ID   PLCB2_MOUSE             Reviewed;        1181 AA.
AC   A3KGF7; Q2M4J1; Q3TER8; Q8BI81;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 131.
DE   RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2 {ECO:0000305};
DE            EC=3.1.4.11 {ECO:0000250|UniProtKB:Q00722};
DE   AltName: Full=Phosphoinositide phospholipase C-beta-2;
DE   AltName: Full=Phospholipase C-beta-2;
DE            Short=PLC-beta-2;
GN   Name=Plcb2 {ECO:0000312|MGI:MGI:107465};
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 [GENOMIC DNA] (ISOFORM 3).
RA   Farber C.R., Corva P.M., Medrano J.F.;
RT   "Characterization of quantitative trait loci influencing growth and
RT   adiposity using congenic mouse strains.";
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Thymus;
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 GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Spleen;
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: The production of the second messenger molecules
CC       diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated
CC       by activated phosphatidylinositol-specific phospholipase C enzymes.
CC       {ECO:0000250|UniProtKB:Q00722}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC         bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-
CC         diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456,
CC         ChEBI:CHEBI:203600; EC=3.1.4.11;
CC         Evidence={ECO:0000250|UniProtKB:Q00722};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC         Evidence={ECO:0000250|UniProtKB:Q00722};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + H2O =
CC         1D-myo-inositol 1-phosphate + a 1,2-diacyl-sn-glycerol + H(+);
CC         Xref=Rhea:RHEA:43484, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17815, ChEBI:CHEBI:57880, ChEBI:CHEBI:58433;
CC         Evidence={ECO:0000250|UniProtKB:Q00722};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43485;
CC         Evidence={ECO:0000250|UniProtKB:Q00722};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Interacts with RAC1. Forms a complex composed of at least
CC       WDR26, a G-beta:gamma unit, and PLCB2. {ECO:0000250|UniProtKB:Q00722}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=A3KGF7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A3KGF7-2; Sequence=VSP_026982, VSP_026985, VSP_026986;
CC       Name=3;
CC         IsoId=A3KGF7-3; Sequence=VSP_026985, VSP_026986;
CC       Name=4;
CC         IsoId=A3KGF7-4; Sequence=VSP_026981, VSP_026983, VSP_026984;
CC   -!- MISCELLANEOUS: The receptor-mediated activation of PLC-beta-2 is most
CC       effectively mediated by one G-protein alpha subunit, alpha-16.
CC       {ECO:0000250}.
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DR   EMBL; AY902324; AAX90609.1; -; Genomic_DNA.
DR   EMBL; AK045469; BAC32384.1; -; mRNA.
DR   EMBL; AK169442; BAE41180.1; -; mRNA.
DR   EMBL; AL772255; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS16582.1; -. [A3KGF7-1]
DR   RefSeq; NP_001277719.1; NM_001290790.1.
DR   RefSeq; NP_808236.2; NM_177568.2. [A3KGF7-1]
DR   AlphaFoldDB; A3KGF7; -.
DR   SMR; A3KGF7; -.
DR   BioGRID; 202233; 3.
DR   CORUM; A3KGF7; -.
DR   IntAct; A3KGF7; 6.
DR   STRING; 10090.ENSMUSP00000099583; -.
DR   iPTMnet; A3KGF7; -.
DR   PhosphoSitePlus; A3KGF7; -.
DR   EPD; A3KGF7; -.
DR   MaxQB; A3KGF7; -.
DR   PaxDb; 10090-ENSMUSP00000099583; -.
DR   PeptideAtlas; A3KGF7; -.
DR   ProteomicsDB; 289525; -. [A3KGF7-1]
DR   ProteomicsDB; 289526; -. [A3KGF7-2]
DR   ProteomicsDB; 289527; -. [A3KGF7-3]
DR   ProteomicsDB; 289528; -. [A3KGF7-4]
DR   Antibodypedia; 4002; 230 antibodies from 28 providers.
DR   DNASU; 18796; -.
DR   Ensembl; ENSMUST00000102524.8; ENSMUSP00000099583.2; ENSMUSG00000040061.18. [A3KGF7-1]
DR   GeneID; 18796; -.
DR   KEGG; mmu:18796; -.
DR   UCSC; uc008lsi.1; mouse. [A3KGF7-1]
DR   UCSC; uc008lsk.1; mouse. [A3KGF7-2]
DR   UCSC; uc008lsl.1; mouse. [A3KGF7-4]
DR   AGR; MGI:107465; -.
