ID   PAFA2_BOVIN             Reviewed;         392 AA.
AC   P79106; Q5E9S1;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   24-JAN-2024, entry version 141.
DE   RecName: Full=Platelet-activating factor acetylhydrolase 2, cytoplasmic {ECO:0000303|PubMed:8955149};
DE            EC=3.1.1.47 {ECO:0000269|PubMed:7673213, ECO:0000269|PubMed:8955149, ECO:0000269|PubMed:9405438};
DE   AltName: Full=PAF acetylhydrolase II {ECO:0000303|PubMed:7673213};
DE   AltName: Full=PAF:lysophospholipid transacetylase {ECO:0000250|UniProtKB:P83006};
DE   AltName: Full=PAF:sphingosine transacetylase {ECO:0000250|UniProtKB:P83006};
DE   AltName: Full=Platelet-activating factor acetyltransferase PAFAH2 {ECO:0000250|UniProtKB:P83006};
DE            EC=2.3.1.149 {ECO:0000250|UniProtKB:P83006};
DE   AltName: Full=Serine-dependent phospholipase A2 {ECO:0000250|UniProtKB:Q99487};
DE            Short=SD-PLA2 {ECO:0000305};
GN   Name=PAFAH2 {ECO:0000250|UniProtKB:Q99487};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC
RP   ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Kidney;
RX   PubMed=8955149; DOI=10.1074/jbc.271.51.33032;
RA   Hattori K., Adachi H., Matsuzawa A., Yamamoto K., Tsujimoto M., Aoki J.,
RA   Hattori M., Arai H., Inoue K.;
RT   "cDNA cloning and expression of intracellular platelet-activating factor
RT   (PAF) acetylhydrolase II. Its homology with plasma PAF acetylhydrolase.";
RL   J. Biol. Chem. 271:33032-33038(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PROTEIN SEQUENCE OF 163-173, CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR
RP   LOCATION, AND ACTIVE SITE.
RX   PubMed=7673213; DOI=10.1074/jbc.270.38.22308;
RA   Hattori K., Hattori M., Adachi H., Tsujimoto M., Arai H., Inoue K.;
RT   "Purification and characterization of platelet-activating factor
RT   acetylhydrolase II from bovine liver cytosol.";
RL   J. Biol. Chem. 270:22308-22313(1995).
RN   [5]
RP   REVIEW.
RX   PubMed=9218411; DOI=10.1074/jbc.272.29.17895;
RA   Stafforini D.M., McIntyre T.M., Zimmerman G.A., Prescott S.M.;
RT   "Platelet-activating factor acetylhydrolases.";
RL   J. Biol. Chem. 272:17895-17898(1997).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MYRISTOYLATION AT
RP   GLY-2, ACTIVE SITE, AND MUTAGENESIS OF SER-236.
RX   PubMed=9405438; DOI=10.1074/jbc.272.51.32315;
RA   Matsuzawa A., Hattori K., Aoki J., Arai H., Inoue K.;
RT   "Protection against oxidative stress-induced cell death by intracellular
RT   platelet-activating factor-acetylhydrolase II.";
RL   J. Biol. Chem. 272:32315-32320(1997).
CC   -!- FUNCTION: Catalyzes the hydrolyze of the acetyl group at the sn-2
CC       position of platelet-activating factor (PAF) and its analogs, leading
CC       to their inactivation (PubMed:7673213, PubMed:8955149, PubMed:9405438).
CC       Hydrolyzes propionyl and butyroyl moieties approximately half as
CC       effectively as PAF (PubMed:7673213). Also catalyzes transacetylation of
CC       the acetyl group from platelet-activating factor (PAF) to
CC       lysoplasmalogen and to sphingosine, producing plasmalogen analogs of
CC       PAF and N-acetylsphingosine (C2-ceramide) respectively. Has a marked
CC       selectivity for phospholipids with short acyl chains at the sn-2
CC       position (By similarity). {ECO:0000250|UniProtKB:P83006,
CC       ECO:0000269|PubMed:7673213, ECO:0000269|PubMed:8955149,
CC       ECO:0000269|PubMed:9405438}.
