UniProtKB - P50393 (PA24A_RAT)
Protein
Cytosolic phospholipase A2
Gene
Pla2g4a
Organism
Rattus norvegicus (Rat)
Status
Functioni
Has primarily calcium-dependent phospholipase and lysophospholipase activities, with a major role in membrane lipid remodeling and biosynthesis of lipid mediators of the inflammatory response (By similarity). Plays an important role in embryo implantation and parturition through its ability to trigger prostanoid production (By similarity). Preferentially hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity). Selectively hydrolyzes sn-2 arachidonoyl group from membrane phospholipids, providing the precursor for eicosanoid biosynthesis via the cyclooxygenase pathway. In an alternative pathway of eicosanoid biosynthesis, hydrolyzes sn-2 fatty acyl chain of eicosanoid lysophopholipids to release free bioactive eicosanoids. Hydrolyzes the ester bond of the fatty acyl group attached at sn-1 position of phospholipids (phospholipase A1 activity) only if an ether linkage rather than an ester linkage is present at the sn-2 position. This hydrolysis is not stereospecific. Has calcium-independent phospholipase A2 and lysophospholipase activities in the presence of phosphoinositides. Has O-acyltransferase activity. Catalyzes the transfer of fatty acyl chains from phospholipids to a primary hydroxyl group of glycerol (sn-1 or sn-3), potentially contributing to monoacylglycerol synthesis (By similarity).By similarity
Catalytic activityi
- a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H+By similarityEC:3.1.1.4By similarityThis reaction proceeds in the forwardBy similarity direction.
- a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H+ + sn-glycerol 3-phosphocholineBy similarityEC:3.1.1.5By similarityThis reaction proceeds in the forwardBy similarity direction.
- 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H+By similarityThis reaction proceeds in the forwardBy similarity direction.
- 1,2-di-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H+By similarityThis reaction proceeds in the forwardBy similarity direction.
- 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-octadecanoyl-sn-glycero-3-phosphocholine + H+By similarityThis reaction proceeds in the forwardBy similarity direction.
- 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H+By similarityThis reaction proceeds in the forwardBy similarity direction.
- 1-octadecanoyl-2-(9Z,12Z,15Z-octadecatrienoyl)-sn-glycero-3-phosphocholine + H2O = (9Z,12Z,15Z)-octadecatrienoate + 1-octadecanoyl-sn-glycero-3-phosphocholine + H+By similarityThis reaction proceeds in the forwardBy similarity direction.
- 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-2-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H+ + hexadecanoateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- 1-O-hexadecyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-O-hexadecyl-sn-glycero-3-phosphocholine + H+By similarityThis reaction proceeds in the forwardBy similarity direction.
- 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1ʼ-sn-glycerol) + H2O = (9Z)-octadecenoate + 1-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + H+By similarityThis reaction proceeds in the forwardBy similarity direction.
- 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-octadecanoyl-sn-glycero-3-phosphate + H+By similarityThis reaction proceeds in the forwardBy similarity direction.
- 1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H+ + hexadecanoate + sn-glycerol 3-phosphocholineBy similarityThis reaction proceeds in the forwardBy similarity direction.
- 2-(prostaglandin E2)-sn-glycero-3-phosphoethanolamine + H2O = H+ + prostaglandin E2 + sn-glycero-3-phosphoethanolamineBy similarityThis reaction proceeds in the forwardBy similarity direction.
- 2-[(15S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl]-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,13E,15S)-hydroxyeicosatetraenoate + H+ + sn-glycerol 3-phosphocholineBy similarityThis reaction proceeds in the forwardBy similarity direction.
- 2-[(15R)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl]-sn-glycero-3-phosphocholine + H2O = (15R)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + H+ + sn-glycerol 3-phosphocholineBy similarityThis reaction proceeds in the forwardBy similarity direction.
- 2-(prostaglandin E2)-sn-glycero-3-phosphocholine + H2O = H+ + prostaglandin E2 + sn-glycerol 3-phosphocholineBy similarityThis reaction proceeds in the forwardBy similarity direction.
