ID PA1B2_HUMAN Reviewed; 229 AA. AC P68402; A8DPS5; A8DPS6; A8DPS7; E9PEJ5; E9PLP3; O00687; Q29459; Q6IBR6; DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 27-MAR-2024, entry version 182. DE RecName: Full=Platelet-activating factor acetylhydrolase IB subunit alpha2 {ECO:0000305}; DE EC=3.1.1.47 {ECO:0000250|UniProtKB:P68401}; DE AltName: Full=PAF acetylhydrolase 30 kDa subunit; DE Short=PAF-AH 30 kDa subunit; DE AltName: Full=PAF-AH subunit beta; DE Short=PAFAH subunit beta; GN Name=PAFAH1B2 {ECO:0000312|HGNC:HGNC:8575}; Synonyms=PAFAHB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Fetal liver; RX PubMed=9144386; DOI=10.1006/bbrc.1997.6383; RA Adachi H., Tsujimoto M., Hattori M., Arai H., Inoue K.; RT "Differential tissue distribution of the beta- and gamma-subunits of human RT cytosolic platelet-activating factor acetylhydrolase (isoform I)."; RL Biochem. Biophys. Res. Commun. 233:10-13(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), AND ALTERNATIVE RP SPLICING. RC TISSUE=Testis; RX PubMed=18155631; DOI=10.1016/j.prostaglandins.2007.10.005; RA Scott B.T., Olson N., Long G.L., Bovill E.G.; RT "Novel isoforms of intracellular platelet activating factor acetylhydrolase RT (PAFAH1b2) in human testis; encoded by alternatively spliced mRNAs."; RL Prostaglandins Other Lipid Mediat. 85:69-80(2008). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NHLBI resequencing and genotyping service (RS&G); RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP PROTEIN SEQUENCE OF 61-79, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, and Cajal-Retzius cell; RA Lubec G., Afjehi-Sadat L.; RL Submitted (MAR-2007) to UniProtKB. RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-64, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [15] {ECO:0007744|PDB:1VYH} RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) IN COMPLEX WITH PAFAH1B1, AND RP SUBUNIT. RX PubMed=15572112; DOI=10.1016/j.neuron.2004.11.019; RA Tarricone C., Perrina F., Monzani S., Massimiliano L., Kim M.-H., RA Derewenda Z.S., Knapp S., Tsai L.-H., Musacchio A.; RT "Coupling PAF signaling to dynein regulation: structure of LIS1 in complex RT with PAF-acetylhydrolase."; RL Neuron 44:809-821(2004). CC -!- FUNCTION: Alpha2 catalytic subunit of the cytosolic type I platelet- CC activating factor (PAF) acetylhydrolase (PAF-AH (I)) heterotetrameric CC enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 CC position of PAF and its analogs and modulates the action of PAF. The CC activity and substrate specificity of PAF-AH (I) are affected by its CC subunit composition. The alpha2/alpha2 homodimer (PAFAH1B2/PAFAH1B2 CC homodimer) hydrolyzes PAF and 1-O-alkyl-2-acetyl-sn-glycero-3- CC phosphorylethanolamine (AAGPE) more efficiently than 1-O-alkyl-2- CC acetyl-sn-glycero-3-phosphoric acid (AAGPA). In contrast, the CC alpha1/alpha2 heterodimer(PAFAH1B3/PAFAH1B3 heterodimer) hydrolyzes CC AAGPA more efficiently than PAF, but has little hydrolytic activity CC towards AAGPE (By similarity). May play a role in male germ cell CC meiosis during the late pachytenestage and meiotic divisions as well as CC early spermiogenesis (By similarity). {ECO:0000250|UniProtKB:P68401, CC ECO:0000250|UniProtKB:Q61206}. 