ID   PLCB3_MOUSE             Reviewed;        1234 AA.
AC   P51432; Q3UIS0;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 195.
DE   RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 {ECO:0000305};
DE            EC=3.1.4.11 {ECO:0000250|UniProtKB:Q99JE6};
DE   AltName: Full=Phosphoinositide phospholipase C-beta-3;
DE   AltName: Full=Phospholipase C-beta-3;
DE            Short=PLC-beta-3;
GN   Name=Plcb3 {ECO:0000312|MGI:MGI:104778};
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/cJ; TISSUE=Kidney;
RX   PubMed=9714794; DOI=10.1016/s0005-2760(98)00074-5;
RA   Wang S., Zhou Y., Lukinius A., Oberg K., Skogseid B., Gobl A.;
RT   "Molecular cloning and characterization of a cDNA encoding mouse
RT   phospholipase C-beta3.";
RL   Biochim. Biophys. Acta 1393:173-178(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, AND IDENTIFICATION BY
RP   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: 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:Q99JE6}.
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:Q99JE6};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC         Evidence={ECO:0000250|UniProtKB:Q99JE6};
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:Q99JE6};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43485;
CC         Evidence={ECO:0000250|UniProtKB:Q99JE6};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Interacts with SHANK2 (By similarity). Interacts with LPAR2
CC       (By similarity). {ECO:0000250|UniProtKB:Q01970,
CC       ECO:0000250|UniProtKB:Q99JE6}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99JE6}.
CC       Membrane {ECO:0000250|UniProtKB:Q99JE6}. Nucleus
CC       {ECO:0000269|PubMed:9714794}. Note=And particulate fractions.
CC       {ECO:0000250|UniProtKB:Q99JE6}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in kidney, skeletal muscle, liver,
CC       lung, heart and brain. {ECO:0000269|PubMed:9714794}.
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DR   EMBL; U43144; AAA85199.1; -; mRNA.
DR   EMBL; AK146793; BAE27436.1; -; mRNA.
DR   EMBL; CH466612; EDL33267.1; -; Genomic_DNA.
DR   CCDS; CCDS70925.1; -.
DR   RefSeq; NP_001277278.1; NM_001290349.1.
DR   RefSeq; NP_032900.2; NM_008874.4.
DR   AlphaFoldDB; P51432; -.
DR   SMR; P51432; -.
DR   BioGRID; 202234; 5.
DR   IntAct; P51432; 1.
DR   MINT; P51432; -.
DR   STRING; 10090.ENSMUSP00000025912; -.
DR   GlyGen; P51432; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P51432; -.
DR   PhosphoSitePlus; P51432; -.
DR   SwissPalm; P51432; -.
DR   EPD; P51432; -.
DR   jPOST; P51432; -.
DR   MaxQB; P51432; -.
DR   PaxDb; 10090-ENSMUSP00000025912; -.
DR   PeptideAtlas; P51432; -.
DR   ProteomicsDB; 289672; -.
DR   Pumba; P51432; -.
DR   Antibodypedia; 3983; 498 antibodies from 36 providers.
DR   DNASU; 18797; -.
DR   Ensembl; ENSMUST00000025912.10; ENSMUSP00000025912.9; ENSMUSG00000024960.10.
DR   GeneID; 18797; -.
DR   KEGG; mmu:18797; -.
DR   UCSC; uc008gjr.2; mouse.
DR   AGR; MGI:104778; -.
DR   CTD; 5331; -.
DR   MGI; MGI:104778; Plcb3.
DR   VEuPathDB; HostDB:ENSMUSG00000024960; -.
DR   eggNOG; KOG1265; Eukaryota.
DR   GeneTree; ENSGT00940000160539; -.
DR   HOGENOM; CLU_002738_2_0_1; -.
DR   InParanoid; P51432; -.
DR   OMA; DQQIGNG; -.
DR   OrthoDB; 2900494at2759; -.
DR   PhylomeDB; P51432; -.
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; 18797; 4 hits in 75 CRISPR screens.
DR   ChiTaRS; Plcb3; mouse.
DR   PRO; PR:P51432; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; P51432; Protein.
DR   Bgee; ENSMUSG00000024960; Expressed in crypt of Lieberkuhn of small intestine and 218 other cell types or tissues.
DR   ExpressionAtlas; P51432; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0099524; C:postsynaptic cytosol; IDA:SynGO.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0042383; C:sarcolemma; ISO:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005516; F:calmodulin binding; ISO:MGI.
DR   GO; GO:0060090; F:molecular adaptor activity; ISO:MGI.
DR   GO; GO:0140677; F:molecular function activator activity; ISO:MGI.
DR   GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; ISS:UniProtKB.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR   GO; GO:0032957; P:inositol trisphosphate metabolic process; ISO:MGI.
DR   GO; GO:0031161; P:phosphatidylinositol catabolic process; ISO:MGI.
