MOUSE:PLA2R

Species (Taxon ID)	Mus musculus (Mouse). (10090)
Gene Name(s)	Pla2r1 (synonyms: Pla2g1br)
Protein Name(s)	Secretory phospholipase A2 receptor PLA2-R PLA2R 180 kDa secretory phospholipase A2 receptor M-type receptor Soluble secretory phospholipase A2 receptor Soluble PLA2-R Soluble PLA2R
External Links
UniProt	Q62028
EMBL	D30779 BX679662 AL928546 AL928546 BX679662 BC048780 BC141355 BC141356
CCDS	CCDS16059.1
PIR	S48719
RefSeq	NP_032893.1
UniGene	Mm.5092
ProteinModelPortal	Q62028
SMR	Q62028
IntAct	Q62028
MINT	MINT-4109893
STRING	10090.ENSMUSP00000108144
PaxDb	Q62028
PRIDE	Q62028
Ensembl	ENSMUST00000067708
GeneID	18779
KEGG	mmu:18779
UCSC	uc008jug.2 uc008juh.2
CTD	22925
MGI	MGI:102468
eggNOG	NOG288621
GeneTree	ENSGT00720000108514
HOGENOM	HOG000231191
HOVERGEN	HBG108261
InParanoid	Q62028
KO	K06560
OrthoDB	EOG7FFMQR
PhylomeDB	Q62028
TreeFam	TF316663
NextBio	295027
PRO	PR:Q62028
Proteomes	UP000000589
Bgee	Q62028
CleanEx	MM_PLA2R1
Genevestigator	Q62028
GO	GO:0005576 GO:0016021 GO:0005886 GO:0043235 GO:0030246 GO:0043274 GO:0004872 GO:0001816 GO:1900139 GO:1900138 GO:0090403 GO:0090238 GO:0043517 GO:0072593 GO:0006898 GO:0090399
Gene3D	2.10.10.10 3.10.100.10
InterPro	IPR001304 IPR016186 IPR018378 IPR016187 IPR000562 IPR000772
Pfam	PF00040 PF00059
SMART	SM00034 SM00059 SM00458
SUPFAM	SSF50370 SSF56436
PROSITE	PS00615 PS50041 PS00023 PS51092 PS50231