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         Evidence={ECO:0000269|PubMed:7673213, ECO:0000269|PubMed:8955149,
CC         ECO:0000269|PubMed:9405438};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17778;
CC         Evidence={ECO:0000305|PubMed:7673213};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-
CC         O-hexadecyl-sn-glycero-3-phosphocholine + acetate + H(+);
CC         Xref=Rhea:RHEA:40479, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30089, ChEBI:CHEBI:44811, ChEBI:CHEBI:64496;
CC         Evidence={ECO:0000269|PubMed:7673213};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40480;
CC         Evidence={ECO:0000305|PubMed:7673213};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-O-hexadecyl-2-glutaryl-sn-glycero-3-phosphocholine + H2O =
CC         1-O-hexadecyl-sn-glycero-3-phosphocholine + glutarate + H(+);
CC         Xref=Rhea:RHEA:41700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30921, ChEBI:CHEBI:64496, ChEBI:CHEBI:78371;
CC         Evidence={ECO:0000269|PubMed:7673213};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41701;
CC         Evidence={ECO:0000305|PubMed:7673213};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-O-hexadecyl-2-succinyl-sn-glycero-3-phosphocholine + H2O =
CC         1-O-hexadecyl-sn-glycero-3-phosphocholine + H(+) + succinate;
CC         Xref=Rhea:RHEA:41696, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:64496, ChEBI:CHEBI:78369;
CC         Evidence={ECO:0000269|PubMed:7673213};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41697;
CC         Evidence={ECO:0000305|PubMed:7673213};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-O-hexadecyl-2-butanoyl-sn-glycero-3-phosphocholine + H2O =
CC         1-O-hexadecyl-sn-glycero-3-phosphocholine + butanoate + H(+);
CC         Xref=Rhea:RHEA:41692, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17968, ChEBI:CHEBI:64496, ChEBI:CHEBI:78368;
CC         Evidence={ECO:0000269|PubMed:7673213};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41693;
CC         Evidence={ECO:0000305|PubMed:7673213};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-O-hexadecyl-2-propanoyl-sn-glycero-3-phosphocholine + H2O =
CC         1-O-hexadecyl-sn-glycero-3-phosphocholine + H(+) + propanoate;
CC         Xref=Rhea:RHEA:41688, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17272, ChEBI:CHEBI:64496, ChEBI:CHEBI:78367;
CC         Evidence={ECO:0000269|PubMed:7673213};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41689;
CC         Evidence={ECO:0000305|PubMed:7673213};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-O-(1Z-alkenyl)-sn-glycero-3-phosphoethanolamine + 1-O-
CC         hexadecyl-2-acetyl-sn-glycero-3-phosphocholine = 1-O-(1Z-alkenyl)-2-
CC         acetyl-sn-glycero-3-phosphoethanolamine + 1-O-hexadecyl-sn-glycero-3-
CC         phosphocholine; Xref=Rhea:RHEA:41396, ChEBI:CHEBI:44811,
CC         ChEBI:CHEBI:64496, ChEBI:CHEBI:77288, ChEBI:CHEBI:78419;
CC         Evidence={ECO:0000250|UniProtKB:P83006};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41397;
CC         Evidence={ECO:0000250|UniProtKB:P83006};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + sphing-4-
CC         enine = 1-O-hexadecyl-sn-glycero-3-phosphocholine + H(+) + N-
CC         (acetyl)-sphing-4-enine; Xref=Rhea:RHEA:41408, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:44811, ChEBI:CHEBI:46979, ChEBI:CHEBI:57756,
CC         ChEBI:CHEBI:64496; Evidence={ECO:0000250|UniProtKB:P83006};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41409;
CC         Evidence={ECO:0000250|UniProtKB:P83006};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + a 1-
CC         organyl-2-lyso-sn-glycero-3-phospholipid = 1-O-alkyl-sn-glycero-3-
CC         phosphocholine + a 1-organyl-2-acetyl-sn-glycero-3-phospholipid;
CC         Xref=Rhea:RHEA:11048, ChEBI:CHEBI:685, ChEBI:CHEBI:30909,
CC         ChEBI:CHEBI:36707, ChEBI:CHEBI:76590; EC=2.3.1.149;
CC         Evidence={ECO:0000250|UniProtKB:P83006};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11049;
CC         Evidence={ECO:0000250|UniProtKB:P83006};
CC   -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:8955149}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7673213,
CC       ECO:0000269|PubMed:8955149, ECO:0000269|PubMed:9405438}. Membrane
CC       {ECO:0000269|PubMed:8955149, ECO:0000269|PubMed:9405438}; Lipid-anchor
CC       {ECO:0000269|PubMed:9405438}. Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:9405438}; Lipid-anchor
CC       {ECO:0000269|PubMed:9405438}. Note=In resting cells, localizes to
CC       intracellular membranes and cytoplasm. Translocates from the cytoplasm
CC       to intracellular membranes upon oxidative stress.