- 2-[(11R)-hydroxy-(5Z,8Z,12E,14Z)-eicosatetraenoyl]-sn-glycero-3-phosphocholine + H2O = (11R)-hydroxy-(5Z,8Z,12E,14Z)-eicosatetraenoate + H+ + sn-glycerol 3-phosphocholineBy similarityThis reaction proceeds in the forwardBy similarity direction.
- 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-2-O-hexadecyl-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 2-O-hexadecyl-sn-glycero-3-phosphocholine + H+By similarityThis reaction proceeds in the forwardBy similarity direction.
- 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + glycerol = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + 1-octadecanoyl-sn-glycero-3-phosphocholineBy similarityThis reaction proceeds in the forwardBy similarity direction.
- 1-octadecanoyl-2-(9Z,12Z,15Z-octadecatrienoyl)-sn-glycero-3-phosphocholine + glycerol = 1-(9Z,12Z,15Z-octadecatrienoyl)-glycerol + 1-octadecanoyl-sn-glycero-3-phosphocholineBy similarityThis reaction proceeds in the forwardBy similarity direction.
Activity regulationi
Activated by cytosolic calcium, which is necessary for binding to membrane lipids. Activated by phosphorylation in response to mitogenic stimuli.By similarity
: arachidonate metabolism Pathwayi
This protein is involved in the pathway arachidonate metabolism, which is part of Lipid metabolism.By similarityView all proteins of this organism that are known to be involved in the pathway arachidonate metabolism and in Lipid metabolism.
Pathwayi: glycerophospholipid metabolism
This protein is involved in the pathway glycerophospholipid metabolism, which is part of Membrane lipid metabolism.By similarityView all proteins of this organism that are known to be involved in the pathway glycerophospholipid metabolism and in Membrane lipid metabolism.
Pathwayi: prostaglandin biosynthesis
This protein is involved in the pathway prostaglandin biosynthesis, which is part of Lipid metabolism.By similarityView all proteins of this organism that are known to be involved in the pathway prostaglandin biosynthesis and in Lipid metabolism.
Pathwayi: leukotriene B4 biosynthesis
This protein is involved in the pathway leukotriene B4 biosynthesis, which is part of Lipid metabolism.By similarityView all proteins of this organism that are known to be involved in the pathway leukotriene B4 biosynthesis and in Lipid metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 40 | Calcium 1By similarity | 1 | |
Metal bindingi | 40 | Calcium 2By similarity | 1 | |
Metal bindingi | 41 | Calcium 1; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 43 | Calcium 1By similarity | 1 | |
Metal bindingi | 43 | Calcium 2By similarity | 1 | |
Metal bindingi | 65 | Calcium 1By similarity | 1 | |
Metal bindingi | 93 | Calcium 2By similarity | 1 | |
Metal bindingi | 94 | Calcium 2; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 95 | Calcium 2By similarity | 1 | |
Active sitei | 228 | NucleophileBy similarity | 1 | |
Active sitei | 549 | Proton acceptorBy similarity | 1 |
GO - Molecular functioni
- calcium-dependent phospholipase A2 activity Source: RGD
- calcium-dependent phospholipid binding Source: UniProtKB
- calcium-independent phospholipase A2 activity Source: RGD
- calcium ion binding Source: UniProtKB
- ceramide 1-phosphate binding Source: UniProtKB
- histone acetyltransferase binding Source: RGD
- lysophospholipase activity Source: UniProtKB
- O-acyltransferase activity Source: UniProtKB
- phosphatidylinositol-3-phosphate binding Source: UniProtKB
- phosphatidylinositol-4-phosphate binding Source: UniProtKB
- phosphatidylinositol-5-phosphate binding Source: UniProtKB
- phosphatidyl phospholipase B activity Source: UniProtKB-EC
- phospholipase A2 activity Source: RGD
- phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine) Source: UniProtKB-EC
- phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine) Source: UniProtKB-EC
GO - Biological processi
- aging Source: RGD
- arachidonic acid metabolic process Source: RGD
- arachidonic acid secretion Source: RGD
- cellular response to antibiotic Source: RGD
- decidualization Source: RGD
- glycerol metabolic process Source: UniProtKB-KW
- glycerophospholipid catabolic process Source: GO_Central
- icosanoid biosynthetic process Source: RGD
- leukotriene biosynthetic process Source: RGD
- luteolysis Source: RGD
- monoacylglycerol biosynthetic process Source: UniProtKB
- ovulation from ovarian follicle Source: RGD
- phosphatidylcholine acyl-chain remodeling Source: RGD
- phosphatidylcholine catabolic process Source: UniProtKB