DR   CTD; 5330; -.
DR   MGI; MGI:107465; Plcb2.
DR   VEuPathDB; HostDB:ENSMUSG00000040061; -.
DR   eggNOG; KOG1265; Eukaryota.
DR   GeneTree; ENSGT00940000159326; -.
DR   HOGENOM; CLU_002738_2_0_1; -.
DR   InParanoid; A3KGF7; -.
DR   OMA; RLAKCQD; -.
DR   OrthoDB; 2900494at2759; -.
DR   PhylomeDB; A3KGF7; -.
DR   TreeFam; TF313216; -.
DR   Reactome; R-MMU-112043; PLC beta mediated events.
DR   Reactome; R-MMU-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR   Reactome; R-MMU-399997; Acetylcholine regulates insulin secretion.
DR   Reactome; R-MMU-4086398; Ca2+ pathway.
DR   Reactome; R-MMU-416476; G alpha (q) signalling events.
DR   Reactome; R-MMU-418217; G beta:gamma signalling through PLC beta.
DR   Reactome; R-MMU-434316; Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
DR   Reactome; R-MMU-500657; Presynaptic function of Kainate receptors.
DR   BioGRID-ORCS; 18796; 1 hit in 81 CRISPR screens.
DR   ChiTaRS; Plcb2; mouse.
DR   PRO; PR:A3KGF7; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; A3KGF7; Protein.
DR   Bgee; ENSMUSG00000040061; Expressed in granulocyte and 89 other cell types or tissues.
DR   ExpressionAtlas; A3KGF7; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0031680; C:G-protein beta/gamma-subunit complex; ISO:MGI.
DR   GO; GO:0098992; C:neuronal dense core vesicle; IDA:SynGO.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; ISO:MGI.
DR   GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; ISS:UniProtKB.
DR   GO; GO:0004629; F:phospholipase C activity; ISO:MGI.
DR   GO; GO:0005543; F:phospholipid binding; ISO:MGI.
DR   GO; GO:0001580; P:detection of chemical stimulus involved in sensory perception of bitter taste; ISO:MGI.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0046488; P:phosphatidylinositol metabolic process; ISS:UniProtKB.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISO:MGI.
DR   GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IBA:GO_Central.
DR   GO; GO:0050913; P:sensory perception of bitter taste; IMP:MGI.
DR   CDD; cd00275; C2_PLC_like; 1.
DR   CDD; cd16209; EFh_PI-PLCbeta2; 1.
DR   CDD; cd13361; PH_PLC_beta; 1.
DR   CDD; cd08624; PI-PLCc_beta2; 1.
DR   Gene3D; 2.30.29.240; -; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR   Gene3D; 1.20.1230.10; Phospholipase C beta, distal C-terminal domain; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR001192; PI-PLC_fam.
DR   InterPro; IPR016280; PLC-beta.
DR   InterPro; IPR028403; PLC-beta2_cat.
DR   InterPro; IPR014815; PLC-beta_C.
DR   InterPro; IPR042531; PLC-beta_C_sf.
DR   InterPro; IPR037862; PLC-beta_PH.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   InterPro; IPR015359; PLC_EF-hand-like.
DR   InterPro; IPR046969; PLCbeta2_EF.
DR   InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR   InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR   PANTHER; PTHR10336:SF10; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE BETA-2; 1.
DR   PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF09279; EF-hand_like; 1.
DR   Pfam; PF17787; PH_14; 1.
DR   Pfam; PF00388; PI-PLC-X; 1.
DR   Pfam; PF00387; PI-PLC-Y; 1.
DR   Pfam; PF08703; PLC-beta_C; 1.
DR   PIRSF; PIRSF000956; PLC-beta; 1.
DR   PRINTS; PR00390; PHPHLIPASEC.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00148; PLCXc; 1.
DR   SMART; SM00149; PLCYc; 1.
DR   SUPFAM; SSF69989; C-terminal domain of PLC-beta; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR   PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
DR   Genevisible; A3KGF7; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Coiled coil; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Metal-binding; Phosphoprotein; Reference proteome;
KW   Transducer.