CC       {ECO:0000269|PubMed:9405438}.
CC   -!- TISSUE SPECIFICITY: Expressed at highest levels in liver and at lower
CC       levels in other tissues. {ECO:0000269|PubMed:8955149}.
CC   -!- SIMILARITY: Belongs to the serine esterase family. {ECO:0000305}.
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DR   EMBL; D87559; BAA13419.1; -; mRNA.
DR   EMBL; BT020849; AAX08866.1; -; mRNA.
DR   EMBL; BC105148; AAI05149.1; -; mRNA.
DR   RefSeq; NP_776995.1; NM_174570.2.
DR   RefSeq; XP_015315520.1; XM_015460034.1.
DR   AlphaFoldDB; P79106; -.
DR   SMR; P79106; -.
DR   STRING; 9913.ENSBTAP00000006727; -.
DR   SwissLipids; SLP:000000690; -.
DR   ESTHER; bovin-paf2; PAF-Acetylhydrolase.
DR   iPTMnet; P79106; -.
DR   PaxDb; 9913-ENSBTAP00000006727; -.
DR   PeptideAtlas; P79106; -.
DR   DNASU; 282299; -.
DR   Ensembl; ENSBTAT00000006727.6; ENSBTAP00000006727.5; ENSBTAG00000005105.6.
DR   GeneID; 282299; -.
DR   KEGG; bta:282299; -.
DR   CTD; 5051; -.
DR   VEuPathDB; HostDB:ENSBTAG00000005105; -.
DR   VGNC; VGNC:32552; PAFAH2.
DR   eggNOG; KOG3847; Eukaryota.
DR   GeneTree; ENSGT00390000005233; -.
DR   HOGENOM; CLU_022501_0_0_1; -.
DR   InParanoid; P79106; -.
DR   OMA; MGVNQSM; -.
DR   OrthoDB; 3079661at2759; -.
DR   TreeFam; TF313831; -.
DR   Reactome; R-BTA-418346; Platelet homeostasis.
DR   Proteomes; UP000009136; Chromosome 2.
DR   Bgee; ENSBTAG00000005105; Expressed in rumen papilla and 103 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:WormBase.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:WormBase.
DR   GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; IDA:UniProtKB.
DR   GO; GO:0047179; F:platelet-activating factor acetyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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:SF6; PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE 2, CYTOPLASMIC; 1.
DR   Pfam; PF03403; PAF-AH_p_II; 1.
DR   PIRSF; PIRSF018169; PAF_acetylhydrolase; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS00120; LIPASE_SER; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Endoplasmic reticulum; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Lipoprotein; Membrane; Myristate;
KW   Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000305|PubMed:9405438"
FT   CHAIN           2..392
FT                   /note="Platelet-activating factor acetylhydrolase 2,
FT                   cytoplasmic"
FT                   /id="PRO_0000090382"
FT   ACT_SITE        236
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000305|PubMed:7673213,
FT                   ECO:0000305|PubMed:9405438"
FT   ACT_SITE        259
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   ACT_SITE        314
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000305|PubMed:9405438"
FT   MUTAGEN         236
FT                   /note="S->C: Loss of catalytic activity. Loss of protection
FT                   against reactive oxygen species (ROS)-induced apoptosis. No
FT                   defect in ROS-induced membrane translocation."
FT                   /evidence="ECO:0000269|PubMed:9405438"
SQ   SEQUENCE   392 AA;  43865 MW;  1DEACA2ADFA4CEA8 CRC64;
     MGVNQSVSFP PVTGPHLVGC GDVMEGQSLQ GSFFRLFYPC QEAEETSEQP LWIPRYEYCA
     GLAEYLKFNK RWGGLLFNLG VGSCRLPVSW NGPFKTKDSG YPLIIFSHGM GAFRTVYSAF
     CMELASRGFV VAVPEHRDGS AAATCFCKQT PEENQPDNEA LKEEWIPHRQ IEEGEKEFYV
     RNYQVHQRVS ECVRVLKILQ EVTAGQAVLN ILPGGLDLMT LKGGIDVSRV AVMGHSFGGA
     TAILALAKEM QFRCAVALDA WMFPLEHDFY PTARGPIFFI NAEKFQTVET VNLMKKICDQ
     HHQSRIITVL GSVHRSLTDF VFVAGNWISK FFSSHTRGSL DPYEGQETVV RAMLAFLQKH
     LDLKEDYDQW NNFIEGIGPS LTPGAPHHLS SL
//