ID   PLCH1_MOUSE             Reviewed;        1682 AA.
AC   Q4KWH5; Q4KWH6; Q4KWH7; Q69ZS3; Q7TPQ1; Q8CFQ2;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   24-JAN-2024, entry version 154.
DE   RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase eta-1 {ECO:0000305};
DE            EC=3.1.4.11 {ECO:0000250|UniProtKB:Q4KWH8};
DE   AltName: Full=Phosphoinositide phospholipase C-eta-1;
DE   AltName: Full=Phospholipase C-eta-1;
DE            Short=PLC-eta-1;
DE   AltName: Full=Phospholipase C-like protein 3;
DE            Short=PLC-L3;
GN   Name=Plch1 {ECO:0000312|MGI:MGI:2683547}; Synonyms=Kiaa1069, Plcl3;
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] (ISOFORMS 1; 3 AND 4), TISSUE SPECIFICITY, AND
RP   FUNCTION.
RX   PubMed=15702972; DOI=10.1042/bj20041677;
RA   Hwang J.-I., Oh Y.-S., Shin K.-J., Kim H., Ryu S.H., Suh P.-G.;
RT   "Molecular cloning and characterization of a novel phospholipase C, PLC-
RT   eta.";
RL   Biochem. J. 389:181-186(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5).
RC   TISSUE=Eye;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 373-1682 (ISOFORM 2).
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
CC   -!- FUNCTION: The production of the second messenger molecules
CC       diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated
CC       by calcium-activated phosphatidylinositol-specific phospholipase C
CC       enzymes. {ECO:0000269|PubMed:15702972}.
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:Q4KWH8};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC         Evidence={ECO:0000250|UniProtKB:Q4KWH8};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00041};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q4KWH8}.
CC       Membrane {ECO:0000250|UniProtKB:Q4KWH8}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1; Synonyms=PLC-eta-1;
CC         IsoId=Q4KWH5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q4KWH5-2; Sequence=VSP_032908, VSP_032909, VSP_032911;
CC       Name=3; Synonyms=PLC-eta-1b;
CC         IsoId=Q4KWH5-3; Sequence=VSP_032912, VSP_032915;
CC       Name=4; Synonyms=PLC-eta-1a;
CC         IsoId=Q4KWH5-4; Sequence=VSP_032913, VSP_032914;
CC       Name=5;
CC         IsoId=Q4KWH5-5; Sequence=VSP_032907, VSP_032910, VSP_032911,
CC                                  VSP_032912, VSP_032915;
CC   -!- TISSUE SPECIFICITY: Expressed in brain and to a lower extent in lung.
CC       In brain, it is found in cerebrum, cerebellum and spinal cord.
CC       {ECO:0000269|PubMed:15702972}.
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DR   EMBL; AY691172; AAW22609.1; -; mRNA.
DR   EMBL; AY691173; AAW22610.1; -; mRNA.
DR   EMBL; AY691174; AAW22611.1; -; mRNA.
DR   EMBL; BC042549; AAH42549.1; -; mRNA.
DR   EMBL; BC052372; AAH52372.1; -; mRNA.
DR   EMBL; BC055005; AAH55005.1; -; mRNA.
DR   EMBL; AK173095; BAD32373.1; -; mRNA.
DR   CCDS; CCDS38444.2; -. [Q4KWH5-1]
DR   CCDS; CCDS50918.1; -. [Q4KWH5-3]
DR   CCDS; CCDS57215.1; -. [Q4KWH5-4]
DR   RefSeq; NP_001171203.1; NM_001177732.1. [Q4KWH5-4]
DR   RefSeq; NP_001171204.1; NM_001177733.1. [Q4KWH5-3]
DR   RefSeq; NP_899014.2; NM_183191.3. [Q4KWH5-1]
DR   AlphaFoldDB; Q4KWH5; -.
DR   SMR; Q4KWH5; -.
DR   STRING; 10090.ENSMUSP00000081122; -.
DR   iPTMnet; Q4KWH5; -.
DR   PhosphoSitePlus; Q4KWH5; -.
DR   MaxQB; Q4KWH5; -.
DR   PaxDb; 10090-ENSMUSP00000081122; -.
DR   PeptideAtlas; Q4KWH5; -.
DR   ProteomicsDB; 289531; -. [Q4KWH5-1]
DR   ProteomicsDB; 289532; -. [Q4KWH5-2]
DR   ProteomicsDB; 289533; -. [Q4KWH5-3]
DR   ProteomicsDB; 289534; -. [Q4KWH5-4]
DR   ProteomicsDB; 289535; -. [Q4KWH5-5]
DR   Antibodypedia; 46750; 96 antibodies from 24 providers.
DR   DNASU; 269437; -.
DR   Ensembl; ENSMUST00000084105.12; ENSMUSP00000081122.6; ENSMUSG00000036834.17. [Q4KWH5-1]
DR   Ensembl; ENSMUST00000159676.9; ENSMUSP00000124632.3; ENSMUSG00000036834.17. [Q4KWH5-3]
DR   Ensembl; ENSMUST00000162269.9; ENSMUSP00000124463.3; ENSMUSG00000036834.17. [Q4KWH5-4]
DR   GeneID; 269437; -.
DR   KEGG; mmu:269437; -.
DR   UCSC; uc008pju.2; mouse. [Q4KWH5-5]
DR   UCSC; uc008pjv.2; mouse. [Q4KWH5-2]
DR   UCSC; uc033htw.1; mouse. [Q4KWH5-4]
DR   UCSC; uc033htx.1; mouse. [Q4KWH5-3]
DR   UCSC; uc033hty.1; mouse. [Q4KWH5-1]
DR   AGR; MGI:2683547; -.
