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P0C869 (PA24B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytosolic phospholipase A2 beta

Short name=cPLA2-beta
EC=3.1.1.4
Alternative name(s):
Phospholipase A2 group IVB
Gene names
Name:PLA2G4B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length781 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Calcium-dependent phospholipase A2 that selectively hydrolyzes glycerophospholipids in the sn-2 position with a preference for arachidonoyl phospholipids. Has a much weaker activity than PLA2G4A. Isoform 3 has calcium-dependent activity against palmitoyl-arachidonyl-phosphatidylethanolamine and low level lysophospholipase activity but no activity against phosphatidylcholine. Isoform 5 does have activity against phosphatidylcholine. Ref.1 Ref.2 Ref.3

Catalytic activity

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate. Ref.1 Ref.2 Ref.3

Enzyme regulation

Stimulated by cytosolic Ca2+. Ref.1 Ref.2

Subcellular location

Cytoplasmcytosol Ref.3.

Isoform 3: Mitochondrion membrane; Peripheral membrane protein. Early endosome membrane; Peripheral membrane protein. Note: Translocates to membrane vesicles in a calcium-dependent fashion. Ref.3

Tissue specificity

Widely expressed. Expressed at higher level in brain, heart, liver, cerebellum and pancreas. Isoform 3 is widely expressed. Ref.1 Ref.2 Ref.3

Domain

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.

Sequence similarities

Contains 1 C2 domain.

Contains 1 PLA2c domain.

Caution

Most tissues also express read-through transcripts from this gene into the upstream gene (JMJD7), some of which may encode fusion proteins.

Biophysicochemical properties

Kinetic parameters:

Vmax=7.9 pmol/min/mg enzyme (isoform 5) Ref.1

Vmax=3.6 pmol/min/µg enzyme with cAMP as substrate (isoform 4)

Vmax=140 nmol/min/µg enzyme with 1-[14C]16:0-2-lyso-PC as substrate (isoform 5)

Vmax=1.6 nmol/min/µg enzyme with 1-[14C]16:0-2-lyso-PC as substrate (isoform 3)

Vmax=2.1 nmol/min/µg enzyme with 1-16:0-2-[14C]20:4-PC as substrate (isoform 5)

Vmax=0.6 nmol/min/µg enzyme with 1-16:0-2-[14C]20:4-PE as substrate (isoform 5)

Vmax=0.8 nmol/min/µg enzyme with 1-16:0-2-[14C]20:4-PE as substrate (isoform 3)

Vmax=0.3 nmol/min/µg enzyme with 1-16:0-2-[14C]18:2-PE as substrate (isoform 3)

Sequence caution

The sequence BAD92387.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentCytoplasm
Endosome
Membrane
Mitochondrion
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of signaling protein activity involved in unfolded protein response

Traceable author statement. Source: Reactome

arachidonic acid metabolic process

Non-traceable author statement Ref.1. Source: UniProtKB

calcium-mediated signaling

Non-traceable author statement Ref.1. Source: UniProtKB

cellular protein metabolic process

Traceable author statement. Source: Reactome

endoplasmic reticulum unfolded protein response

Traceable author statement. Source: Reactome

glycerophospholipid biosynthetic process

Traceable author statement. Source: Reactome

glycerophospholipid catabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

inflammatory response

Non-traceable author statement Ref.1. Source: UniProtKB

parturition

Non-traceable author statement Ref.1. Source: UniProtKB

phosphatidic acid biosynthetic process

Traceable author statement. Source: Reactome

phosphatidylcholine acyl-chain remodeling

Traceable author statement. Source: Reactome

phosphatidylethanolamine acyl-chain remodeling

Traceable author statement. Source: Reactome

phosphatidylglycerol acyl-chain remodeling

Traceable author statement. Source: Reactome

phosphatidylserine acyl-chain remodeling

Traceable author statement. Source: Reactome

phospholipid metabolic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Inferred from direct assay Ref.2. Source: UniProtKB

early endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Traceable author statement Ref.1. Source: UniProtKB

mitochondrial inner membrane

Traceable author statement. Source: Reactome

   Molecular_functioncalcium ion binding

Non-traceable author statement Ref.1. Source: UniProtKB

calcium-dependent phospholipase A2 activity

Inferred from direct assay Ref.1. Source: UniProtKB

calcium-dependent phospholipid binding

Non-traceable author statement Ref.1. Source: UniProtKB

lysophospholipase activity

Non-traceable author statement Ref.2. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P0C869-1)

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 2 (identifier: P0C869-7)

Also known as: beta2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-3: MAV → MAEAALEAVR...KVVDEEAMEK
     650-662: QLQLLGRFCQEQG → GSGGHPRRRQLGR
     663-781: Missing.
Note: Based on a naturally occurring readthrough transcript which produces a JMJD7-PLA2G4B fusion protein.
Isoform 3 (identifier: P0C869-8)

Also known as: beta3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-3: MAV → MAEAALEAVR...KVVDEEAMEK
     641-765: Missing.
Note: Based on a naturally occurring readthrough transcript which produces a JMJD7-PLA2G4B fusion protein.
Isoform 4 (identifier: P0C869-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-299: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: P0C869-6)

