PA1B2_MOUSE
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 03-AUG-2022, entry version 164.
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, Pancreas,
RC 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; 4.
DR IntAct; Q61206; 3.
DR MINT; Q61206; -.
DR STRING; 10090.ENSMUSP00000127851; -.
DR BindingDB; Q61206; -.
DR ChEMBL; CHEMBL3259481; -.
DR iPTMnet; Q61206; -.
DR PhosphoSitePlus; Q61206; -.
DR SwissPalm; Q61206; -.
DR REPRODUCTION-2DPAGE; IPI00118821; -.
DR REPRODUCTION-2DPAGE; Q61206; -.
DR UCD-2DPAGE; Q61206; -.
DR EPD; Q61206; -.
DR jPOST; Q61206; -.
DR MaxQB; Q61206; -.
DR PaxDb; Q61206; -.
DR PeptideAtlas; Q61206; -.
DR PRIDE; Q61206; -.
DR ProteomicsDB; 294315; -.
DR Antibodypedia; 32310; 248 antibodies from 27 providers.
DR DNASU; 18475; -.
DR Ensembl; ENSMUST00000172450; ENSMUSP00000127851; ENSMUSG00000003131.
DR Ensembl; ENSMUST00000214179; ENSMUSP00000149819; ENSMUSG00000003131.
DR GeneID; 18475; -.
DR KEGG; mmu:18475; -.
DR UCSC; uc009pgx.1; mouse.
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; QQCEIWR; -.
DR OrthoDB; 1604899at2759; -.
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 75 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 283 other tissues.
DR ExpressionAtlas; Q61206; baseline and differential.
DR Genevisible; Q61206; MM.
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:0007420; P:brain development; IBA:GO_Central.
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 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 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