DR   GO; GO:0046488; P:phosphatidylinositol metabolic process; ISS:UniProtKB.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR   GO; GO:0006892; P:post-Golgi vesicle-mediated transport; ISO:MGI.
DR   GO; GO:0003073; P:regulation of systemic arterial blood pressure; ISO:MGI.
DR   GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IBA:GO_Central.
DR   CDD; cd00275; C2_PLC_like; 1.
DR   CDD; cd16210; EFh_PI-PLCbeta3; 1.
DR   CDD; cd13361; PH_PLC_beta; 1.
DR   CDD; cd08591; PI-PLCc_beta; 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; 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; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR   InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR   PANTHER; PTHR10336:SF11; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE BETA-3; 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; P51432; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Calcium; Cytoplasm; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Membrane; Nucleus; Phosphoprotein; Reference proteome;
KW   Transducer.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q01970"
FT   CHAIN           2..1234
FT                   /note="1-phosphatidylinositol 4,5-bisphosphate
FT                   phosphodiesterase beta-3"
FT                   /id="PRO_0000088492"
FT   DOMAIN          318..468
FT                   /note="PI-PLC X-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT   DOMAIN          591..707
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT   DOMAIN          708..836
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   REGION          466..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          888..938
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1001..1026
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1207..1234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1231..1234
FT                   /note="Interaction with SHANK2"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        484..519
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        888..903
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        904..920
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        921..938
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1220..1234
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        332
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT   ACT_SITE        379
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01970"
FT   MOD_RES         474
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01970"
FT   MOD_RES         490
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01970"
FT   MOD_RES         495
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01970"
FT   MOD_RES         537
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         927
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01970"
FT   MOD_RES         1105
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01970"
FT   CONFLICT        16
FT                   /note="P -> S (in Ref. 1; AAA85199)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        20
FT                   /note="E -> K (in Ref. 1; AAA85199)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        609
FT                   /note="A -> S (in Ref. 1; AAA85199)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1234 AA;  139487 MW;  E055744A33C5F6B0 CRC64;
     MAGARPGVHA LQLEPPTVVE TLRRGSKFIK WDEEASSRNL VTLRVDPNGF FLYWTGPNME
     VDTLDISSIR DTRTGRYARL PKDPKIREVL GFGGPDTRLE EKLMTVVAGP DPVNTTFLNF
     MAVQDDTVKV WSEELFKLAM NILAQNASRN TFLRKAYTKL KLQVNQDGRI PVKNILKMFS
     ADKKRVETAL ESCGLNFNRS ESIRPDEFPL EIFERFLNKL CLRPDIDKIL LEIGAKGKPY
     LTLEQLMDFI NQKQRDPRLN EVLYPPLRSS QARLLIEKYE TNKQFLERDQ MSMEGFSRYL
     GGEENGILPL EALDLSMDMT QPLSAYFINS SHNTYLTAGQ LAGPSSVEMY RQALLWGCRC
     VELDVWKGRP PEEEPFITHG FTMTTEVPLR DVLEAIAEAA FKTSPYPVIL SFENHVDSAK
     QQAKMAEYCR SIFGDALLID PLDKYPLSAG IPLPSPQDLM GRILVKNKKR HRPSTGVPDS
     SVRKRPLEQS NSALSESSAA TEPSSPQLGS PSSDSCPGLS NGEEVGLEKT SLEPQKSLGE
     ESLSREPNVP MPDRDREDEE EDEEEEETTD PKKPTTDEGT ASSEVNATEE MSTLVNYVEP
     VKFKSFEAAR KRNKCFEMSS FVETKAMEQL TKSPMEFVEY NKQQLSRIYP KGTRVDSSNY
     MPQLFWNVGC QLVALNFQTL DLPMQLNAGV FEYNGRSGYL LKPEFMRRPD KSFDPFTEVI
     VDGIVANALR VKVISGQFLS DKKVGIYVEV DMFGLPVDTR RKYRTRTSQG NSFNPVWDEE
     PFDFPKVVLP TLASLRIAAF EEGGKFVGHR ILPVSAIRSG YHYVCLRNEA NQPLCLPALL
     IYTEASDYIP DDHQDYAEAL INPIKHVSLM DQRAKQLAAL IGESEAQAST ETYQETPCQQ
     PGSQLPSNPT PNPLDASPRW PPGPTTSSTS SSLSSPGQRD DLIASILSEV TPTPLEELRS
     HKAMVKLRSR QDRDLRELHK KHQRKAVALT RRLLDGLAQA RAEGKCRPSP SALGKATNSE
     DVKEEEEAKQ YREFQNRQVQ SLLELREAQA DVETKRKLEH LRQAHQRLKE VVLDTHTTQF
     KRLKELNERE KKELQKILDR KRNNSISEAK TREKHKKEVE LTEINRRHIT ESVNSIRRLE
     EAQKQRHERL VAGQQQVLQQ LEEEEPKLLA QLTQECQEQR ERLPQEIRRC LLGETAEGLG
     DGPLVACASN GHAPGSGGHL SSADSESQEE NTQL
//