Also known as: Beta1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-3: MAV → MAEAALEAVR...KVVDEEAMEK
Note: Based on a naturally occurring readthrough transcript which produces a JMJD7-PLA2G4B fusion protein.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 781781Cytosolic phospholipase A2 beta
PRO_0000247021

Regions

Domain1 – 9797C2
Domain246 – 781536PLA2c

Sites

Active site3351Nucleophile By similarity
Active site6151Proton acceptor By similarity

Natural variations

Alternative sequence1 – 299299Missing in isoform 4.
VSP_019871
Alternative sequence1 – 33MAV → MAEAALEAVRSELREFPAAA RELCVPLAVPYLDKPPTPLH FYRDWVCPNRPCIIRNALQH WPALQKWSLPYFRATVGSTE VSVAVTPDGYADAVRGDRFM MPAERRLPLSFVLDVLEGRA QHPGVLYVQKQCSNLPSELP QLLPDLESHVPWASEALGKM PDAVNFWLGEAAAVTSLHKD HYENLYCVVSGEKHFLFHPP SDRPFIPYELYTPATYQLTE EGTFKVVDEEAMEK in isoform 2, isoform 3 and isoform 5.
VSP_039387
Alternative sequence641 – 765125Missing in isoform 3.
VSP_039388
Alternative sequence650 – 66213QLQLL…CQEQG → GSGGHPRRRQLGR in isoform 2.
VSP_039389
Alternative sequence663 – 781119Missing in isoform 2.
VSP_039390
Natural variant1911R → C. Ref.4
Corresponds to variant rs3816533 [ dbSNP | Ensembl ].
VAR_027047
Natural variant2391M → I.
Corresponds to variant rs2290552 [ dbSNP | Ensembl ].
VAR_027048
Natural variant3911R → H.
Corresponds to variant rs34807597 [ dbSNP | Ensembl ].
VAR_034365
Natural variant5911T → I.
Corresponds to variant rs36126315 [ dbSNP | Ensembl ].
VAR_060082

Experimental info

Mutagenesis3351S → A: Abolishes enzyme activity. Ref.1
Mutagenesis4171H → A: No effect. Ref.1
Mutagenesis6151D → A: Abolishes enzyme activity. Ref.1
Mutagenesis6321R → A: Abolishes enzyme activity. Ref.1
Sequence conflict1381L → F in AAD32135. Ref.2
Sequence conflict1621Q → P in ABF69195. Ref.3
Sequence conflict1621Q → P in ABF69196. Ref.3
Sequence conflict4381A → V in ABF69195. Ref.3
Sequence conflict5171S → P in ABF69195. Ref.3
Sequence conflict5751R → C in BAG61401. Ref.4
Sequence conflict7231G → E in BAG61401. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 13, 2010. Version 2.
Checksum: 4C5C6861E7BAB1B8

FASTA78187,978
        10         20         30         40         50         60 
MAVAEVSRTC LLTVRVLQAH RLPSKDLVTP SDCYVTLWLP TACSHRLQTR TVKNSSSPVW 

        70         80         90        100        110        120 
NQSFHFRIHR QLKNVMELKV FDQDLVTGDD PVLSVLFDAG TLRAGEFRRE SFSLSPQGEG 

       130        140        150        160        170        180 
RLEVEFRLQS LADRGEWLVS NGVLVARELS CLHVQLEETG DQKSSEHRVQ LVVPGSCEGP 

       190        200        210        220        230        240 
QEASVGTGTF RFHCPACWEQ ELSIRLQDAP EEQLKAPLSA LPSGQVVRLV FPTSQEPLMR 

       250        260        270        280        290        300 
VELKKEAGLR ELAVRLGFGP CAEEQAFLSR RKQVVAAALR QALQLDGDLQ EDEIPVVAIM 

       310        320        330        340        350        360 
ATGGGIRAMT SLYGQLAGLK ELGLLDCVSY ITGASGSTWA LANLYEDPEW SQKDLAGPTE 

       370        380        390        400        410        420 
LLKTQVTKNK LGVLAPSQLQ RYRQELAERA RLGYPSCFTN LWALINEALL HDEPHDHKLS 

       430        440        450        460        470        480 
DQREALSHGQ NPLPIYCALN TKGQSLTTFE FGEWCEFSPY EVGFPKYGAF IPSELFGSEF 

       490        500        510        520        530        540 
FMGQLMKRLP ESRICFLEGI WSNLYAANLQ DSLYWASEPS QFWDRWVRNQ ANLDKEQVPL 

       550        560        570        580        590        600 
LKIEEPPSTA GRIAEFFTDL LTWRPLAQAT HNFLRGLHFH KDYFQHPHFS TWKATTLDGL 

       610        620        630        640        650        660 
PNQLTPSEPH LCLLDVGYLI NTSCLPLLQP TRDVDLILSL DYNLHGAFQQ LQLLGRFCQE 

       670        680        690        700        710        720 
QGIPFPPISP SPEEQLQPRE CHTFSDPTCP GAPAVLHFPL VSDSFREYSA PGVRRTPEEA 

       730        740        750        760        770        780 
AAGEVNLSSS DSPYHYTKVT YSQEDVDKLL HLTHYNVCNN QEQLLEALRQ AVQRRRQRRP 


H 

« Hide

Isoform 2 (beta2) [UniParc].

