P97570 (PLPL9_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
85/88 kDa calcium-independent phospholipase A2
Short name=CaI-PLA2
EC=3.1.1.4

Alternative name(s):
Group VI phospholipase A2
Short name=GVI PLA2
Intracellular membrane-associated calcium-independent phospholipase A2 beta
Short name=iPLA2-beta
Patatin-like phospholipase domain-containing protein 9
Short name=PNPLA9

Gene names

Name:	Pla2g6
Synonyms:	Pnpla9

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	807 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the release of fatty acids from phospholipids. It has been implicated in normal phospholipid remodeling, nitric oxide-induced or vasopressin-induced arachidonic acid release and in leukotriene and prostaglandin production. May participate in fas mediated apoptosis and in regulating transmembrane ion flux in glucose-stimulated B-cells. Has a role in cardiolipin (CL) deacylation. Required for both speed and directionality of monocyte MCP1/CCL2-induced chemotaxis through regulation of F-actin polymerization at the pseudopods By similarity.
Catalytic activity	Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.
Enzyme regulation	Inhibited by calcium-activated calmodulin. Ref.5
Subcellular location	Isoform Long: Membrane By similarity; Peripheral membrane protein. Note: Recruited to the membrane-enriched pseudopod upon MCP1/CCL2 stimulation in monocytes By similarity. Isoform Short: Cytoplasm By similarity.
Tissue specificity	Found in brain, lung, spleen, kidney, liver, heart and skeletal muscle.
Sequence similarities	Contains 7 ANK repeats. Contains 1 patatin domain.

Ontologies

Keywords
Biological process	Chemotaxis Lipid degradation Lipid metabolism
Cellular component	Cytoplasm Membrane
Coding sequence diversity	Alternative splicing
Domain	ANK repeat Repeat
Ligand	Calmodulin-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cardiolipin biosynthetic process Inferred from electronic annotation. Source: Compara chemotaxis Inferred from electronic annotation. Source: UniProtKB-KW elevation of cytosolic calcium ion concentration Inferred from mutant phenotype PubMed 21178110. Source: RGD lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW maternal process involved in female pregnancy Inferred from expression pattern PubMed 16436530. Source: RGD memory Inferred from mutant phenotype PubMed 15830227. Source: RGD negative regulation of synaptic transmission, glutamatergic Inferred from mutant phenotype PubMed 15132431. Source: RGD positive regulation of arachidonic acid secretion Inferred from mutant phenotype PubMed 20732873. Source: RGD positive regulation of ceramide biosynthetic process Inferred from direct assay PubMed 18936091. Source: RGD positive regulation of exocytosis Inferred from mutant phenotype PubMed 12023524. Source: RGD positive regulation of insulin secretion involved in cellular response to glucose stimulus Inferred from direct assay PubMed 11278673. Source: RGD positive regulation of protein kinase C signaling cascade Inferred from mutant phenotype PubMed 22057271. Source: RGD positive regulation of protein phosphorylation Inferred from direct assay PubMed 15576376. Source: RGD positive regulation of release of cytochrome c from mitochondria Inferred from direct assay PubMed 18936091. Source: RGD positive regulation of vasodilation Inferred from mutant phenotype PubMed 12183647. Source: RGD regulation of store-operated calcium channel activity Inferred from mutant phenotype PubMed 12547829. Source: RGD response to endoplasmic reticulum stress Inferred from direct assay PubMed 20732873. Source: RGD urinary bladder smooth muscle contraction Inferred from mutant phenotype PubMed 12750876. Source: RGD
Cellular_component	centrosome Inferred from electronic annotation. Source: Compara cytosol Inferred from direct assay Ref.1. Source: RGD mitochondrial inner membrane Traceable author statement. Source: Reactome
Molecular_function	ATP-dependent protein binding Inferred from direct assay PubMed 20732873. Source: RGD calcium-independent phospholipase A2 activity Inferred from direct assay Ref.1. Source: RGD
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Long (identifier: P97570-1)

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.

Isoform Short (identifier: P97570-2)

The sequence of this isoform differs from the canonical sequence as follows:
     396-451: LITRKALLTLLKTVGADYHFPFIQGVSTEQSSAAGPHPFFSLDRTQPPTISLNNLE → Q

