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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)DescriptionActionsGraphical viewLength
Binding sitei46Substrate; via amide nitrogenCombined sources1 Publication1
Active sitei198Acyl-ester intermediateSequence analysisCombined sources1 Publication1
Binding sitei199Substrate; via amide nitrogenCombined sources1 Publication1
Active sitei360Charge relay system1 Publication1
Active sitei392Charge relay system1 Publication1

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

Enzyme and pathway databases

BioCyciZFISH:HS02451-MONOMER.

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)DescriptionActionsGraphical viewLength
Mutagenesisi46D → A: Decreases phospholipase and transacetylase activity. Has no effect on association with membranes. 1 Publication1
Mutagenesisi83L → S: No effect on phospholipase activity. Strongly decreases transacetylase activity and association with membranes. 1 Publication1
Mutagenesisi85V → S: No effect on phospholipase activity. Strongly decreases transacetylase activity and association with membranes. 1 Publication1
Mutagenesisi99N → A: Loss of glycosylation site. Leads to retention in the endoplasmic reticulum and nearly abolishes the production of the mature, active enzyme. 1 Publication1
Mutagenesisi198S → A: Abolishes phospholipase and transacetylase activity. Abolishes association with membranes. 1 Publication1
Mutagenesisi235K → A: No effect on phospholipase activity. Abolishes transacetylase activity. Has no effect on association with membranes. 1 Publication1
Mutagenesisi273N → A: Loss of glycosylation site. Mildly reduces production of the mature, active enzyme. 1 Publication1
Mutagenesisi289N → A: Loss of glycosylation site. Mildly reduces production of the mature, active enzyme. 1 Publication1
Mutagenesisi362T → A: No effect on phospholipase activity. Strongly decreases transacetylase activity and abolishes association with membranes. 1 Publication1
Mutagenesisi398N → A: Loss of glycosylation site. Slightly reduces production of the mature, active enzyme. 1 Publication1

Organism-specific databases

DisGeNETi23659.
OpenTargetsiENSG00000103066.
PharmGKBiPA164724567.

Chemistry databases

ChEMBLiCHEMBL4986.

Polymorphism and mutation databases

BioMutaiPLA2G15.
DMDMi44888104.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 332 PublicationsAdd BLAST33
ChainiPRO_000001780834 – 412Group XV phospholipase A2Add BLAST379

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi65 ↔ 89Combined sources1 Publication
Glycosylationi99N-linked (GlcNAc...)Sequence analysisCombined sources1 Publication1
Glycosylationi273N-linked (GlcNAc...)Sequence analysisCombined sources1 Publication1
Glycosylationi289N-linked (GlcNAc...)Sequence analysisCombined sources1 Publication1
Glycosylationi398N-linked (GlcNAc...)Sequence analysisCombined sources1 Publication1

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.
PhosphoSitePlusiQ8NCC3.

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 interactors.
IntActiQ8NCC3. 2 interactors.
MINTiMINT-1403291.
STRINGi9606.ENSP00000219345.

Chemistry databases

BindingDBiQ8NCC3.

Structurei

Secondary structure

1412
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi40 – 43Combined sources4
Beta strandi51 – 56Combined sources6
Beta strandi73 – 77Combined sources5
Helixi79 – 82Combined sources4
Helixi86 – 94Combined sources9
Beta strandi97 – 99Combined sources3
Turni100 – 103Combined sources4
Beta strandi104 – 106Combined sources3
Beta strandi111 – 114Combined sources4
Helixi122 – 125Combined sources4
Beta strandi126 – 128Combined sources3
Helixi133 – 135Combined sources3
Beta strandi136 – 138Combined sources3
Helixi139 – 147Combined sources9
Turni153 – 155Combined sources3
Beta strandi156 – 158Combined sources3
Helixi167 – 169Combined sources3
Helixi171 – 188Combined sources18
Beta strandi192 – 197Combined sources6
Helixi200 – 209Combined sources10
Helixi213 – 219Combined sources7
Beta strandi220 – 227Combined sources8
Helixi235 – 242Combined sources8
Helixi253 – 262Combined sources10
Helixi264 – 268Combined sources5
Turni273 – 275Combined sources3
Beta strandi281 – 284Combined sources4
Beta strandi289 – 291Combined sources3
Helixi292 – 294Combined sources3
Helixi295 – 301Combined sources7
Helixi305 – 314Combined sources10
Beta strandi328 – 336Combined sources9
Beta strandi338 – 343Combined sources6
Turni347 – 349Combined sources3
Beta strandi353 – 364Combined sources12
Helixi365 – 367Combined sources3
Helixi368 – 374Combined sources7
Turni375 – 377Combined sources3
Beta strandi382 – 388Combined sources7
Helixi394 – 397Combined sources4
Helixi399 – 410Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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)DescriptionActionsGraphical viewLength
Sequence conflicti94I → T in BAD96510 (Ref. 4) Curated1
Sequence conflicti370Q → R in BAC11233 (PubMed:14702039).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_05668943 – 114VPGDL…GVDVR → GWFTTKHPGPPSFLMVWMYV SLALGRPSHWSSWTPAKAAW VPISTPWWRALWAGATHGVR MSEGLPMTGAEP in isoform 2. 1 PublicationAdd BLAST72
Alternative sequenceiVSP_056690115 – 208Missing in isoform 2. 1 PublicationAdd BLAST94

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry databases

BindingDBiQ8NCC3.
ChEMBLiCHEMBL4986.

Protein family/group databases

ESTHERihuman-PLA2G15. PC-sterol_acyltransferase.

PTM databases

iPTMnetiQ8NCC3.
PhosphoSitePlusiQ8NCC3.

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.
DisGeNETi23659.
GeneCardsiPLA2G15.
HGNCiHGNC:17163. PLA2G15.
HPAiHPA041702.
HPA041727.
MIMi609362. gene.
neXtProtiNX_Q8NCC3.
OpenTargetsiENSG00000103066.
PharmGKBiPA164724567.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciZFISH:HS02451-MONOMER.

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: November 2, 2016
This is version 131 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.