ID G1T3V9_RABIT Unreviewed; 449 AA.
AC G1T3V9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 2.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Platelet-activating factor acetylhydrolase {ECO:0000256|PIRNR:PIRNR018169};
DE EC=3.1.1.47 {ECO:0000256|PIRNR:PIRNR018169};
GN Name=PAFAH2 {ECO:0000313|Ensembl:ENSOCUP00000010926.3};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000010926.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000010926.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000010926.3,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000010926.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000010926.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00023721};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40480;
CC Evidence={ECO:0000256|ARBA:ARBA00023721};
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:0000256|ARBA:ARBA00023737};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17778;
CC Evidence={ECO:0000256|ARBA:ARBA00023737};
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DR EMBL; AAGW02062869; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02062870; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02062871; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_002716152.2; XM_002716106.3.
DR AlphaFoldDB; G1T3V9; -.
DR SMR; G1T3V9; -.
DR STRING; 9986.ENSOCUP00000010926; -.
DR PaxDb; 9986-ENSOCUP00000010926; -.
DR Ensembl; ENSOCUT00000012694.4; ENSOCUP00000010926.3; ENSOCUG00000012696.4.
DR GeneID; 100338757; -.
DR KEGG; ocu:100338757; -.
DR CTD; 5051; -.
DR eggNOG; KOG3847; Eukaryota.
DR GeneTree; ENSGT00390000005233; -.
DR HOGENOM; CLU_022501_0_0_1; -.
DR InParanoid; G1T3V9; -.
DR OMA; MGVNQSM; -.
DR OrthoDB; 3079661at2759; -.
DR TreeFam; TF313831; -.
DR Proteomes; UP000001811; Chromosome 13.
DR Bgee; ENSOCUG00000012696; Expressed in blood and 16 other cell types or tissues.
DR GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; IEA:UniProtKB-UniRule.
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.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR018169};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR018169};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|PIRNR:PIRNR018169};
KW Reference proteome {ECO:0000313|Proteomes:UP000001811}.
FT ACT_SITE 293
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
FT ACT_SITE 316
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
FT ACT_SITE 371
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
SQ SEQUENCE 449 AA; 50476 MW; D7FF1C354832AC78 CRC64;
MLSSAHVDPE NYNYQRATGS WAVSPFRRVK RQGLLLRDHL DWPSAALPES LASSGDEMGA
SQSVCFPPVT GPHRVGCGDV MEGQGLQGSF FRIFYPCQEA EETPEQPLWI PRYEYYTGLA
DYLRFNKRWG GLLFNLAVGS YRLPVSWNGP FKTKDSGYPL IIFSHGLGGF RTLYSAFCME
LASHGFVVAL PEHRDQSAAT TYFCKQAPEE TQPTNKLLEE EWIPFRRIEE GEKEFHVRNP
QVHQRARECV RVLRILQEVA AGQPIDNILP GGLDLKTLRG SIDPSRVAVM GHSFGGATAI
LALAKETQFR CAVALDAWMF PLERDLYPQA RGPVFFINTE KFQTVESINL MKKICAQHEQ
SRIITVLGSV HHSQTDFAFV TGNLLVKYLS SHTRGSLDPY EGQETMVHAM LAFLQKHLDL
KEDYDQWNSL IEGIGPWLTP GAPTHLSSL
//