Checksum: 0A7C3BE752C48F55
Show »

FASTA893100,516
Isoform 3 (beta3) [UniParc].

Checksum: 4C5CC6D084F2DF99
Show »

FASTA887100,094
Isoform 4 [UniParc] [UniParc].

Checksum: EB8FC2F2EB2AE258
Show »

FASTA48254,679
Isoform 5 (Beta1) [UniParc].

Checksum: 989EDB4AD3CF19DD
Show »

FASTA1,012114,121

References

« Hide 'large scale' references
[1]"Molecular cloning of two new human paralogs of 85-kDa cytosolic phospholipase A2."
Pickard R.T., Strifler B.A., Kramer R.M., Sharp J.D.
J. Biol. Chem. 274:8823-8831(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, TISSUE SPECIFICITY, MUTAGENESIS OF SER-335; HIS-417; ASP-615 AND ARG-632.
[2]"Molecular characterization of cytosolic phospholipase A2-beta."
Song C., Chang X.J., Bean K.M., Proia M.S., Knopf J.L., Kriz R.W.
J. Biol. Chem. 274:17063-17067(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, TISSUE SPECIFICITY.
[3]"Identification of the expressed form of human cytosolic phospholipase A2beta (cPLA2beta): cPLA2beta3 is a novel variant localized to mitochondria and early endosomes."
Ghosh M., Loper R., Gelb M.H., Leslie C.C.
J. Biol. Chem. 281:16615-16624(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT CYS-191.
Tissue: Tongue.
[5]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Brain.
[6]"Analysis of the DNA sequence and duplication history of human chromosome 15."
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. expand/collapse author list , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF065215 mRNA. Translation: AAC78836.1.
AF121908 mRNA. Translation: AAD32135.1.
DQ523799 mRNA. Translation: ABF69195.1.
DQ523800 mRNA. Translation: ABF69196.1.
AK299419 mRNA. Translation: BAG61401.1.
AB209150 mRNA. Translation: BAD92387.1. Different initiation.
AC020659 Genomic DNA. No translation available.
RefSeqNP_001108105.1. NM_001114633.1.
NP_001185517.1. NM_001198588.1.
NP_005081.1. NM_005090.3.
UniGeneHs.198161.

3D structure databases

ProteinModelPortalP0C869.
SMRP0C869. Positions 5-777.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid936685. 4 interactions.
IntActP0C869. 2 interactions.
STRING9606.ENSP00000396045.

Chemistry

BindingDBP0C869.
ChEMBLCHEMBL4136.

PTM databases

PhosphoSiteP0C869.

Polymorphism databases

DMDM300669659.

Proteomic databases

PaxDbP0C869.
PRIDEP0C869.

Protocols and materials databases

DNASU8681.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000452633; ENSP00000396045; ENSG00000243708. [P0C869-1]
ENST00000458483; ENSP00000416610; ENSG00000243708. [P0C869-1]
ENST00000542534; ENSP00000441905; ENSG00000243708. [P0C869-6]
GeneID100137049.
8681.
KEGGhsa:100137049.
hsa:8681.
UCSCuc001zoo.4. human. [P0C869-6]
uc001zoq.4. human.
uc010bcn.3. human. [P0C869-7]

Organism-specific databases

CTD100137049.
8681.
GeneCardsGC15P042129.
HGNCHGNC:9036. PLA2G4B.
HPAHPA005726.
MIM606088. gene.
neXtProtNX_P0C869.
PharmGKBPA165479070.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG239428.
HOVERGENHBG080412.
InParanoidP0C869.
KOK16342.
OrthoDBEOG70CR62.
PhylomeDBP0C869.
TreeFamTF325228.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_17015. Metabolism of proteins.

Gene expression databases

BgeeP0C869.
GenevestigatorP0C869.

Family and domain databases

Gene3D2.60.40.150. 1 hit.
InterProIPR016035. Acyl_Trfase/lysoPLipase.
IPR000008. C2_dom.
IPR002642. LysoPLipase_cat_dom.
[Graphical view]
PfamPF00168. C2. 1 hit.
PF01735. PLA2_B. 1 hit.
[Graphical view]
SMARTSM00239. C2. 1 hit.
SM00022. PLAc. 1 hit.
[Graphical view]
SUPFAMSSF49562. SSF49562. 1 hit.
SSF52151. SSF52151. 1 hit.
PROSITEPS50004. C2. 1 hit.
PS51210. PLA2C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPLA2G4B.
NextBio20774774.
PROP0C869.
SOURCESearch...

Entry information

Entry namePA24B_HUMAN
AccessionPrimary (citable) accession number: P0C869
Secondary accession number(s): B4DRT9 expand/collapse secondary AC list , O95712, Q19KD5, Q19KD6, Q59GF9, Q8TB10, Q9UKV7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: July 13, 2010
Last modified: April 16, 2014
This is version 58 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM