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Protein

Cytosolic phospholipase A2 delta

Gene

PLA2G4D

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

Functioni

Calcium-dependent phospholipase A2 that selectively hydrolyzes glycerophospholipids in the sn-2 position. Not arachidonic acid-specific but has linoleic acid-specific activity. May play a role in inflammation in psoriatic lesions.1 Publication

Catalytic activityi

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Enzyme regulationi

Stimulated by cytosolic Ca2+.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei361NucleophileBy similarity1
Active sitei647Proton acceptorBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:HS14755-MONOMER.
ReactomeiR-HSA-1482788. Acyl chain remodelling of PC.
R-HSA-1482801. Acyl chain remodelling of PS.
R-HSA-1482839. Acyl chain remodelling of PE.
R-HSA-1482922. Acyl chain remodelling of PI.
R-HSA-1482925. Acyl chain remodelling of PG.
R-HSA-1483115. Hydrolysis of LPC.
R-HSA-1483166. Synthesis of PA.

Chemistry databases

SwissLipidsiSLP:000001080.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytosolic phospholipase A2 delta (EC:3.1.1.4)
Short name:
cPLA2-delta
Alternative name(s):
Phospholipase A2 group IVD
Gene namesi
Name:PLA2G4D
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:30038. PLA2G4D.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi283748.
OpenTargetsiENSG00000159337.
PharmGKBiPA134974074.

Polymorphism and mutation databases

BioMutaiPLA2G4D.
DMDMi269849641.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002470231 – 818Cytosolic phospholipase A2 deltaAdd BLAST818

Proteomic databases

MaxQBiQ86XP0.
PaxDbiQ86XP0.
PeptideAtlasiQ86XP0.
PRIDEiQ86XP0.

PTM databases

iPTMnetiQ86XP0.
PhosphoSitePlusiQ86XP0.

Expressioni

Tissue specificityi

Expressed in stratified squamous epithelia, such as those in skin and cervix, but not in other tissues. Strongly expressed in the upper spinous layer of the psoriatic epidermis, expressed weakly and discontinuously in atopic dermatitis and mycosis fungoides, and not detected in the epidermis of normal skin.1 Publication

Gene expression databases

BgeeiENSG00000159337.
CleanExiHS_PLA2G4D.

Interactioni

Protein-protein interaction databases

BioGridi129664. 1 interactor.
STRINGi9606.ENSP00000290472.

Structurei

Secondary structure

1818
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi17 – 19Combined sources3
Beta strandi21 – 33Combined sources13
Turni38 – 40Combined sources3
Beta strandi45 – 51Combined sources7
Beta strandi71 – 81Combined sources11
Beta strandi87 – 94Combined sources8
Beta strandi97 – 99Combined sources3
Beta strandi102 – 110Combined sources9
Helixi111 – 113Combined sources3
Beta strandi120 – 124Combined sources5
Beta strandi133 – 142Combined sources10
Beta strandi148 – 152Combined sources5
Beta strandi154 – 158Combined sources5
Beta strandi161 – 167Combined sources7
Beta strandi183 – 189Combined sources7
Beta strandi192 – 194Combined sources3
Beta strandi196 – 200Combined sources5
Turni201 – 203Combined sources3
Beta strandi206 – 212Combined sources7
Beta strandi217 – 225Combined sources9
Beta strandi230 – 232Combined sources3
Beta strandi240 – 244Combined sources5
Beta strandi251 – 257Combined sources7
Beta strandi260 – 262Combined sources3
Beta strandi265 – 273Combined sources9
Beta strandi279 – 282Combined sources4
Helixi288 – 309Combined sources22
Helixi317 – 319Combined sources3
Beta strandi323 – 327Combined sources5
Helixi331 – 347Combined sources17
Helixi351 – 353Combined sources3
Beta strandi356 – 359Combined sources4
Helixi363 – 371Combined sources9
Helixi376 – 378Combined sources3
Helixi382 – 393Combined sources12
Helixi396 – 398Combined sources3
Helixi402 – 418Combined sources17
Helixi424 – 436Combined sources13
Beta strandi437 – 439Combined sources3
Helixi445 – 452Combined sources8
Beta strandi459 – 466Combined sources8
Turni469 – 473Combined sources5
Beta strandi474 – 476Combined sources3
Beta strandi479 – 483Combined sources5
Beta strandi488 – 490Combined sources3
Turni491 – 494Combined sources4
Beta strandi495 – 497Combined sources3
Helixi499 – 501Combined sources3
Beta strandi504 – 507Combined sources4
Beta strandi510 – 513Combined sources4
Helixi520 – 527Combined sources8
Turni530 – 533Combined sources4
Helixi537 – 539Combined sources3
Helixi577 – 579Combined sources3
Beta strandi581 – 583Combined sources3
Helixi584 – 590Combined sources7
Turni605 – 608Combined sources4
Beta strandi610 – 612Combined sources3
Helixi613 – 615Combined sources3
Helixi618 – 621Combined sources4
Beta strandi623 – 625Combined sources3
Beta strandi628 – 631Combined sources4
Turni634 – 636Combined sources3
Helixi648 – 650Combined sources3
Helixi656 – 660Combined sources5
Beta strandi667 – 672Combined sources6
Helixi681 – 692Combined sources12
Helixi704 – 708Combined sources5
Beta strandi714 – 716Combined sources3
Beta strandi719 – 723Combined sources5
Beta strandi726 – 730Combined sources5
Turni736 – 739Combined sources4
Beta strandi740 – 742Combined sources3
Turni749 – 751Combined sources3
Helixi753 – 755Combined sources3
Beta strandi760 – 763Combined sources4
Helixi775 – 790Combined sources16
Helixi793 – 806Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5IXCX-ray2.65A/B2-810[»]
5IZ5X-ray2.20A/B2-810[»]
5IZRX-ray3.25A/B/C/D2-810[»]
ProteinModelPortaliQ86XP0.
SMRiQ86XP0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini9 – 120C2PROSITE-ProRule annotationAdd BLAST112
Domaini273 – 818PLA2cPROSITE-ProRule annotationAdd BLAST546

