
Mass (Da):35,717
Checksum:i9E52C12B51F5D3C6
GO

Sequence cautioni

The sequence CAB53675 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti94 – 941I → T in BAD96510 (Ref. 4) Curated
Sequence conflicti370 – 3701Q → R in BAC11233 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei43 – 11472VPGDL…GVDVR → GWFTTKHPGPPSFLMVWMYV SLALGRPSHWSSWTPAKAAW VPISTPWWRALWAGATHGVR MSEGLPMTGAEP in isoform 2. 1 PublicationVSP_056689Add
BLAST
Alternative sequencei115 – 20894Missing in isoform 2. 1 PublicationVSP_056690Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017494 mRNA. Translation: BAA76877.1.
AY358425 mRNA. Translation: AAQ88791.1.
AK001705 mRNA. Translation: BAG50965.1.
AK074828 mRNA. Translation: BAC11233.1.
AK300596 mRNA. Translation: BAG62293.1.
AK222790 mRNA. Translation: BAD96510.1.
AL110209 mRNA. Translation: CAB53675.1. Different initiation.
AC020978 Genomic DNA. No translation available.
CH471092 Genomic DNA. Translation: EAW83217.1.
BC011640 mRNA. Translation: AAH11640.2.
BC062605 mRNA. Translation: AAH62605.1.
AL389957 mRNA. Translation: CAB97531.1.
CCDSiCCDS10864.1. [Q8NCC3-1]
PIRiT14755.
RefSeqiNP_036452.1. NM_012320.3. [Q8NCC3-1]
UniGeneiHs.632199.

Genome annotation databases

EnsembliENST00000219345; ENSP00000219345; ENSG00000103066. [Q8NCC3-1]
ENST00000413021; ENSP00000394197; ENSG00000103066. [Q8NCC3-2]
GeneIDi23659.
KEGGihsa:23659.
UCSCiuc002evr.4. human. [Q8NCC3-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017494 mRNA. Translation: BAA76877.1.
AY358425 mRNA. Translation: AAQ88791.1.
AK001705 mRNA. Translation: BAG50965.1.
AK074828 mRNA. Translation: BAC11233.1.
AK300596 mRNA. Translation: BAG62293.1.
AK222790 mRNA. Translation: BAD96510.1.
AL110209 mRNA. Translation: CAB53675.1. Different initiation.
AC020978 Genomic DNA. No translation available.
CH471092 Genomic DNA. Translation: EAW83217.1.
BC011640 mRNA. Translation: AAH11640.2.
BC062605 mRNA. Translation: AAH62605.1.
AL389957 mRNA. Translation: CAB97531.1.
CCDSiCCDS10864.1. [Q8NCC3-1]
PIRiT14755.
RefSeqiNP_036452.1. NM_012320.3. [Q8NCC3-1]
UniGeneiHs.632199.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4X90X-ray1.84A/B/C/D34-412[»]
4X91X-ray2.30A/B/C/D34-412[»]
4X92X-ray3.00A34-412[»]
4X93X-ray2.60A/B34-412[»]
4X94X-ray2.70A34-412[»]
4X95X-ray3.08A/B34-412[»]
4X97X-ray2.65A/B/C/D34-412[»]
ProteinModelPortaliQ8NCC3.
SMRiQ8NCC3. Positions 37-412.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117181. 2 interactions.
IntActiQ8NCC3. 2 interactions.
MINTiMINT-1403291.
STRINGi9606.ENSP00000219345.

Chemistry

BindingDBiQ8NCC3.
ChEMBLiCHEMBL4986.

Protein family/group databases

ESTHERihuman-PLA2G15. PC-sterol_acyltransferase.

PTM databases

iPTMnetiQ8NCC3.
PhosphoSiteiQ8NCC3.

Polymorphism and mutation databases

BioMutaiPLA2G15.
DMDMi44888104.

Proteomic databases

EPDiQ8NCC3.
MaxQBiQ8NCC3.
PaxDbiQ8NCC3.
PeptideAtlasiQ8NCC3.
PRIDEiQ8NCC3.

Protocols and materials databases

DNASUi23659.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000219345; ENSP00000219345; ENSG00000103066. [Q8NCC3-1]
ENST00000413021; ENSP00000394197; ENSG00000103066. [Q8NCC3-2]
GeneIDi23659.
KEGGihsa:23659.
UCSCiuc002evr.4. human. [Q8NCC3-1]

Organism-specific databases

CTDi23659.
GeneCardsiPLA2G15.
HGNCiHGNC:17163. PLA2G15.
HPAiHPA041702.
HPA041727.
MIMi609362. gene.
neXtProtiNX_Q8NCC3.
PharmGKBiPA164724567.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2369. Eukaryota.
ENOG410Y9CF. LUCA.
GeneTreeiENSGT00390000004902.
HOGENOMiHOG000238654.
InParanoidiQ8NCC3.
KOiK06129.
OMAiEMIEEMH.
OrthoDBiEOG091G07S3.
PhylomeDBiQ8NCC3.
TreeFamiTF313258.

Miscellaneous databases

ChiTaRSiPLA2G15. human.
GeneWikiiLYPLA3_(gene).
GenomeRNAii23659.
PROiQ8NCC3.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000103066.
CleanExiHS_PLA2G15.
ExpressionAtlasiQ8NCC3. baseline and differential.
GenevisibleiQ8NCC3. HS.

Family and domain databases

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

Entry informationi

Entry nameiPAG15_HUMAN
AccessioniPrimary (citable) accession number: Q8NCC3
Secondary accession number(s): B3KMF3
, B4DUD1, Q53GZ1, Q9NPQ6, Q9UG04, Q9Y2B3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: March 1, 2004
Last modified: September 7, 2016
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.