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:0000250|UniProtKB:P68401}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17778; CC Evidence={ECO:0000250|UniProtKB:P68401}; 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:0000250|UniProtKB:P68401}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40480; CC Evidence={ECO:0000250|UniProtKB:P68401}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphate + H2O = 1-O- CC hexadecyl-sn-glycero-3-phosphate + acetate + H(+); CC Xref=Rhea:RHEA:41704, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30089, ChEBI:CHEBI:77580, ChEBI:CHEBI:78385; CC Evidence={ECO:0000250|UniProtKB:P68401}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41705; CC Evidence={ECO:0000250|UniProtKB:P68401}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphoethanolamine + H2O CC = 1-O-hexadecyl-sn-glycero-3-phosphoethanolamine + acetate + H(+); CC Xref=Rhea:RHEA:41708, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30089, ChEBI:CHEBI:78387, ChEBI:CHEBI:78390; CC Evidence={ECO:0000250|UniProtKB:P68401}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41709; CC Evidence={ECO:0000250|UniProtKB:P68401}; CC -!- ACTIVITY REGULATION: Beta subunit (PAFAH1B1) stimulates the CC acetylhydrolase activity of the alpha2/alpha2 catalytic homodimer. CC {ECO:0000250|UniProtKB:P68401}. CC -!- SUBUNIT: Forms a catalytic dimer which is either homodimer CC (alpha2/alpha2 homodimer) or heterodimer with PAFAH1B3 (alpha2/alpha1 CC heterodimer). Component of the cytosolic (PAF-AH (I)) heterotetrameric CC enzyme, which is composed of PAFAH1B1 (beta), PAFAH1B2 (alpha2) and CC PAFAH1B3 (alpha1) subunits. The catalytic activity of the enzyme CC resides in the alpha1 (PAFAH1B3) and alpha2 (PAFAH1B2) subunits, CC whereas the beta subunit (PAFAH1B1) has regulatory activity. Trimer CC formation is not essential for the catalytic activity (By similarity). CC Interacts (homodimer form) with PAFAH1B1 (homodimer form); PAFAH1B2 CC competes with NDEL1 for PAFAH1B1 binding (PubMed:15572112). Interacts CC with VLDLR; this interaction may modulate the Reelin pathway (By CC similarity). {ECO:0000250|UniProtKB:P68401, CC ECO:0000250|UniProtKB:Q61206, ECO:0000269|PubMed:15572112}. CC -!- INTERACTION: CC P68402; Q5SYC1: CLVS2; NbExp=3; IntAct=EBI-713724, EBI-12357161; CC P68402; Q15102: PAFAH1B3; NbExp=4; IntAct=EBI-713724, EBI-711522; CC P68402; O60260-5: PRKN; NbExp=3; IntAct=EBI-713724, EBI-21251460; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=P68402-1; Sequence=Displayed; CC Name=2; CC IsoId=P68402-2; Sequence=VSP_042896; CC Name=3; CC IsoId=P68402-3; Sequence=VSP_043217; CC Name=4; CC IsoId=P68402-4; Sequence=VSP_044680; CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9144386}. CC -!- MISCELLANEOUS: Originally the subunits of the type I platelet- CC activating factor (PAF) acetylhydrolase was named alpha (PAFAH1B1), CC beta (PAFAH1B2) and gamma (PAFAH1B3) (PubMed:9144386) (By similarity). CC Now these subunits have been renamed beta (PAFAH1B1), alpha2 (PAFAH1B2) CC and alpha1 (PAFAH1B3) respectively (By similarity). CC {ECO:0000250|UniProtKB:P43034, ECO:0000250|UniProtKB:Q15102, CC ECO:0000250|UniProtKB:Q29460, ECO:0000303|PubMed:9144386}. CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family. Platelet- CC activating factor acetylhydrolase IB beta/gamma subunits subfamily. CC {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; D63390; BAA19917.1; -; mRNA. DR EMBL; DQ836738; ABI58225.1; -; mRNA. DR EMBL; DQ836739; ABI58226.1; -; mRNA. DR EMBL; DQ836740; ABI58227.1; -; mRNA. DR EMBL; DQ836741; ABI58228.1; -; mRNA. DR EMBL; DQ836742; ABI58229.1; -; mRNA. DR EMBL; DQ836743; ABI58230.1; -; mRNA. DR EMBL; AK292973; BAF85662.1; -; mRNA. DR EMBL; CR456736; CAG33017.1; -; mRNA. DR EMBL; EF445007; ACA06040.1; -; Genomic_DNA. DR