FT   CHAIN           1..1181
FT                   /note="1-phosphatidylinositol 4,5-bisphosphate
FT                   phosphodiesterase beta-2"
FT                   /id="PRO_0000295683"
FT   DOMAIN          312..463
FT                   /note="PI-PLC X-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT   DOMAIN          547..663
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT   DOMAIN          666..791
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   REGION          465..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          847..890
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1149..1181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          893..940
FT                   /evidence="ECO:0000255"
FT   COILED          974..1026
FT                   /evidence="ECO:0000255"
FT   COILED          1075..1141
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        499..522
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        847..873
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        327
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT   ACT_SITE        374
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT   BINDING         328
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         357
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         359
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         408
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         950
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00722"
FT   VAR_SEQ         1..55
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_026981"
FT   VAR_SEQ         55..77
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_026982"
FT   VAR_SEQ         637..688
FT                   /note="DLPMQQNMALFEFNGQSGYLLKHEFMRRLDKQFNPFSVDRIDVVVATTLSIT
FT                   -> GKNTSKTREPSPGPLTTSPEPSPGPCIPRCPPSEPSSGPCLSDPYSSLDKEL (in
FT                   isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_026983"
FT   VAR_SEQ         689..1181
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_026984"
FT   VAR_SEQ         689..702
FT                   /note="IISGQFLSERSVRT -> ARPRADKWLGGLGS (in isoform 2 and
FT                   isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_026985"
FT   VAR_SEQ         703..1181
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_026986"
SQ   SEQUENCE   1181 AA;  134546 MW;  8E23BD29391ABE4E CRC64;
     MSLLNPVLLP PNVKAYLSQG ERFIKWDDET SIASPVILRV DPKGYYLYWT YQNQEMEFLD
     VTSIRDTRFG KFAKIPKSQK LREVFNMDFP DNHFLLKTLT VVSGPDMVDL TFYNFVSYKE
     NVGKDWAEDV LALAKHPMTV NAPRSTFLDK ILVKLKMQLN PEGKIPVKNF FQMFPADRKR
     VEAALGACHL AKGKNDAINP EDFPESVYKS FLMSLCPRPE IDEIFTSYHS KAKPYMTKEH
     LTKFINQKQR DPRLNSLLFP PARPEQVQVL IDKYEPSGIN VQRGQLSPEG MVWFLCGPEN
     SVLAHDTLLI HQDMTQPLNH YFINSSHNTY LTAGQFSGLS SAEMYRQVLL SGCRCVELDC
     WKGKPPDEEP IITHGFTMTT DILFKEAIEA IAESAFKTSP YPVILSFENH VDSPRQQAKM
     AEYCRSMFGE TLLTDPLENF PLKPGIPLPS PEDLRGKILI KNKKNQFSGP ASPSKKPGGV
     AEGSLPSSVP VEEDTGWTAE DRTEVEEEEV VEEEEEEESG NLDEEEIKKM QSDEGTAGLE
     VTAYEEMSSL VNYIQPTKFI SFEFSAQKNR SYVVSSFTEL KAYELLSKAS MQFVDYNKRQ
     MSRVYPKGTR MDSSNYMPQM FWNAGCQMVA LNFQTMDLPM QQNMALFEFN GQSGYLLKHE
     FMRRLDKQFN PFSVDRIDVV VATTLSITII SGQFLSERSV RTYVEVELFG LPGDPKRRYR
     TKLSPTANSI NPVWKEEPFI FEKILMPELA SLRIAVMEEG SKFLGHRIIP INALHSGYHH
     LCLRSESNMA LTMPALFVFL EMKDYIPDTW ADLTVALANP IKYFNAQDKK SVKLKGVTGS
     LPEKLFSGTP VASQSNGAPV SAGNGSTAPG TKATGEEATK EVTEPQTASL EELRELKGVV
     KLQRRHEKEL RELERRGARR WEELLQRGAA QLAELQTQAA GCKLRPGKGS RKKRTLPCEE
     TVVAPSEPHD RADPRVQELK DRLEQELQQQ GEEQYRSVLK RKEQHVTEQI AKMMELAREK
     QAAELKTFKE TSETDTKEMK KKLEAKRLER IQAMTKVTTD KVAQERLKRE INNSHIQEVV
     QAVKQMTETL ERHQEKLEER QTACLEQIQA MEKQFQEKAL AEYEAKMKGL EAEVKESVRA
     YFKDCFPTEA EDKPERSCEA SEESCPQEPL VSKADTQESR L
//