- phosphatidylglycerol catabolic process Source: UniProtKB
- platelet activating factor biosynthetic process Source: RGD
- positive regulation of apoptotic process Source: RGD
- positive regulation of bone mineralization Source: RGD
- positive regulation of cell population proliferation Source: RGD
- positive regulation of fever generation Source: RGD
- positive regulation of inflammatory response Source: RGD
- positive regulation of macrophage activation Source: RGD
- positive regulation of platelet activation Source: RGD
- positive regulation of prostaglandin biosynthetic process Source: RGD
- positive regulation of prostaglandin secretion Source: RGD
- positive regulation of T-helper 1 type immune response Source: RGD
- positive regulation of vesicle fusion Source: RGD
- prostaglandin biosynthetic process Source: UniProtKB
- regulation of cell population proliferation Source: RGD
- response to calcium ion Source: RGD
- response to glucocorticoid Source: RGD
- response to heat Source: RGD
- response to hormone Source: RGD
- response to hydrogen peroxide Source: RGD
- response to lipopolysaccharide Source: RGD
- response to lithium ion Source: RGD
- response to methylmercury Source: RGD
- response to organic substance Source: RGD
- response to organonitrogen compound Source: RGD
- response to vitamin D Source: RGD
- surfactant homeostasis Source: RGD
Keywordsi
Enzyme and pathway databases
Reactomei | R-RNO-111995, phospho-PLA2 pathway R-RNO-1482788, Acyl chain remodelling of PC R-RNO-1482798, Acyl chain remodeling of CL R-RNO-1482801, Acyl chain remodelling of PS R-RNO-1482839, Acyl chain remodelling of PE R-RNO-1482922, Acyl chain remodelling of PI R-RNO-1482925, Acyl chain remodelling of PG R-RNO-1483115, Hydrolysis of LPC R-RNO-1483166, Synthesis of PA R-RNO-2142753, Arachidonic acid metabolism R-RNO-418592, ADP signalling through P2Y purinoceptor 1 R-RNO-432142, Platelet sensitization by LDL R-RNO-6811436, COPI-independent Golgi-to-ER retrograde traffic |
UniPathwayi | UPA00383 UPA00662 UPA00878 UPA00940 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:Pla2g4a Synonyms:Cpla2, Pla2g4 |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 67366, Pla2g4a |
Subcellular locationi
Nucleus
- Nucleus envelope By similarity
Golgi apparatus
- Golgi apparatus membrane By similarity
Cytoplasm and Cytosol
- Cytoplasm By similarity
Note: Translocates to intracellular membranes in a calcium-dependent way.By similarity
Cytosol
- cytosol Source: RGD
Endoplasmic reticulum
- endoplasmic reticulum Source: RGD
Golgi apparatus
- Golgi apparatus Source: RGD
- Golgi membrane Source: UniProtKB
Nucleus
- nuclear envelope Source: UniProtKB
- nucleus Source: RGD
Other locations
- cytoplasm Source: RGD
- intracellular membrane-bounded organelle Source: RGD
- perinuclear region of cytoplasm Source: RGD
- zymogen granule Source: RGD
Keywords - Cellular componenti
Cytoplasm, Golgi apparatus, Membrane, NucleusPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000187264 | 1 – 752 | Cytosolic phospholipase A2Add BLAST | 752 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | PhosphoserineBy similarity | 1 | |
Modified residuei | 268 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 434 | PhosphoserineCombined sources | 1 | |
Modified residuei | 435 | PhosphoserineBy similarity | 1 | |
Modified residuei | 437 | PhosphoserineCombined sources | 1 | |
Modified residuei | 505 | Phosphoserine; by MAPKBy similarity | 1 | |
Modified residuei | 511 | PhosphoserineCombined sources | 1 | |
Modified residuei | 515 | PhosphoserineCombined sources | 1 | |
Cross-linki | 541 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Cross-linki | 606 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Modified residuei | 727 | PhosphoserineCombined sources | 1 | |
Modified residuei | 729 | PhosphoserineBy similarity | 1 |
Post-translational modificationi
Phosphorylated at both Ser-505 and Ser-727 in response to mitogenic stimuli.By similarity
Keywords - PTMi
Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
PaxDbi | P50393 |
PRIDEi | P50393 |
PTM databases
iPTMneti | P50393 |
PhosphoSitePlusi | P50393 |
Expressioni
Tissue specificityi
In brain tissue, expressed in low levels in olfactory mitral and granule cells, in hippocampal pyramidal cells and in dentate and cerebellar granule cells.1 Publication
Inductioni
Levels of rat CPLA2 are increased in dentate granule cells during ischemia.1 Publication
Interactioni
Subunit structurei
Interacts with KAT5.
