PLA1_CAEEL
ID PLA1_CAEEL Reviewed; 840 AA.
AC G5EEM9; A0A0K3AU10; G4SGS5; G4SGU1; G5EE61; G8JYA8; Q21478; Q8WQE0;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Intracellular phospholipase A1 {ECO:0000303|PubMed:18497747};
DE Short=IPLA-1 {ECO:0000303|PubMed:20668164};
DE Short=PLA(1) {ECO:0000303|PubMed:18497747};
DE EC=3.1.1.111 {ECO:0000269|PubMed:20668164};
DE EC=3.1.1.4 {ECO:0000269|PubMed:23007400};
GN Name=ipla-1 {ECO:0000312|EMBL:ABW23572.1, ECO:0000312|WormBase:M03A1.6e};
GN ORFNames=M03A1.6 {ECO:0000312|WormBase:M03A1.6e};
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 [MRNA], AND FUNCTION.
RX PubMed=18497747; DOI=10.1038/emboj.2008.102;
RA Kanamori T., Inoue T., Sakamoto T., Gengyo-Ando K., Tsujimoto M.,
RA Mitani S., Sawa H., Aoki J., Arai H.;
RT "Beta-catenin asymmetry is regulated by PLA1 and retrograde traffic in C.
RT elegans stem cell divisions.";
RL EMBO J. 27:1647-1657(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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 [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20668164; DOI=10.1091/mbc.e10-03-0195;
RA Imae R., Inoue T., Kimura M., Kanamori T., Tomioka N.H., Kage-Nakadai E.,
RA Mitani S., Arai H.;
RT "Intracellular phospholipase A1 and acyltransferase, which are involved in
RT Caenorhabditis elegans stem cell divisions, determine the sn-1 fatty acyl
RT chain of phosphatidylinositol.";
RL Mol. Biol. Cell 21:3114-3124(2010).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
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: Hydrolyzes the ester bond at the sn-1 position of
CC glycerophospholipids and produces 2-acyl lysophospholipids, being
CC phosphatidylinositol (PI) its major substrate. PI is a versatile lipid
CC that not only serves as a structural component of cellular membranes,
CC but also plays important roles in signal transduction through distinct
CC phosphorylated derivatives of the inositol head group
CC (PubMed:20668164). Catalyzes the hydrolysis of phosphatidylcholine at
CC sn-2 position in vitro (PubMed:23007400). Regulates asymmetric
CC division, an important property of stem cells in C.elegans, by
CC controlling the subcellular localizations of beta-catenin
CC (PubMed:18497747, PubMed:20668164). {ECO:0000269|PubMed:18497747,
CC ECO:0000269|PubMed:20668164, ECO:0000269|PubMed:23007400}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol) +
CC H2O = 2-hexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol) + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:66708, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72835,
CC ChEBI:CHEBI:167448; Evidence={ECO:0000305|PubMed:20668164};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66709;
CC Evidence={ECO:0000305|PubMed:20668164};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H2O = a 2-acyl-
CC sn-glycero-3-phospho-L-serine + a fatty acid + H(+);
CC Xref=Rhea:RHEA:42212, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:57262, ChEBI:CHEBI:65214;
CC EC=3.1.1.111; Evidence={ECO:0000269|PubMed:20668164};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42213;
CC Evidence={ECO:0000305|PubMed:20668164};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-
CC serine + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine +
CC H(+) + hexadecanoate; Xref=Rhea:RHEA:43968, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:75029,
CC ChEBI:CHEBI:77342; Evidence={ECO:0000269|PubMed:20668164};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43969;
CC Evidence={ECO:0000305|PubMed:20668164};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O =
CC (9Z)-octadecenoate + (9Z-octadecenoyl)-sn-glycero-3-phosphocholine +
CC H(+); Xref=Rhea:RHEA:38699, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:74669, ChEBI:CHEBI:76083;
CC Evidence={ECO:0000269|PubMed:20668164};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38700;
CC Evidence={ECO:0000305|PubMed:20668164};
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:0000269|PubMed:23007400};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000305|PubMed:23007400};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000269|PubMed:23007400};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC Evidence={ECO:0000305|PubMed:23007400};
CC -!- ACTIVITY REGULATION: Inhibited by E-6-bromomethylene-3-1-naphthalenyl-
CC 2H-tetrahydropyran-2-one (BEL) in vitro. {ECO:0000269|PubMed:23007400}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=e;
CC IsoId=G5EEM9-1; Sequence=Displayed;
CC Name=c;
CC IsoId=G5EEM9-2; Sequence=VSP_061036;
CC Name=d;
CC IsoId=G5EEM9-3; Sequence=VSP_061035;
CC Name=b;
CC IsoId=G5EEM9-4; Sequence=VSP_061034;
CC Name=a;
CC IsoId=G5EEM9-5; Sequence=VSP_061033;
CC Name=f;
CC IsoId=G5EEM9-6; Sequence=VSP_061032;
CC -!- SIMILARITY: Belongs to the PA-PLA1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EU180219; ABW23572.1; -; mRNA.
DR EMBL; BX284602; CCD70559.1; -; Genomic_DNA.
DR EMBL; BX284602; CCD70557.1; -; Genomic_DNA.
DR EMBL; BX284602; CCD70558.1; -; Genomic_DNA.
DR EMBL; BX284602; CCD70553.1; -; Genomic_DNA.
DR EMBL; BX284602; CCD70552.1; -; Genomic_DNA.
DR EMBL; BX284602; CTQ86513.1; -; Genomic_DNA.
DR PIR; T29582; T29582.
DR RefSeq; NP_001040793.1; NM_001047328.3. [G5EEM9-2]
DR RefSeq; NP_001040794.1; NM_001047329.2. [G5EEM9-3]
DR RefSeq; NP_001122623.1; NM_001129151.2.
DR RefSeq; NP_001300574.1; NM_001313645.1. [G5EEM9-6]
DR RefSeq; NP_740975.1; NM_170978.5.
DR RefSeq; NP_740976.1; NM_170979.3. [G5EEM9-5]
DR AlphaFoldDB; G5EEM9; -.
DR STRING; 6239.M03A1.6e; -.
DR SwissLipids; SLP:000001014; -.
DR EPD; G5EEM9; -.
DR PaxDb; G5EEM9; -.
DR PeptideAtlas; G5EEM9; -.
DR EnsemblMetazoa; M03A1.6a.1; M03A1.6a.1; WBGene00019747. [G5EEM9-5]
DR EnsemblMetazoa; M03A1.6b.1; M03A1.6b.1; WBGene00019747. [G5EEM9-4]
DR EnsemblMetazoa; M03A1.6b.2; M03A1.6b.2; WBGene00019747. [G5EEM9-4]
DR EnsemblMetazoa; M03A1.6b.3; M03A1.6b.3; WBGene00019747. [G5EEM9-4]
DR EnsemblMetazoa; M03A1.6b.4; M03A1.6b.4; WBGene00019747. [G5EEM9-4]
DR EnsemblMetazoa; M03A1.6c.1; M03A1.6c.1; WBGene00019747. [G5EEM9-2]
DR EnsemblMetazoa; M03A1.6d.1; M03A1.6d.1; WBGene00019747. [G5EEM9-3]
DR EnsemblMetazoa; M03A1.6e.1; M03A1.6e.1; WBGene00019747. [G5EEM9-1]
DR EnsemblMetazoa; M03A1.6f.1; M03A1.6f.1; WBGene00019747. [G5EEM9-6]
DR GeneID; 173795; -.
DR UCSC; M03A1.6c; c. elegans.
DR CTD; 173795; -.
DR WormBase; M03A1.6a; CE07393; WBGene00019747; ipla-1.
DR WormBase; M03A1.6b; CE29816; WBGene00019747; ipla-1.
DR WormBase; M03A1.6c; CE40099; WBGene00019747; ipla-1.
DR WormBase; M03A1.6d; CE40100; WBGene00019747; ipla-1.
DR WormBase; M03A1.6e; CE41917; WBGene00019747; ipla-1.
DR WormBase; M03A1.6f; CE50406; WBGene00019747; ipla-1.
DR eggNOG; KOG2308; Eukaryota.
DR GeneTree; ENSGT00940000156065; -.
DR HOGENOM; CLU_006932_2_0_1; -.
DR InParanoid; G5EEM9; -.
DR OMA; WQNENIV; -.
DR OrthoDB; 777968at2759; -.
DR PhylomeDB; G5EEM9; -.
DR Reactome; R-CEL-1483226; Synthesis of PI.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00019747; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; G5EEM9; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:WormBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:1903293; C:phosphatase complex; IPI:WormBase.
DR GO; GO:0047499; F:calcium-independent phospholipase A2 activity; IDA:WormBase.
DR GO; GO:0042802; F:identical protein binding; IPI:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0070300; F:phosphatidic acid binding; IDA:WormBase.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:WormBase.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:WormBase.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:WormBase.
DR GO; GO:0008970; F:phospholipase A1 activity; IDA:WormBase.