Domaini

The N-terminal C2 domain associates with lipid membranes upon calcium binding. It modulates enzyme activity by presenting the active site to its substrate in response to elevations of cytosolic Ca2+ (By similarity).By similarity

Sequence similaritiesi

Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 1 PLA2c domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1028. Eukaryota.
KOG1325. Eukaryota.
ENOG410XR72. LUCA.
GeneTreeiENSGT00550000074489.
HOGENOMiHOG000231788.
HOVERGENiHBG080412.
InParanoidiQ86XP0.
KOiK16342.
OMAiKDHSAPG.
OrthoDBiEOG091G011T.
PhylomeDBiQ86XP0.
TreeFamiTF325228.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR016035. Acyl_Trfase/lysoPLipase.
IPR000008. C2_dom.
IPR002642. LysoPLipase_cat_dom.
[Graphical view]
PfamiPF00168. C2. 1 hit.
PF01735. PLA2_B. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 1 hit.
SM00022. PLAc. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF52151. SSF52151. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS51210. PLA2C. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q86XP0-1) [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
MESLSPGGPP GHPYQGEAST CWQLTVRVLE ARNLRWADLL SEADPYVILQ
60 70 80 90 100
LSTAPGMKFK TKTLTDTSHP VWNEAFRFLI QSQVKNVLEL SIYDEDSVTE
110 120 130 140 150
DDICFKVLYD ISEVLPGKLL RKTFSQSPQG EEELDVEFLM EETSDRPENL
160 170 180 190 200
ITNKVIVARE LSCLDVHLDS TGSTAVVADQ DKLELELVLK GSYEDTQTSF
210 220 230 240 250
LGTASAFRFH YMAALETELS GRLRSSRSNG WNGDNSAGYL TVPLRPLTIG
260 270 280 290 300
KEVTMDVPAP NAPGVRLQLK AEGCPEELAV HLGFNLCAEE QAFLSRRKQV
310 320 330 340 350
VAKALKQALQ LDRDLQEDEV PVVGIMATGG GARAMTSLYG HLLALQKLGL
360 370 380 390 400
LDCVTYFSGI SGSTWTMAHL YGDPEWSQRD LEGPIRYARE HLAKSKLEVF
410 420 430 440 450
SPERLASYRR ELELRAEQGH PTTFVDLWAL VLESMLHGQV MDQKLSGQRA
460 470 480 490 500
ALERGQNPLP LYLSLNVKEN NLETLDFKEW VEFSPYEVGF LKYGAFVPPE
510 520 530 540 550
LFGSEFFMGR LMRRIPEPRI CFLEAIWSNI FSLNLLDAWY DLTSSGESWK
560 570 580 590 600
QHIKDKTRSL EKEPLTTSGT SSRLEASWLQ PGTALAQAFK GFLTGRPLHQ
610 620 630 640 650
RSPNFLQGLQ LHQDYCSHKD FSTWADYQLD SMPSQLTPKE PRLCLVDAAY
660 670 680 690 700
FINTSSPSMF RPGRRLDLIL SFDYSLSAPF EALQQTELYC RARGLPFPRV
710 720 730 740 750
EPSPQDQHQP RECHLFSDPA CPEAPILLHF PLVNASFKDH SAPGVQRSPA
760 770 780 790 800
ELQGGQVDLT GATCPYTLSN MTYKEEDFER LLRLSDYNVQ TSQGAILQAL
810
RTALKHRTLE ARPPRAQT
Length:818
Mass (Da):91,952
Last modified:November 24, 2009 - v2
Checksum:i06187324748A4C21
GO
Isoform 2 (identifier: Q86XP0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     682-723: ALQQTELYCR...HLFSDPACPE → VPWSPQGNPS...VPKGRRGVRP
     724-818: Missing.