By similarityGO - Molecular functioni
- histone acetyltransferase binding Source: RGD
Protein-protein interaction databases
STRINGi | 10116.ENSRNOP00000003630 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 6 – 122 | C2PROSITE-ProRule annotationAdd BLAST | 117 | |
Domaini | 140 – 740 | PLA2cPROSITE-ProRule annotationAdd BLAST | 601 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 178 | Phospholipid bindingCuratedAdd BLAST | 178 |
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 calcium. In the presence of phosphoinositides, regulates phospholipase A2 and lysophospholipase activities in a calcium-independent way.By similarity
Phylogenomic databases
eggNOGi | KOG1012, Eukaryota KOG1325, Eukaryota |
InParanoidi | P50393 |
PhylomeDBi | P50393 |
Family and domain databases
CDDi | cd04036, C2_cPLA2, 1 hit |
Gene3Di | 2.60.40.150, 1 hit |
InterProi | View protein in InterPro IPR016035, Acyl_Trfase/lysoPLipase IPR041847, C2_cPLA2 IPR000008, C2_dom IPR035892, C2_domain_sf IPR002642, LysoPLipase_cat_dom |
Pfami | View protein in Pfam PF00168, C2, 1 hit PF01735, PLA2_B, 1 hit |
SMARTi | View protein in SMART SM00239, C2, 1 hit SM00022, PLAc, 1 hit |
SUPFAMi | SSF52151, SSF52151, 1 hit |
PROSITEi | View protein in PROSITE PS50004, C2, 1 hit PS51210, PLA2C, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All
P50393-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSFIDPYQHI IVEHQYSHKF TVVVLRATKV TKGTFGDMLD TPDPYVELFI
60 70 80 90 100
STTPDSRKRT RHFNNDINPV WNETFEFILD PNQENVLEIT LMDANYVMDE
110 120 130 140 150
TLGTATFPVS SMKVGEKKEV PFIFNQVTEM ILEMSLEVCS CPDLRFSMAL
160 170 180 190 200
CDQEKTFRRQ RKENIKENMK KLLGPKKSEG LYSTRDVPVV AILGSGGGFR
210 220 230 240 250
AMVGFSGVMK ALYESGILDC ATYVAGLSGS TWYMSTLYSH PDFPEKGPEE
260 270 280 290 300
INEELMKNVS HNPLLLLTPQ KVKRYVESLW KKKSSGQPVT FTDIFGMLIG
310 320 330 340 350
ETLIQNRMST TLSSLKEKVS AARCPLPLFT CLHVKPDVSE LMFADWVEFS
360 370 380 390 400
PYEIGMAKYG TFMTPDLFGS KFFMGTVVKK YEENPLHFLM GVWGSAFSIL
410 420 430 440 450
FNRVLGVSGS QNKGSTMEEE LENITAKHIV SNDSSDSDDE AQGPKGTENE
460 470 480 490 500
DAEREYQNDN QASWVHRMLM ALVSDSALFN TREGRAGKEH NFMLGLNLNT
510 520 530 540 550
SYPLSPLRDF SPQDSFDDDE LDAAVADPDE FERIYEPLDV KSKKIHVVDS
560 570 580 590 600
GLTFNLPYPL ILRPQRGVDL IISFDFSARP SDTSPPFKEL LLAEKWAKMN
610 620 630 640 650
KLPFPKIDPY VFDREGLKEC YVFKPKNPDV EKDCPTIIHF VLANINFRKY
660 670 680 690 700
KAPGVLRETK EEKEIADFDI FDDPESPFST FNFQYPNQAF KRLHDLMYFN
710 720 730 740 750
TLNNIDVIKD AIVESIEYRR QNPSRCSVSL SNVEARKFFN KEFLSKPTAE
SI
Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketQ6IRF5 | Q6IRF5_RAT | Phospholipase A2 | Pla2g4a rCG_46421 | 752 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 139 | C → S in AAC21591 (PubMed:9555100).Curated | 1 | |
Sequence conflicti | 159 | R → Q in AAC21591 (PubMed:9555100).Curated | 1 | |