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 807	807	85/88 kDa calcium-independent phospholipase A2		PRO_0000067039
Regions
	Repeat	150 – 180	31	ANK 1
	Repeat	184 – 214	31	ANK 2
	Repeat	218 – 247	30	ANK 3
	Repeat	250 – 280	31	ANK 4
	Repeat	285 – 311	27	ANK 5
	Repeat	315 – 344	30	ANK 6
	Repeat	348 – 377	30	ANK 7
	Domain	481 – 665	185	Patatin
	Region	678 – 687	10	Calmodulin-binding
	Region	749 – 760	12	Calmodulin-binding
Sites
	Active site	520	1	Potential
Amino acid modifications
	Modified residue	588	1	Phosphothreonine By similarity
Natural variations
	Alternative sequence	396 – 451	56	LITRK…LNNLE → Q in isoform Short.		VSP_044365
Experimental info
	Sequence conflict	24	1	V → A in AAC53136. Ref.1
	Sequence conflict	58	1	V → D in AAC53136. Ref.1
	Sequence conflict	68	1	G → D in AAC53136. Ref.1
	Sequence conflict	80	1	A → V in AAC53136. Ref.1
	Sequence conflict	99	1	V → E in AAC53136. Ref.1
	Sequence conflict	109	1	Missing in AAC53136. Ref.1
	Sequence conflict	142	1	S → T in AAC53136. Ref.1
	Sequence conflict	477	1	S → T in AAC53136. Ref.1
	Sequence conflict	793	1	H → Y in AAC53136. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified October 31, 2012. Version 2. Checksum: 1B9018AE1B2D252F	FASTA	807	89,556
	10 20 30 40 50 60 MQFFGRLVNT LSSVTNLFSN PFRVKEVSLA DYASSERVRE EGQLILLQNA SNRTWDCVLV 70 80 90 100 110 120 SPRNPQSGFR LFQLESEADA LVNFQQYSSQ LPPFYESSVQ VLHVEVLQHL TDLIRNHPSW 130 140 150 160 170 180 TVTHLAVELG IRECFHHSRI ISCANSTENE EGCTPLHLAC RKGDSEILVE LVQYCHAQMD 190 200 210 220 230 240 VTDNKGETAF HYAVQGDNPQ VLQLLGKNAS AGLNQVNNQG LTPLHLACQM GKQEMVRVLL 250 260 270 280 290 300 LCNARCNIMG PGGFPIHTAM KFSQKGCAEM IISMDSNQIH SKDPRYGASP LHWAKNAEMA 310 320 330 340 350 360 RMLLKRGCDV DSTSASGNTA LHVAVTRNRF DCVMVLLTYG ANAGARGEHG NTPLHLAMSK 370 380 390 400 410 420 DNMEMVKALI VFGAEVDTPN DFGETPAFIA SKISKLITRK ALLTLLKTVG ADYHFPFIQG 430 440 450 460 470 480 VSTEQSSAAG PHPFFSLDRT QPPTISLNNL ELQDLMPVSR ARKPAFILSS MRDEKRSHDH 490 500 510 520 530 540 LLCLDGGGVK GLVIIQLLIA IEKASGVATK DLFDWVAGTS TGGILALAIL HSKSMAYMRG 550 560 570 580 590 600 VYFRMKDEVF RGSRPYESGP LEEFLKREFG EHTKMTDVKK PKVMLTGTLS DRQPAELHLF 610 620 630 640 650 660 RNYDAPEAVR EPRCTPNINL KPPTQPADQL VWRAARSSGA APTYFRPNGR FLDGGLLANN 670 680 690 700 710 720 PTLDAMTEIH EYNQDMIRKG QGNKVKKLSI VVSLGTGKSP QVPVTCVDVF RPSNPWELAK 730 740 750 760 770 780 TVFGAKELGK MVVDCCTDPD GRAVDRARAW CEMVGIQYFR LNPQLGSDIM LDEVSDAVLV 790 800 NALWETEVYI YEHREEFQKL VQLLLSP
	Isoform Short [UniParc]. Checksum: E622616FB108FDA0	FASTA	752	83,562
	10 20 30 40 50 60 MQFFGRLVNT LSSVTNLFSN PFRVKEVSLA DYASSERVRE EGQLILLQNA SNRTWDCVLV 70 80 90 100 110 120 SPRNPQSGFR LFQLESEADA LVNFQQYSSQ LPPFYESSVQ VLHVEVLQHL TDLIRNHPSW 130 140 150 160 170 180 TVTHLAVELG IRECFHHSRI ISCANSTENE EGCTPLHLAC RKGDSEILVE LVQYCHAQMD 190 200 210 220 230 240 VTDNKGETAF HYAVQGDNPQ VLQLLGKNAS AGLNQVNNQG LTPLHLACQM GKQEMVRVLL 250 260 270 280 290 300 LCNARCNIMG PGGFPIHTAM KFSQKGCAEM IISMDSNQIH SKDPRYGASP LHWAKNAEMA 310 320 330 340 350 360 RMLLKRGCDV DSTSASGNTA LHVAVTRNRF DCVMVLLTYG ANAGARGEHG NTPLHLAMSK 370 380 390 400 410 420 DNMEMVKALI VFGAEVDTPN DFGETPAFIA SKISKQLQDL MPVSRARKPA FILSSMRDEK 430 440 450 460 470 480 RSHDHLLCLD GGGVKGLVII QLLIAIEKAS GVATKDLFDW VAGTSTGGIL ALAILHSKSM 490 500 510 520 530 540 AYMRGVYFRM KDEVFRGSRP YESGPLEEFL KREFGEHTKM TDVKKPKVML TGTLSDRQPA 550 560 570 580 590 600 ELHLFRNYDA PEAVREPRCT PNINLKPPTQ PADQLVWRAA RSSGAAPTYF RPNGRFLDGG 610 620 630 640 650 660 LLANNPTLDA MTEIHEYNQD MIRKGQGNKV KKLSIVVSLG TGKSPQVPVT CVDVFRPSNP 670 