ID   PAFA_CAEEL              Reviewed;         388 AA.
AC   Q22943;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2002, sequence version 2.
DT   27-MAR-2024, entry version 142.
DE   RecName: Full=Platelet-activating factor acetylhydrolase homolog 2;
DE            EC=3.1.1.47;
GN   Name=paf-2; ORFNames=C52B9.7;
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] (ISOFORM A).
RA   Inoue T., Suzuki Y., Aoki J., Sugimoto A., Yamamoto M., Tsujimoto M.,
RA   Inoue K., Arai H.;
RT   "A short-chain acyl hydrolase is required for early epithelial
RT   morphogenesis in Caenorhabditis elegans.";
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-
CC         alkyl-sn-glycero-3-phosphocholine + acetate + H(+);
CC         Xref=Rhea:RHEA:17777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30089, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707; EC=3.1.1.47;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=a;
CC         IsoId=Q22943-1; Sequence=Displayed;
CC       Name=b;
CC         IsoId=Q22943-2; Sequence=VSP_003132, VSP_003133;
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   EMBL; AF386745; AAL57290.1; -; mRNA.
DR   EMBL; FO080644; CCD65415.1; -; Genomic_DNA.
DR   EMBL; FO080644; CCD65416.1; -; Genomic_DNA.
DR   RefSeq; NP_741768.1; NM_171668.6. [Q22943-1]
DR   RefSeq; NP_741769.1; NM_171669.3.
DR   AlphaFoldDB; Q22943; -.
DR   SMR; Q22943; -.
DR   STRING; 6239.C52B9.7a.1; -.
DR   ESTHER; caeel-pafa; PAF-Acetylhydrolase.
DR   EPD; Q22943; -.
DR   PaxDb; 6239-C52B9-7a; -.
DR   PeptideAtlas; Q22943; -.
DR   EnsemblMetazoa; C52B9.7a.1; C52B9.7a.1; WBGene00003907. [Q22943-1]
DR   EnsemblMetazoa; C52B9.7a.2; C52B9.7a.2; WBGene00003907. [Q22943-1]
DR   EnsemblMetazoa; C52B9.7b.1; C52B9.7b.1; WBGene00003907. [Q22943-2]
DR   GeneID; 180704; -.
DR   KEGG; cel:CELE_C52B9.7; -.
DR   UCSC; C52B9.7a; c. elegans. [Q22943-1]
DR   AGR; WB:WBGene00003907; -.
DR   WormBase; C52B9.7a; CE30264; WBGene00003907; paf-2. [Q22943-1]
DR   WormBase; C52B9.7b; CE30265; WBGene00003907; paf-2. [Q22943-2]
DR   eggNOG; KOG3847; Eukaryota.
DR   GeneTree; ENSGT00390000005233; -.
DR   HOGENOM; CLU_022501_0_0_1; -.
DR   InParanoid; Q22943; -.
DR   OMA; DKWPIVV; -.
DR   OrthoDB; 3079661at2759; -.
DR   PhylomeDB; Q22943; -.
DR   BRENDA; 3.1.1.47; 1045.
DR   Reactome; R-CEL-418346; Platelet homeostasis.
DR   PRO; PR:Q22943; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00003907; Expressed in material anatomical entity and 5 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; ISS:WormBase.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:WormBase.
DR   GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; IDA:WormBase.
DR   GO; GO:0016042; P:lipid catabolic process; IDA:WormBase.
DR   GO; GO:0016331; P:morphogenesis of embryonic epithelium; IMP:WormBase.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR016715; PAF_acetylhydro_eukaryote.
DR   PANTHER; PTHR10272; PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE; 1.
DR   PANTHER; PTHR10272:SF0; PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE; 1.
DR   Pfam; PF03403; PAF-AH_p_II; 1.
DR   PIRSF; PIRSF018169; PAF_acetylhydrolase; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Reference proteome.
FT   CHAIN           1..388
FT                   /note="Platelet-activating factor acetylhydrolase homolog
FT                   2"
FT                   /id="PRO_0000090381"
FT   ACT_SITE        238
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        261
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        316
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         187..190
FT                   /note="GKRV -> SVKV (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_003132"
FT   VAR_SEQ         191..388
FT                   /note="Missing (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_003133"
SQ   SEQUENCE   388 AA;  43418 MW;  98B71A8ADA43E701 CRC64;
     MGSYISSPQV LTRQVSGQFQ VGCKDLMIDG TVLGDRGLFM RLYFPTDSQA ADISSYPLWL
     PKPQYAHGLG EYLGQSSQKM NVITSTVVGE KREDCIENAQ MSTKCDKWPI VVFSHGLGGS
     RTFYSTYCTS LASHGYVVAA VEHKDHSACW TYQLTEKNGE LVEQPIKIKL IEKNEKNEFK
     IRNQQVGKRV TECVKALNVL EQLNLGTVPE KVLIGNDYNW AQFKNKLVMS SASVIGHSFG
     GATSLASSAY TTDFQKAIVF DGWMYPLDST QQEQAKQPTL FLNVGDWQWN ENLDVMKKII
     SHNDGNLALT LNGAVHQCFS DFPFIFPSWL AKKFGVQGRT EPSLCMQAAI ELSLAFLENG
     KDGAQKLKDE KFSSFISNEI YGREKYKL
//