Sequence conflicti | 287 | Q → L in AAC21591 (PubMed:9555100).Curated | 1 | |
Sequence conflicti | 308 – 310 | MST → IVP in AAC21591 (PubMed:9555100).Curated | 3 | |
Sequence conflicti | 410 | S → L in AAC21591 (PubMed:9555100).Curated | 1 | |
Sequence conflicti | 489 | E → V in AAC21591 (PubMed:9555100).Curated | 1 | |
Sequence conflicti | 635 | P → T in AAC21591 (PubMed:9555100).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | S77829 mRNA Translation: AAB33847.1 U38376 mRNA Translation: AAC21591.1 |
Genome annotation databases
UCSCi | RGD:67366, rat |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | S77829 mRNA Translation: AAB33847.1 U38376 mRNA Translation: AAC21591.1 |
3D structure databases
BMRBi | P50393 |
SMRi | P50393 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 10116.ENSRNOP00000003630 |
PTM databases
iPTMneti | P50393 |
PhosphoSitePlusi | P50393 |
Proteomic databases
PaxDbi | P50393 |
PRIDEi | P50393 |
Genome annotation databases
UCSCi | RGD:67366, rat |
Organism-specific databases
RGDi | 67366, Pla2g4a |
Phylogenomic databases
eggNOGi | KOG1012, Eukaryota KOG1325, Eukaryota |
InParanoidi | P50393 |
PhylomeDBi | P50393 |
Enzyme and pathway databases
UniPathwayi | UPA00383 UPA00662 UPA00878 UPA00940 |
Reactomei | R-RNO-111995, phospho-PLA2 pathway R-RNO-1482788, Acyl chain remodelling of PC R-RNO-1482798, Acyl chain remodeling of CL R-RNO-1482801, Acyl chain remodelling of PS R-RNO-1482839, Acyl chain remodelling of PE R-RNO-1482922, Acyl chain remodelling of PI R-RNO-1482925, Acyl chain remodelling of PG R-RNO-1483115, Hydrolysis of LPC R-RNO-1483166, Synthesis of PA R-RNO-2142753, Arachidonic acid metabolism R-RNO-418592, ADP signalling through P2Y purinoceptor 1 R-RNO-432142, Platelet sensitization by LDL R-RNO-6811436, COPI-independent Golgi-to-ER retrograde traffic |
Miscellaneous databases
PROi | PR:P50393 |
Family and domain databases
CDDi | cd04036, C2_cPLA2, 1 hit |
Gene3Di | 2.60.40.150, 1 hit |
InterProi | View protein in InterPro IPR016035, Acyl_Trfase/lysoPLipase IPR041847, C2_cPLA2 IPR000008, C2_dom IPR035892, C2_domain_sf IPR002642, LysoPLipase_cat_dom |
Pfami | View protein in Pfam PF00168, C2, 1 hit PF01735, PLA2_B, 1 hit |
SMARTi | View protein in SMART SM00239, C2, 1 hit SM00022, PLAc, 1 hit |
SUPFAMi | SSF52151, SSF52151, 1 hit |
PROSITEi | View protein in PROSITE PS50004, C2, 1 hit PS51210, PLA2C, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PA24A_RAT | |
Accessioni | P50393Primary (citable) accession number: P50393 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1996 |
Last sequence update: | October 1, 1996 | |
Last modified: | April 7, 2021 | |
This is version 143 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways