ID   PA1B2_MOUSE             Reviewed;         229 AA.
AC   Q61206; Q6PKE6; Q7TNP3;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   27-MAR-2024, 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|MGI:MGI:108415}; Synonyms=Pafahb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ;
RX   PubMed=8954729; DOI=10.1006/dbio.1996.0330;
RA   Albrecht U., Abu-Issa R., Raetz B., Hattori M., Aoki J., Arai H., Inoue K.,
RA   Eichele G.;
RT   "Platelet-activating factor acetylhydrolase expression and activity suggest
RT   a link between neuronal migration and platelet-activating factor.";
RL   Dev. Biol. 180:579-593(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Embryo, and Mammary tumor;
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   [4]
RP   PROTEIN SEQUENCE OF 61-79 AND 134-142, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [5]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=12775763; DOI=10.1073/pnas.1236145100;
RA   Yan W., Assadi A.H., Wynshaw-Boris A., Eichele G., Matzuk M.M., Clark G.D.;
RT   "Previously uncharacterized roles of platelet-activating factor
RT   acetylhydrolase 1b complex in mouse spermatogenesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7189-7194(2003).
RN   [6]
RP   INTERACTION WITH VLDLR.
RX   PubMed=17330141; DOI=10.1371/journal.pone.0000252;
RA   Zhang G., Assadi A.H., McNeil R.S., Beffert U., Wynshaw-Boris A., Herz J.,
RA   Clark G.D., D'Arcangelo G.;
RT   "The Pafah1b complex interacts with the reelin receptor VLDLR.";
RL   PLoS ONE 2:e252-e252(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64 AND THR-220, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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 (PubMed:12775763). {ECO:0000250|UniProtKB:P68401,
CC       ECO:0000269|PubMed:12775763}.
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 (By similarity). Interacts
CC       with VLDLR; this interaction may modulate the Reelin pathway
CC       (PubMed:17330141). {ECO:0000250|UniProtKB:P68401,
CC       ECO:0000250|UniProtKB:P68402, ECO:0000269|PubMed:17330141}.
CC   -!- INTERACTION:
CC       Q61206; O35685: Nudc; NbExp=2; IntAct=EBI-7445518, EBI-911192;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DEVELOPMENTAL STAGE: Expressed already by the time of neurulation. By
CC       10.5 dpc, expression is abundant in the developing central and
CC       peripheral nervous systems. Major sites include the neuroepithelium of
CC       the fore-, mid-, and hindbrain, the spinal cord, the dorsal root, and
CC       cranial ganglia.
CC   -!- DISRUPTION PHENOTYPE: Knockout mice which are homozygous for the
CC       PAFAH1B2 gene appear developmentally normal, and are born at the
CC       expected Mendelian rate (PubMed:12775763). Females bred normally,
CC       whereas male are infertile, and spermatogenesis is disrupted at mid- or
CC       late pachytene stages of meiosis or early spermiogenesis
CC       (PubMed:12775763). Double mutant female mice which are homozygous for
CC       PAFAH1B2 and PAFAH1B3 are grossly normal and fertile, whereas double-
CC       mutant males are infertile. Double mutan mice manifest an earlier
CC       disturbance of spermatogenesis with an onset at preleptotene or
CC       leptotene stages of meiosis (PubMed:12775763).
CC       {ECO:0000269|PubMed:12775763}.
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) (By similarity). Now these
CC       subunits have been renamed beta (PAFAH1B1), alpha2 (PAFAH1B2) and
CC       alpha1 (PAFAH1B3) respectively (By similarity).
CC       {ECO:0000250|UniProtKB:P43034, ECO:0000250|UniProtKB:P68402,
CC       ECO:0000250|UniProtKB:Q15102, ECO:0000250|UniProtKB:Q29460}.
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; U57747; AAC52997.1; -; mRNA.
DR   EMBL; AK153424; BAE31983.1; -; mRNA.
DR   EMBL; BC002037; AAH02037.1; -; mRNA.
DR   EMBL; BC056211; AAH56211.1; -; mRNA.
DR   CCDS; CCDS23139.1; -.
DR   RefSeq; NP_032801.2; NM_008775.3.
DR   RefSeq; XP_006510147.1; XM_006510084.3.
DR   RefSeq; XP_006510148.1; XM_006510085.1.
DR   RefSeq; XP_017168698.1; XM_017313209.1.
DR   AlphaFoldDB; Q61206; -.
DR   SMR; Q61206; -.
DR   BioGRID; 202016; 5.
DR   IntAct; Q61206; 3.
DR   MINT; Q61206; -.
DR   STRING; 10090.ENSMUSP00000127851; -.
DR   BindingDB; Q61206; -.
DR   ChEMBL; CHEMBL3259481; -.
DR   GlyGen; Q61206; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q61206; -.
DR   PhosphoSitePlus; Q61206; -.
DR   SwissPalm; Q61206; -.
DR   REPRODUCTION-2DPAGE; IPI00118821; -.
DR   REPRODUCTION-2DPAGE; Q61206; -.
DR   EPD; Q61206; -.
DR   jPOST; Q61206; -.
DR   MaxQB; Q61206; -.
DR   PaxDb; 10090-ENSMUSP00000127851; -.
DR   PeptideAtlas; Q61206; -.
DR   ProteomicsDB; 294315; -.
DR   Pumba; Q61206; -.
DR   Antibodypedia; 32310; 280 antibodies from 27 providers.
DR   DNASU; 18475; -.
DR   Ensembl; ENSMUST00000172450.3; ENSMUSP00000127851.2; ENSMUSG00000003131.8.
DR   Ensembl; ENSMUST00000214179.2; ENSMUSP00000149819.2; ENSMUSG00000003131.8.
DR   GeneID; 18475; -.
DR   KEGG; mmu:18475; -.
DR   UCSC; uc009pgx.1; mouse.
DR   AGR; MGI:108415; -.
DR   CTD; 5049; -.
DR   MGI; MGI:108415; Pafah1b2.
DR   VEuPathDB; HostDB:ENSMUSG00000003131; -.
DR   eggNOG; KOG1388; Eukaryota.
DR   GeneTree; ENSGT00950000183199; -.
DR   HOGENOM; CLU_051989_2_0_1; -.
DR   InParanoid; Q61206; -.
DR   OMA; EAWNQYF; -.
DR   OrthoDB; 4162633at2759; -.
DR   PhylomeDB; Q61206; -.
DR   TreeFam; TF323955; -.
DR   BRENDA; 3.1.1.47; 3474.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   Reactome; R-MMU-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR   BioGRID-ORCS; 18475; 4 hits in 80 CRISPR screens.
DR   ChiTaRS; Pafah1b2; mouse.
DR   PRO; PR:Q61206; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q61206; Protein.
DR   Bgee; ENSMUSG00000003131; Expressed in spermatid and 287 other cell types or tissues.
DR   ExpressionAtlas; Q61206; baseline and differential.
DR   GO; GO:0008247; C:1-alkyl-2-acetylglycerophosphocholine esterase complex; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0047179; F:platelet-activating factor acetyltransferase activity; ISO:MGI.
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; ISO:MGI.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0016239; P:positive regulation of macroautophagy; ISO:MGI.
DR   GO; GO:0007283; P:spermatogenesis; IMP: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   UCD-2DPAGE; Q61206; -.
DR   Genevisible; Q61206; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P68402"
FT   CHAIN           2..229
FT                   /note="Platelet-activating factor acetylhydrolase IB
FT                   subunit alpha2"
FT                   /id="PRO_0000058152"
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:0000250|UniProtKB:P68402"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P68402"
FT   MOD_RES         64
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         220
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CONFLICT        129..130
FT                   /note="QP -> HA (in Ref. 1; AAC52997)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        188
FT                   /note="C -> W (in Ref. 3; AAH56211)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        222
FT                   /note="E -> G (in Ref. 1; AAC52997)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   229 AA;  25581 MW;  B4D24048621AB182 CRC64;
     MSQGDSNPAA IPHAAEDIQG DDRWMSQHNR FVLDCKDKEP DVLFVGDSMV QLMQQYEIWR
     ELFSPLHALN FGIGGDTTRH VLWRLKNGEL ENIKPKVIVV WVGTNNHENT AEEVAGGIEA
     IVQLINTRQP QAKIIVLGLL PRGEKPNPLR QKNAKVNQLL KVSLPKLANV QLLDIDGGFV
     HSDGAISCHD MFDFLHLTGG GYAKICKPLH ELIMQLLEET PEEKQTTIA
//