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0004623	phospholipase A2 activity	PMID:25623068^[1]	ECO:0000314			F		This paper tests the effects of phospholipase A2 activity and provides necessary information for the annotation.	complete CACAO 10681
involved_in	GO:0090403	oxidative stress-induced premature senescence	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q13018	P		Seeded From UniProt	complete
involved_in	GO:0090399	replicative senescence	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q13018	P		Seeded From UniProt	complete
involved_in	GO:0090238	positive regulation of arachidonic acid secretion	PMID:10946309^[2]	ECO:0000314	direct assay evidence used in manual assertion		P	occurs_in:(CL:0000097)	Seeded From UniProt	complete
involved_in	GO:0072593	reactive oxygen species metabolic process	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q13018	P		Seeded From UniProt	complete
involved_in	GO:0043517	positive regulation of DNA damage response, signal transduction by p53 class mediator	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q13018	P		Seeded From UniProt	complete
enables	GO:0043274	phospholipase binding	PMID:7925459^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P00592	F		Seeded From UniProt	complete
involved_in	GO:0006898	receptor-mediated endocytosis	PMID:7925459^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q13018	C		Seeded From UniProt	complete
enables	GO:0038023	signaling receptor activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q13018-1	F		Seeded From UniProt	complete
involved_in	GO:0001816	cytokine production	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q13018	P		Seeded From UniProt	complete
enables	GO:0004888	transmembrane signaling receptor activity	PMID:21873635^[4]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:97142 PANTHER:PTN002335023	F		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0090403	oxidative stress-induced premature senescence	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q13018	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0090399	replicative senescence	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q13018	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0072593	reactive oxygen species metabolic process	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q13018	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0043517	positive regulation of DNA damage response, signal transduction by p53 class mediator	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q13018	P		Seeded From UniProt	complete
enables	GO:0043274	phospholipase binding	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q13018	F		Seeded From UniProt	complete
part_of	GO:0043235	receptor complex	PMID:23382219^[5]	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q13018	C		Seeded From UniProt	complete
enables	GO:0038023	signaling receptor activity	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q13018	F		Seeded From UniProt	complete
part_of	GO:0009986	cell surface	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q13018	C		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0006898	receptor-mediated endocytosis	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q13018	P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q13018	C		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0001816	cytokine production	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q13018	P		Seeded From UniProt	complete
involved_in	GO:0090403	oxidative stress-induced premature senescence	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q13018 ensembl:ENSP00000283243	P		Seeded From UniProt	complete
involved_in	GO:0090399	replicative senescence	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q13018 ensembl:ENSP00000283243	P		Seeded From UniProt	complete
involved_in	GO:0072593	reactive oxygen species metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q13018 ensembl:ENSP00000283243	P		Seeded From UniProt	complete
involved_in	GO:0043517	positive regulation of DNA damage response, signal transduction by p53 class mediator	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q13018 ensembl:ENSP00000283243	P		Seeded From UniProt	complete
part_of	GO:0043235	receptor complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q13018 ensembl:ENSP00000283243	C		Seeded From UniProt	complete
part_of	GO:0009986	cell surface	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q13018 ensembl:ENSP00000283243	C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q13018 ensembl:ENSP00000283243	C		Seeded From UniProt	complete
involved_in	GO:0001816	cytokine production	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q13018 ensembl:ENSP00000283243	P		Seeded From UniProt	complete
involved_in	GO:1900139	negative regulation of arachidonic acid secretion	PMID:11830583^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1900138	negative regulation of phospholipase A2 activity	PMID:11830583^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P97391)	Seeded From UniProt	complete
enables	GO:0043274	phospholipase binding	PMID:11830583^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P00592	F		Seeded From UniProt	complete
enables	GO:0043274	phospholipase binding	PMID:11830583^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P97391	F		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	PMID:11830583^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0016021	integral component of membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0812	C		Seeded From UniProt	complete
enables	GO:0030246	carbohydrate binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0430	F		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1003 UniProtKB-SubCell:SL-0039	C		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0964 UniProtKB-SubCell:SL-0243	C		Seeded From UniProt	complete
involved_in	GO:0006897	endocytosis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0254	P		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Layne, JD et al. (2015) Ectopically expressed pro-group X secretory phospholipase A2 is proteolytically activated in mouse adrenal cells by furin-like proprotein convertases: implications for the regulation of adrenal steroidogenesis. J. Biol. Chem. 290 7851-60 PubMed GONUTS page
↑ Fonteh, AN et al. (2000) Secretory phospholipase A2 receptor-mediated activation of cytosolic phospholipase A2 in murine bone marrow-derived mast cells. J. Immunol. 165 2773-82 PubMed GONUTS page
↑ ^3.0 ^3.1 Higashino, K et al. (1994) Structural comparison of phospholipase-A2-binding regions in phospholipase-A2 receptors from various mammals. Eur. J. Biochem. 225 375-82 PubMed GONUTS page
↑ Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Ghai, R et al. (2013) Structural basis for endosomal trafficking of diverse transmembrane cargos by PX-FERM proteins. Proc. Natl. Acad. Sci. U.S.A. 110 E643-52 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 ^6.3 ^6.4 Higashino Ki, K et al. (2002) Identification of a soluble form phospholipase A2 receptor as a circulating endogenous inhibitor for secretory phospholipase A2. J. Biol. Chem. 277 13583-8 PubMed GONUTS page

[PMID:25623068-1] Layne, JD et al. (2015) Ectopically expressed pro-group X secretory phospholipase A2 is proteolytically activated in mouse adrenal cells by furin-like proprotein convertases: implications for the regulation of adrenal steroidogenesis. J. Biol. Chem. 290 7851-60 PubMed GONUTS page

[PMID:10946309-2] Fonteh, AN et al. (2000) Secretory phospholipase A2 receptor-mediated activation of cytosolic phospholipase A2 in murine bone marrow-derived mast cells. J. Immunol. 165 2773-82 PubMed GONUTS page

[PMID:7925459-3] 3.0 ^3.1 Higashino, K et al. (1994) Structural comparison of phospholipase-A2-binding regions in phospholipase-A2 receptors from various mammals. Eur. J. Biochem. 225 375-82 PubMed GONUTS page

[PMID:21873635-4] Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:23382219-5] Ghai, R et al. (2013) Structural basis for endosomal trafficking of diverse transmembrane cargos by PX-FERM proteins. Proc. Natl. Acad. Sci. U.S.A. 110 E643-52 PubMed GONUTS page

[PMID:11830583-6] 6.0 ^6.1 ^6.2 ^6.3 ^6.4 Higashino Ki, K et al. (2002) Identification of a soluble form phospholipase A2 receptor as a circulating endogenous inhibitor for secretory phospholipase A2. J. Biol. Chem. 277 13583-8 PubMed GONUTS page

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MOUSE:PLA2R

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