EMBL; AP005018; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471065; EAW67281.1; -; Genomic_DNA. DR EMBL; BC000398; AAH00398.1; -; mRNA. DR EMBL; BC019301; AAH19301.1; -; mRNA. DR CCDS; CCDS53713.1; -. [P68402-3] DR CCDS; CCDS53714.1; -. [P68402-4] DR CCDS; CCDS53715.1; -. [P68402-2] DR CCDS; CCDS8380.1; -. [P68402-1] DR PIR; JC5409; JC5409. DR RefSeq; NP_001171675.1; NM_001184746.1. [P68402-4] DR RefSeq; NP_001171676.1; NM_001184747.1. [P68402-2] DR RefSeq; NP_001171677.1; NM_001184748.1. [P68402-3] DR RefSeq; NP_001296360.1; NM_001309431.1. DR RefSeq; NP_002563.1; NM_002572.3. [P68402-1] DR PDB; 1VYH; X-ray; 3.40 A; A/B/E/F/I/J/M/N/Q/R=1-229. DR PDBsum; 1VYH; -. DR AlphaFoldDB; P68402; -. DR SMR; P68402; -. DR BioGRID; 111086; 69. DR IntAct; P68402; 23. DR STRING; 9606.ENSP00000435289; -. DR BindingDB; P68402; -. DR ChEMBL; CHEMBL4463; -. DR GlyGen; P68402; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P68402; -. DR PhosphoSitePlus; P68402; -. DR SwissPalm; P68402; -. DR BioMuta; PAFAH1B2; -. DR DMDM; 55977294; -. DR REPRODUCTION-2DPAGE; IPI00026546; -. DR EPD; P68402; -. DR jPOST; P68402; -. DR MassIVE; P68402; -. DR MaxQB; P68402; -. DR PaxDb; 9606-ENSP00000435289; -. DR PeptideAtlas; P68402; -. DR ProteomicsDB; 21857; -. DR ProteomicsDB; 57538; -. [P68402-1] DR ProteomicsDB; 57539; -. [P68402-2] DR ProteomicsDB; 57540; -. [P68402-3] DR Pumba; P68402; -. DR Antibodypedia; 32310; 280 antibodies from 27 providers. DR DNASU; 5049; -. DR Ensembl; ENST00000419197.6; ENSP00000388742.2; ENSG00000168092.14. [P68402-3] DR Ensembl; ENST00000527958.6; ENSP00000435289.1; ENSG00000168092.14. [P68402-1] DR Ensembl; ENST00000529887.6; ENSP00000434951.2; ENSG00000168092.14. [P68402-2] DR Ensembl; ENST00000530272.1; ENSP00000431365.1; ENSG00000168092.14. [P68402-4] DR GeneID; 5049; -. DR KEGG; hsa:5049; -. DR MANE-Select; ENST00000527958.6; ENSP00000435289.1; NM_002572.4; NP_002563.1. DR UCSC; uc009yzk.3; human. [P68402-1] DR AGR; HGNC:8575; -. DR CTD; 5049; -. DR DisGeNET; 5049; -. DR GeneCards; PAFAH1B2; -. DR HGNC; HGNC:8575; PAFAH1B2. DR HPA; ENSG00000168092; Low tissue specificity. DR MIM; 602508; gene. DR neXtProt; NX_P68402; -. DR OpenTargets; ENSG00000168092; -. DR PharmGKB; PA32906; -. DR VEuPathDB; HostDB:ENSG00000168092; -. DR eggNOG; KOG1388; Eukaryota. DR GeneTree; ENSGT00950000183199; -. DR HOGENOM; CLU_051989_2_0_1; -. DR InParanoid; P68402; -. DR OMA; QYEXVIV; -. DR OrthoDB; 4162633at2759; -. DR PhylomeDB; P68402; -. DR TreeFam; TF323955; -. DR BRENDA; 3.1.1.47; 2681. DR PathwayCommons; P68402; -. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-6811436; COPI-independent Golgi-to-ER retrograde traffic. DR SignaLink; P68402; -. DR SIGNOR; P68402; -. DR BioGRID-ORCS; 5049; 17 hits in 1161 CRISPR screens. DR ChiTaRS; PAFAH1B2; human. DR EvolutionaryTrace; P68402; -. DR GeneWiki; PAFAH1B2; -. DR GenomeRNAi; 5049; -. DR Pharos; P68402; Tchem. DR PRO; PR:P68402; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; P68402; Protein. DR Bgee; ENSG00000168092; Expressed in secondary oocyte and 192 other cell types or tissues. DR ExpressionAtlas; P68402; baseline and differential. DR GO; GO:0008247; C:1-alkyl-2-acetylglycerophosphocholine esterase complex; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0001650; C:fibrillar center; IDA:HPA. DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome. DR GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; ISS:UniProtKB. DR GO; GO:0047179; F:platelet-activating factor acetyltransferase