ID A8X073_CAEBR Unreviewed; 1062 AA.
AC A8X073;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 2.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=phospholipase A2 {ECO:0000256|ARBA:ARBA00013278};
DE EC=3.1.1.4 {ECO:0000256|ARBA:ARBA00013278};
GN Name=ipla-3 {ECO:0000313|WormBase:CBG05582a};
GN ORFNames=CBG05582 {ECO:0000313|EMBL:CAP26033.2,
GN ECO:0000313|WormBase:CBG05582a}, CBG_05582
GN {ECO:0000313|EMBL:CAP26033.2};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP26033.2, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP26033.2, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP26033.2,
RC ECO:0000313|Proteomes:UP000008549};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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:0000256|ARBA:ARBA00023422};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000256|ARBA:ARBA00023422};
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DR EMBL; HE601419; CAP26033.2; -; Genomic_DNA.
DR AlphaFoldDB; A8X073; -.
DR STRING; 6238.A8X073; -.
DR WormBase; CBG05582a; CBP44538; WBGene00028002; Cbr-ipla-3.
DR eggNOG; KOG0513; Eukaryota.
DR HOGENOM; CLU_010817_0_0_1; -.
DR InParanoid; A8X073; -.
DR OMA; KAYMHSN; -.
DR OrthoDB; 518048at2759; -.
DR Proteomes; UP000008549; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0047499; F:calcium-independent phospholipase A2 activity; IEA:InterPro.
DR GO; GO:0051017; P:actin filament bundle assembly; IBA:GO_Central.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd07212; Pat_PNPLA9; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR047148; PLPL9.
DR InterPro; IPR002641; PNPLA_dom.
DR PANTHER; PTHR24139:SF34; 85_88 KDA CALCIUM-INDEPENDENT PHOSPHOLIPASE A2; 1.
DR PANTHER; PTHR24139; CALCIUM-INDEPENDENT PHOSPHOLIPASE A2; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF01734; Patatin; 1.
DR SMART; SM00248; ANK; 6.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS51635; PNPLA; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000008549};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REPEAT 340..372
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 546..578
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 716..913
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 33..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1062 AA; 119399 MW; D2077861F1A88865 CRC64;
MAFTGLNWDH VKTTFWEANK MLDSMVTMIA RSSGSRESSA ESRSSGSSSD GALVAGPNGK
LVMLKRKSTD EDEEDGAAMS KKPCLESDSA SESSEAEDAK GSIRFLSSLT NVIMRPAQKA
TSTYSGADEW VPKEMEEIAE FPLESIDKYK KVHPNAEAPK KFMLVNGEFA VVASLEKLTE
EQALRAQENS PHQHKHHDSR EERLTKNELT DNEDQKKKKE RDFRAKEEEE AKKGEKVLYH
LAITLFNENK EKYVMSLFRS HKLADVVALC ERCRENPELF RVFPKNVNIK EYLHLIFMEL
RDNMTWKSVH ISSKIGLLEF FENMRSHKLQ KYLNLIVQPE GLSPLMIAIQ NDQQETVRWM
VEHGADLNTI TSDGQNVLHM AATISNGEIL KFLWDTNKCE AMINKTDVNG STPAYSAFSS
ACITNWQMLR GHGGALQSTE STTNATPFIG AMKRGKLDEA SLKKMLEQKA DGLQEVESTT
GNSVIHFASN KKCLILLMEK FRDQTDPEAR NKFQQTPLHT FVINGELGLV MTLCAYGVEK
DAQDVNGNTP LHCAVTRGFT EIARMLLCLG AKPDLKNRYK ESPRHLAARL TDKEAKMDIV
RALIICGAPA CDDGFVGCAF GCMHNRGLTS CKTQLGSSSS DEQSMEERVK DIHVSENAAS
APYEFVLDPD TQLVEEAYAE RSETRAYPHE MALERVKNKL KDLIEKKKTS NVINVLGLDG
GGIRGLVTVQ MLICLESYLD RPLIDYFDWI GATSTGCYIM STLMTGGSLR HAQQYYLMFK
DQLFDSWTRP YDTKTLETFI KRSFGADRLM GDIKYPRFFC TTVRADTFPV QLDLARNYRL
PISDKENKDL GFTDPMGTID STSSELLNCV YFSELSMWRA VRRSSAAPTY FSASEGKFID
GGMISNNPVL DLMSEICFWN TTCQKQQLID KIVDVGCVLS VGTGITPICP VDPSVFEMND
WLGMLRGIKN LSLVVIDQAT ATEGAPITRS RSWCHSLGIP YYRLNAPIFK DVILDTNDDY
DLAKIMWDSV VYSHTHKKDF QELAELLKTV GTVDERKELL KI
//