680 690 700 710 720 WELAKTVFGA KELGKMVVDC CTDPDGRAVD RARAWCEMVG IQYFRLNPQL GSDIMLDEVS 730 740 750 DAVLVNALWE TEVYIYEHRE EFQKLVQLLL SP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Pancreatic islets express a Ca2+-independent phospholipase A2 enzyme that contains a repeated structural homologous to the integral membrane protein binding domain of ankyrin." Ma Z., Ramanadham S., Kempe K., Chi X.S., Ladenson J., Turk J. J. Biol. Chem. 272:11118-11127(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT). Strain: Sprague-Dawley. Tissue: Pancreatic islet.
[2]	"Genome sequence of the Brown Norway rat yields insights into mammalian evolution." Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S. Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Brown Norway.
[3]	Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M., Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L., Lu F. , Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Brown Norway.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG). Tissue: Testis.
[5]	"Identification of the calmodulin-binding domain of recombinant calcium-independent phospholipase A2beta. implications for structure and function." Jenkins C.M., Wolf M.J., Mancuso D.J., Gross R.W. J. Biol. Chem. 276:7129-7135(2001) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION, CALMODULIN-BINDING REGIONS.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U51898 mRNA. Translation: AAC53136.1. AABR06052011 Genomic DNA. No translation available. CH473950 Genomic DNA. Translation: EDM15808.1. CH473950 Genomic DNA. Translation: EDM15809.1. BC081916 mRNA. Translation: AAH81916.1.
IPI	IPI00189942. IPI00205595.
RefSeq	NP_001005560.1. NM_001005560.1. NP_001257725.1. NM_001270796.1.
UniGene	Rn.44692.
3D structure databases
ProteinModelPortal	P97570.
ModBase	Search...
Protein-protein interaction databases
IntAct	P97570. 1 interaction.
STRING	10116.ENSRNOP00000017104.
PTM databases
PhosphoSite	P97570.
Proteomic databases
PaxDb	P97570.
PRIDE	P97570.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000016827; ENSRNOP00000016827; ENSRNOG00000012295. ENSRNOT00000017108; ENSRNOP00000017104; ENSRNOG00000012295.
GeneID	360426.
KEGG	rno:360426.
UCSC	RGD:628867. rat.
Organism-specific databases
CTD	8398.
RGD	628867. Pla2g6.
Phylogenomic databases
eggNOG	COG0666.
GeneTree	ENSGT00530000063645.
HOGENOM	HOG000013092.
HOVERGEN	HBG053482.
KO	K16343.
OMA	PNGRFLD.
Enzyme and pathway databases
Reactome	REACT_113568. Metabolism.
Gene expression databases
ArrayExpress	P97570.
Genevestigator	P97570.
GermOnline	ENSRNOG00000012295. Rattus norvegicus.
Family and domain databases
Gene3D	1.25.40.20. 1 hit.
InterPro	IPR016035. Acyl_Trfase/lysoPLipase. IPR002110. Ankyrin_rpt. IPR020683. Ankyrin_rpt-contain_dom. IPR002641. Patatin/PLipase_A2-rel. [Graphical view]
Pfam	PF00023. Ank. 1 hit. PF12796. Ank_2. 2 hits. PF01734. Patatin. 1 hit. [Graphical view]
PRINTS	PR01415. ANKYRIN.
SMART	SM00248. ANK. 6 hits. [Graphical view]
SUPFAM	SSF52151. Acyl_Trfase/lysoPlipase. 1 hit. SSF48403. ANK. 1 hit.
PROSITE	PS50297. ANK_REP_REGION. 1 hit. PS50088. ANK_REPEAT. 4 hits. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL1075318.
NextBio	35583980.

Entry information

Entry name

PLPL9_RAT

Accession

Primary (citable) accession number: P97570
Secondary accession number(s): G3V7M8, Q66HD1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	October 31, 2012
Last modified:	May 1, 2013
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program