PA1B2_HUMAN
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 03-AUG-2022, entry version 173.
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}.
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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; 62.
DR IntAct; P68402; 22.
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 BioMuta; PAFAH1B2; -.
DR DMDM; 55977294; -.
DR REPRODUCTION-2DPAGE; IPI00026546; -.
DR EPD; P68402; -.
DR jPOST; P68402; -.
DR MassIVE; P68402; -.
DR MaxQB; P68402; -.
DR PaxDb; P68402; -.
DR PeptideAtlas; P68402; -.
DR PRIDE; P68402; -.
DR ProteomicsDB; 21857; -.
DR ProteomicsDB; 57538; -. [P68402-1]
DR ProteomicsDB; 57539; -. [P68402-2]
DR ProteomicsDB; 57540; -. [P68402-3]
DR Antibodypedia; 32310; 248 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 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; NHAISCH; -.
DR OrthoDB; 1604899at2759; -.
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; 14 hits in 1079 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 190 other tissues.
DR ExpressionAtlas; P68402; baseline and differential.
DR Genevisible; P68402; HS.
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:0007420; P:brain development; IBA:GO_Central.
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 Gene3D; 3.40.50.1110; -; 1.
DR InterPro; IPR013830; SGNH_hydro.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR Pfam; PF13472; Lipase_GDSL_2; 1.
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