activity; IBA:GO_Central. DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB. DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl. DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW. DR GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc. DR GO; GO:0016239; P:positive regulation of macroautophagy; IMP:BHF-UCL. DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB. DR CDD; cd01820; PAF_acetylesterase_like; 1. DR Gene3D; 3.40.50.1110; SGNH hydrolase; 1. DR InterPro; IPR013830; SGNH_hydro. DR InterPro; IPR036514; SGNH_hydro_sf. DR PANTHER; PTHR11852; PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE; 1. DR PANTHER; PTHR11852:SF1; PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE IB SUBUNIT ALPHA2; 1. DR Pfam; PF13472; Lipase_GDSL_2; 1. DR SUPFAM; SSF52266; SGNH hydrolase; 1. DR Genevisible; P68402; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; KW Direct protein sequencing; Hydrolase; Lipid degradation; Lipid metabolism; KW Phosphoprotein; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT CHAIN 2..229 FT /note="Platelet-activating factor acetylhydrolase IB FT subunit alpha2" FT /id="PRO_0000058151" FT ACT_SITE 48 FT /evidence="ECO:0000250" FT ACT_SITE 193 FT /evidence="ECO:0000250" FT ACT_SITE 196 FT /evidence="ECO:0000250" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT MOD_RES 2 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 64 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 220 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q61206" FT VAR_SEQ 133..229 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:18155631" FT /id="VSP_043217" FT VAR_SEQ 138..229 FT /note="GLLPRGEKPNPLRQKNAKVNQLLKVSLPKLANVQLLDTDGGFVHSDGAISCH FT DMFDFLHLTGGGYAKICKPLHELIMQLLEETPEEKQTTIA -> IIYWQDEQDYHERKV FT QMD (in isoform 2)" FT /evidence="ECO:0000303|PubMed:18155631" FT /id="VSP_042896" FT VAR_SEQ 139..229 FT /note="LLPRGEKPNPLRQKNAKVNQLLKVSLPKLANVQLLDTDGGFVHSDGAISCHD FT MFDFLHLTGGGYAKICKPLHELIMQLLEETPEEKQTTIA -> KAAASKYSISEIVRLE FT QGSVNWSIGTYPDDTPATTRPAILQLFTGKMSRITMKEKSRWTEEILH (in FT isoform 4)" FT /evidence="ECO:0000303|PubMed:18155631" FT /id="VSP_044680" FT HELIX 8..10 FT /evidence="ECO:0007829|PDB:1VYH" FT STRAND 19..21 FT /evidence="ECO:0007829|PDB:1VYH" FT HELIX 23..37 FT /evidence="ECO:0007829|PDB:1VYH" FT STRAND 41..47 FT /evidence="ECO:0007829|PDB:1VYH" FT HELIX 48..53 FT /evidence="ECO:0007829|PDB:1VYH" FT HELIX 57..62 FT /evidence="ECO:0007829|PDB:1VYH" FT HELIX 64..66 FT /evidence="ECO:0007829|PDB:1VYH" FT STRAND 68..72 FT /evidence="ECO:0007829|PDB:1VYH" FT HELIX 78..86 FT /evidence="ECO:0007829|PDB:1VYH" FT TURN 87..90 FT /evidence="ECO:0007829|PDB:1VYH" FT STRAND 96..101 FT /evidence="ECO:0007829|PDB:1VYH" FT HELIX 111..128 FT /evidence="ECO:0007829|PDB:1VYH" FT STRAND 133..137 FT /evidence="ECO:0007829|PDB:1VYH" FT STRAND 143..145 FT /evidence="ECO:0007829|PDB:1VYH" FT HELIX 148..163 FT /evidence="ECO:0007829|PDB:1VYH" FT STRAND 164..167 FT /evidence="ECO:0007829|PDB:1VYH" FT STRAND 170..173 FT /evidence="ECO:0007829|PDB:1VYH" FT TURN 188..190 FT /evidence="ECO:0007829|PDB:1VYH" FT STRAND 194..197 FT /evidence="ECO:0007829|PDB:1VYH" FT HELIX 199..219 FT /evidence="ECO:0007829|PDB:1VYH" FT CONFLICT P68402-4:151 FT /note="V -> M (in Ref. 2; ABI58227/ABI58228)" FT /evidence="ECO:0000305" SQ SEQUENCE 229 AA; 25569 MW; 14CF5D48621AA504 CRC64; MSQGDSNPAA IPHAAEDIQG DDRWMSQHNR FVLDCKDKEP DVLFVGDSMV QLMQQYEIWR ELFSPLHALN FGIGGDTTRH VLWRLKNGEL ENIKPKVIVV WVGTNNHENT AEEVAGGIEA IVQLINTRQP QAKIIVLGLL PRGEKPNPLR QKNAKVNQLL KVSLPKLANV QLLDTDGGFV HSDGAISCHD MFDFLHLTGG GYAKICKPLH ELIMQLLEET PEEKQTTIA //