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PLA2_CAEEL
ID   PLA2_CAEEL              Reviewed;        1071 AA.
AC   Q20500;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 162.
DE   RecName: Full=Intracellular phospholipase A2;
DE            Short=IPLA-2;
DE            Short=PLA(2);
DE            EC=3.1.1.4 {ECO:0000250|UniProtKB:P97570};
DE   AltName: Full=Calcium-independent phospholipase A2 {ECO:0000303|PubMed:23007400};
GN   Name=ipla-2 {ECO:0000312|EMBL:CAA90061.1, ECO:0000312|WormBase:F47A4.5};
GN   ORFNames=F47A4.5 {ECO:0000312|WormBase:F47A4.5};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|EMBL:CAA90061.1,
RC   ECO:0000312|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=23007400; DOI=10.1074/jbc.m112.391508;
RA   Morrison K., Witte K., Mayers J.R., Schuh A.L., Audhya A.;
RT   "Roles of acidic phospholipids and nucleotides in regulating membrane
RT   binding and activity of a calcium-independent phospholipase A2 isoform.";
RL   J. Biol. Chem. 287:38824-38834(2012).
CC   -!- FUNCTION: Phospholipase that plays a critical role during oogenesis,
CC       ovulation, and/or embryogenesis. {ECO:0000269|PubMed:23007400}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC         glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC         Evidence={ECO:0000250|UniProtKB:P97570};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC         Evidence={ECO:0000250|UniProtKB:P97570};
CC   -!- DISRUPTION PHENOTYPE: Mutant animals generate fewer progeny and slower
CC       larval development. {ECO:0000269|PubMed:23007400}.
CC   -!- SIMILARITY: Belongs to the patatin family. {ECO:0000305}.
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DR   EMBL; BX284606; CAA90061.1; -; Genomic_DNA.
DR   PIR; T22327; T22327.
DR   RefSeq; NP_509647.1; NM_077246.4.
DR   AlphaFoldDB; Q20500; -.
DR   SMR; Q20500; -.
DR   STRING; 6239.F47A4.5; -.
DR   EPD; Q20500; -.
DR   PaxDb; Q20500; -.
DR   PeptideAtlas; Q20500; -.
DR   EnsemblMetazoa; F47A4.5.1; F47A4.5.1; WBGene00009801.
DR   GeneID; 181196; -.
DR   KEGG; cel:CELE_F47A4.5; -.
DR   UCSC; F47A4.5; c. elegans.
DR   CTD; 181196; -.
DR   WormBase; F47A4.5; CE02248; WBGene00009801; ipla-2.
DR   eggNOG; KOG0513; Eukaryota.
DR   HOGENOM; CLU_287465_0_0_1; -.
DR   InParanoid; Q20500; -.
DR   OMA; CHTENCY; -.
DR   OrthoDB; 146995at2759; -.
DR   PhylomeDB; Q20500; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00009801; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR   GO; GO:0051017; P:actin filament bundle assembly; IBA:GO_Central.
DR   GO; GO:0044258; P:intestinal lipid catabolic process; IMP:WormBase.
DR   GO; GO:0042594; P:response to starvation; IEP:WormBase.
DR   Gene3D; 1.25.40.20; -; 2.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR002641; PNPLA_dom.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF01734; Patatin; 1.
DR   SMART; SM00248; ANK; 6.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 3.
DR   PROSITE; PS51635; PNPLA; 1.
PE   3: Inferred from homology;
KW   ANK repeat; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Reference proteome; Repeat.
FT   CHAIN           1..1071
FT                   /note="Intracellular phospholipase A2"
FT                   /id="PRO_0000452652"
FT   REPEAT          411..440
FT                   /note="ANK 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          479..508
FT                   /note="ANK 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          510..539
FT                   /note="ANK 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          544..570
FT                   /note="ANK 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          578..610
FT                   /note="ANK 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          614..651
FT                   /note="ANK 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00023"
FT   REPEAT          652..681
FT                   /note="ANK 7"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          748..921
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           752..757
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           784..788
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           908..910
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        786
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        908
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
SQ   SEQUENCE   1071 AA;  119090 MW;  138067CA3E31C1D5 CRC64;
     MTTTNKDGPF RQQYLPGVHK EPNLAISEST HSSDWYSATS SEDCFQAASQ SFSSQKSNGN
     VITQQPGKLH CEISDPKSCS FVPAISTDNA QMGTSGIIKY RSYSNPDLLV AMSPLAYRDE
     APQSQKSVAN SRQDLTQTSC EVVTVSETVV NADSITTTTV TSSTTTTATA SQEDFIMVEA
     EQDETAGLCD ATMPLVDKKN ITTSSTTSSP SRQITPRIEN GLSFENVVSL VKIFPAFVNK
     LLKKPWYASR CDEVCQFPKA ELAYYDIVST DVDDEHFVIV AGKVTTDEHL MDNQFHLVFA
     PVGFSEDVSL DERPFSLFRA TDKKDLMDLL HLCDEKSFLF TSLDMSTMRA DILRSKIEEL
     VIQIRLKPHY HMIHVAIATD RLDFFSDGMI KTMNETLEPF ESQLRCLCHT ENCYPVHLAL
     TMDRQKIVER LLELDPTLFC ETDKAGNNVW HHVNSSFCAQ IIWDRCPASQ HFIDERNMDG
     QSPLNEAVST AKPLVATFLI GKGAKFTRGD RNELFVAMTS KNAQSVVEVV LTDKPEIANE
     RDALGNSAIH VALYKESLNA LLNRKVELGL DIDVKNNAGE TALLLFITTR KPDLLPLLVT
     LYAHGANMNA TDPHGNTALH KSAALVDAKK ISLECVKFLI SAGSNPNKIN LRGESPRHLA
     ASLQNQEMLA ILKAAGATRC PKGYKGCRSN CRHDCSSAED EYEETLQKIR IGNESDYEKT
     EFTASEKLNI QDTLDGSRRG KKAKVNLISM DGGGIRGLVI IQTLIAIEER LGDDIFKYFD
     WSAGTSTGSL IMAGLATGKS LREMQQTYLL LKDRVFDGIM PPYDTVQLEK FIQDQFGTGT
     VWEIPYPRLM ISAVNSEKLP VRLEMARNYK PAKDVAPETP KEMPLWMALR RSTAAPVLFK
     PSEDRYIDGG IISNNPALDL MSEVHAYNRE LQLSGRKSDA VQMNVLVSFG TGQIPSTVIE
     TLSIDSNSPL QSIKTIKNLA AMFIDQATAS EGAPVARSRQ WADSLEIPFF RFSAPLSKNI
     FLSSTSDLDV CTMMWDSFIY CRKHRDYIDE LVKVLKHDTD HPHVKTPFTD L
 
 
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