Note: May be due to an intron retention.Curated
Show »
Length:723
Mass (Da):80,930
Checksum:i0C385309D4BAB085
GO

Sequence cautioni

The sequence AAH34571 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti10P → T in BAC67158 (PubMed:14709560).Curated1
Isoform 2 (identifier: Q86XP0-2)
Sequence conflicti713G → R in AAH34571 (PubMed:16572171).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_057676275P → R.Corresponds to variant rs11635685dbSNPEnsembl.1
Natural variantiVAR_057677434S → T.Corresponds to variant rs4924618dbSNPEnsembl.1
Natural variantiVAR_027049573R → W.Corresponds to variant rs17747505dbSNPEnsembl.1
Natural variantiVAR_027050649A → G.Corresponds to variant rs17690899dbSNPEnsembl.1
Natural variantiVAR_027051747R → G.1 PublicationCorresponds to variant rs2459692dbSNPEnsembl.1
Natural variantiVAR_057678783R → Q.Corresponds to variant rs750052dbSNPEnsembl.1
Natural variantiVAR_057679807R → Q.Corresponds to variant rs750051dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_019881682 – 723ALQQT…PACPE → VPWSPQGNPSAQPGQAPEAS SRATEPLPHTAGVPKGRRGV RP in isoform 2. 1 PublicationAdd BLAST42
Alternative sequenceiVSP_019882724 – 818Missing in isoform 2. 1 PublicationAdd BLAST95

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB090876 mRNA. Translation: BAC67158.1.
AC084693 Genomic DNA. No translation available.
BC034571 mRNA. Translation: AAH34571.1. Different initiation.
CCDSiCCDS32203.1. [Q86XP0-1]
RefSeqiNP_828848.3. NM_178034.3. [Q86XP0-1]
UniGeneiHs.380225.

Genome annotation databases

EnsembliENST00000290472; ENSP00000290472; ENSG00000159337. [Q86XP0-1]
GeneIDi283748.
KEGGihsa:283748.
UCSCiuc001zox.3. human. [Q86XP0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB090876 mRNA. Translation: BAC67158.1.
AC084693 Genomic DNA. No translation available.
BC034571 mRNA. Translation: AAH34571.1. Different initiation.
CCDSiCCDS32203.1. [Q86XP0-1]
RefSeqiNP_828848.3. NM_178034.3. [Q86XP0-1]
UniGeneiHs.380225.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5IXCX-ray2.65A/B2-810[»]
5IZ5X-ray2.20A/B2-810[»]
5IZRX-ray3.25A/B/C/D2-810[»]
ProteinModelPortaliQ86XP0.
SMRiQ86XP0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi129664. 1 interactor.
STRINGi9606.ENSP00000290472.

Chemistry databases

SwissLipidsiSLP:000001080.

PTM databases

iPTMnetiQ86XP0.
PhosphoSitePlusiQ86XP0.

Polymorphism and mutation databases

BioMutaiPLA2G4D.
DMDMi269849641.

Proteomic databases

MaxQBiQ86XP0.
PaxDbiQ86XP0.
PeptideAtlasiQ86XP0.
PRIDEiQ86XP0.

Protocols and materials databases

DNASUi283748.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000290472; ENSP00000290472; ENSG00000159337. [Q86XP0-1]
GeneIDi283748.
KEGGihsa:283748.
UCSCiuc001zox.3. human. [Q86XP0-1]

Organism-specific databases

CTDi283748.
DisGeNETi283748.
GeneCardsiPLA2G4D.
H-InvDBHIX0026772.
HGNCiHGNC:30038. PLA2G4D.
MIMi612864. gene.
neXtProtiNX_Q86XP0.
OpenTargetsiENSG00000159337.
PharmGKBiPA134974074.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1028. Eukaryota.
KOG1325. Eukaryota.
ENOG410XR72. LUCA.
GeneTreeiENSGT00550000074489.
HOGENOMiHOG000231788.
HOVERGENiHBG080412.
InParanoidiQ86XP0.
KOiK16342.
OMAiKDHSAPG.
OrthoDBiEOG091G011T.
PhylomeDBiQ86XP0.
TreeFamiTF325228.

Enzyme and pathway databases

BioCyciZFISH:HS14755-MONOMER.
ReactomeiR-HSA-1482788. Acyl chain remodelling of PC.
R-HSA-1482801. Acyl chain remodelling of PS.
R-HSA-1482839. Acyl chain remodelling of PE.
R-HSA-1482922. Acyl chain remodelling of PI.
R-HSA-1482925. Acyl chain remodelling of PG.
R-HSA-1483115. Hydrolysis of LPC.
R-HSA-1483166. Synthesis of PA.

Miscellaneous databases

GenomeRNAii283748.
PROiQ86XP0.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000159337.
CleanExiHS_PLA2G4D.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR016035. Acyl_Trfase/lysoPLipase.
IPR000008. C2_dom.
IPR002642. LysoPLipase_cat_dom.
[Graphical view]
PfamiPF00168. C2. 1 hit.
PF01735. PLA2_B. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 1 hit.
SM00022. PLAc. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF52151. SSF52151. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS51210. PLA2C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPA24D_HUMAN
AccessioniPrimary (citable) accession number: Q86XP0
Secondary accession number(s): Q8N176
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: November 24, 2009
Last modified: November 2, 2016
This is version 113 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, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.