DR GO; GO:0004620; F:phospholipase activity; IBA:GO_Central.
DR GO; GO:0034638; P:phosphatidylcholine catabolic process; IDA:WormBase.
DR GO; GO:0031161; P:phosphatidylinositol catabolic process; ISS:WormBase.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IDA:WormBase.
DR GO; GO:0009786; P:regulation of asymmetric cell division; IMP:WormBase.
DR GO; GO:0032880; P:regulation of protein localization; IMP:WormBase.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR004177; DDHD_dom.
DR Pfam; PF02862; DDHD; 1.
DR SMART; SM01127; DDHD; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS51043; DDHD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Lipid metabolism; Phospholipid metabolism;
KW Reference proteome.
FT CHAIN 1..840
FT /note="Intracellular phospholipase A1"
FT /id="PRO_0000452653"
FT DOMAIN 564..827
FT /note="DDHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00378"
FT REGION 1..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..694
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..172
FT /note="Missing (in isoform f)"
FT /id="VSP_061032"
FT VAR_SEQ 1..141
FT /note="MSGSEEEHLVSLTFRKNEEDMDEDEGKVKQKEKPKEKQMEFVNQNFVESTED
FT ESEVSTPTAVGLPIGTSTPDGDETPTQPDPNGKYTMAQTKDADLSRPSGLPSNGNPGSS
FT TTVPPASKSGPVAPPRPSGTPVAPQRNRRR -> MEKSPPTSPTPIPSIDSNFMISPKK
FT SRSKSVPNARKILNDLVETTERNLEAPYRSIMWQKYIFDRP (in isoform a)"
FT /id="VSP_061033"
FT VAR_SEQ 1..87
FT /note="Missing (in isoform b)"
FT /id="VSP_061034"
FT VAR_SEQ 1..78
FT /note="MSGSEEEHLVSLTFRKNEEDMDEDEGKVKQKEKPKEKQMEFVNQNFVESTED
FT ESEVSTPTAVGLPIGTSTPDGDETPT -> MNIMFPEISAFSHYL (in isoform
FT d)"
FT /id="VSP_061035"
FT VAR_SEQ 1..77
FT /note="MSGSEEEHLVSLTFRKNEEDMDEDEGKVKQKEKPKEKQMEFVNQNFVESTED
FT ESEVSTPTAVGLPIGTSTPDGDETP -> MVLGKKKVSRATKSDD (in isoform
FT c)"
FT /id="VSP_061036"
SQ SEQUENCE 840 AA; 94811 MW; 955587D1ED425C6F CRC64;
MSGSEEEHLV SLTFRKNEED MDEDEGKVKQ KEKPKEKQME FVNQNFVEST EDESEVSTPT
AVGLPIGTST PDGDETPTQP DPNGKYTMAQ TKDADLSRPS GLPSNGNPGS STTVPPASKS
GPVAPPRPSG TPVAPQRNRR RKVTELKCSE VRWFFQEPKG TLWNPFNGRD SIMLEIKYRK
EKGIELDEAM QEIYDESLTH YKMEMKDEPE IENGNIGMEQ EKPMVVVMNG QYKVNKDNSK
IDPIYWKDDS KEIRRGSWFS PDYQPLEMPL SDQIEKNHLQ CFRNQMIPEG TTVFSKSETS
NKPVLAELHV DGYDIRWSSV IDISLHQKGN AILRYLWAKS TPLRRGYEKE ADWNDAAAEI
SHLILVVHGI GQKGYENLIA QNANQVRDGV VSAMEKVYPE EKSRPMFLPV EWRSALKLDN
GLTDNITIPK MSSMRASLNS TAMDVMYYQS PLFRTEIVRG VVSQLNRTYK LFKANNPQFN
GHVSVFGHSL GSVICYDVLT QYSPLMLFDK YVTKSIDEYL KRDDTNASEE ARKALEAMKL
AREQLRDNLE GGIHKLLVTK EEQLEFKVKY LFAVGSPLGV FLTMRGGEST DLLSKATNVE
RVFNIFHPYD PVAYRLEPFF APEYRHIRPI KLFSNTDLRA RASYENLPLD VYKHYLKKLK
NLNKAKKNKD DKTADARSGG DDENEDEDEC DSDEDARSGC SSPRSMTPPP FETAAANAAA
AAKETKAVKK GWFSFGTSSN PKKTQSTASL GSVNATSTEN IEFAKEAAEE LPLAEKILGS
GVRVPHRIDF QLQPALTEKS YWSVLKSHFA YWTNADLALF LANVLYCKPL KPEEAKPTWA