DR   CTD; 23007; -.
DR   MGI; MGI:2683547; Plch1.
DR   VEuPathDB; HostDB:ENSMUSG00000036834; -.
DR   eggNOG; KOG0169; Eukaryota.
DR   GeneTree; ENSGT00940000157185; -.
DR   HOGENOM; CLU_002738_4_0_1; -.
DR   InParanoid; Q4KWH5; -.
DR   OMA; CRTAKCR; -.
DR   OrthoDB; 2900494at2759; -.
DR   PhylomeDB; Q4KWH5; -.
DR   TreeFam; TF313216; -.
DR   BRENDA; 3.1.4.11; 3474.
DR   Reactome; R-MMU-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR   BioGRID-ORCS; 269437; 4 hits in 79 CRISPR screens.
DR   ChiTaRS; Plch1; mouse.
DR   PRO; PR:Q4KWH5; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q4KWH5; Protein.
DR   Bgee; ENSMUSG00000036834; Expressed in optic fissure and 156 other cell types or tissues.
DR   ExpressionAtlas; Q4KWH5; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0050429; F:calcium-dependent phospholipase C activity; ISO:MGI.
DR   GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IBA:GO_Central.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR   GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IBA:GO_Central.
DR   CDD; cd00275; C2_PLC_like; 1.
DR   CDD; cd16220; EFh_PI-PLCeta1; 1.
DR   CDD; cd08632; PI-PLCc_eta1; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
DR   Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 2.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR001192; PI-PLC_fam.
DR   InterPro; IPR028392; PLC-eta1_cat.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   InterPro; IPR015359; PLC_EF-hand-like.
DR   InterPro; IPR046972; PLCeta1_EF.
DR   InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR   InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR   PANTHER; PTHR10336:SF51; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE ETA-1; 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; PF16457; PH_12; 1.
DR   Pfam; PF00388; PI-PLC-X; 1.
DR   Pfam; PF00387; PI-PLC-Y; 1.
DR   PRINTS; PR00390; PHPHLIPASEC.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00054; EFh; 2.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00148; PLCXc; 1.
DR   SMART; SM00149; PLCYc; 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; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 3.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR   PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
DR   Genevisible; Q4KWH5; MM.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Calcium; Cytoplasm; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Membrane; Metal-binding; Reference proteome; Repeat;
KW   Transducer.
FT   CHAIN           1..1682
FT                   /note="1-phosphatidylinositol 4,5-bisphosphate
FT                   phosphodiesterase eta-1"
FT                   /id="PRO_0000329008"
FT   DOMAIN          20..128
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          142..177
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          178..214
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          226..246
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          299..444
FT                   /note="PI-PLC X-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT   DOMAIN          602..715
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT   DOMAIN          716..844
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   REGION          534..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          992..1083
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1296..1321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1581..1603
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..562
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        563..578
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        992..1021
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1022..1052
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        314
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT   ACT_SITE        358
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT   BINDING         155
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         157
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         159
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         166
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         315
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         344
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         346
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         393
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         442
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         444
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         628
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         655
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         759
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         761
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         785
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         814
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         815
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         816
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..563
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_032907"
FT   VAR_SEQ         1..21
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15368895,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_032908"
FT   VAR_SEQ         557
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15368895,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_032909"
FT   VAR_SEQ         564..584
FT                   /note="SKSYSTDDEDDSLQNPGKEGG -> MDFFSLHFKTWAVTMSSCHQR (in
FT                   isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_032910"
FT   VAR_SEQ         863..882
FT                   /note="Missing (in isoform 2 and isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15368895,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_032911"
FT   VAR_SEQ         1001..1073
FT                   /note="AGDKDDRRKGAATRKDPHFSNFNKKLSSSSSALLHKDANQGPTASVSNPEQC
FT                   GGRGAKSERIKPNMTNDCQEN -> DLNRKQRKQETRMTEEREPQLEKTHIFQISTKSY
FT                   PPPPVRSSTKMPTKGQLPVYQTQNSVEDEVQRVRGSNQI (in isoform 3 and
FT                   isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:15702972"
FT                   /id="VSP_032912"
FT   VAR_SEQ         1001..1003
FT                   /note="AGD -> VQI (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15702972"
FT                   /id="VSP_032913"
FT   VAR_SEQ         1004..1682
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15702972"
FT                   /id="VSP_032914"
FT   VAR_SEQ         1074..1682
FT                   /note="Missing (in isoform 3 and isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:15702972"
FT                   /id="VSP_032915"
FT   CONFLICT        373..385
FT                   /note="VETINKHAFVKNE -> AIDRPWLCCCSLR (in Ref. 3;
FT                   BAD32373)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        523
FT                   /note="H -> D (in Ref. 3; BAD32373)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1682 AA;  187743 MW;  84B1BA6B4B6378A4 CRC64;
     MADLEVYKNL SPEKVERCMS VMQSGTQMIK LKRGTKGLVR LFYLDEHRTR LRWRPSRKSE
     KAKILIDSIY KVTEGRQSEI FHRQAEGNFD PSCCFTIYHG NHMESLDLIT SNPEEARTWI
     TGLKYLMAGI SDEDSLAKRQ RTHDQWVKQT FEEADKNGDG LLNIEEIHQL MHKLNVNLPR
     RKVRQMFQEA DTDENQGTLT FEEFCVFYKM MSLRRDLYLL LLSYSDKKDH LTVEELAQFL
     KVEQKMSNVT LDYCLDIIMK FEVSEENKVK NVLGIEGFTN FMRSPACDVF NPLHHEVYQD
     MDQPLCNYYI ASSHNTYLTG DQLLSQSKVD MYARVLQEGC RCVEVDCWDG PDGEPVVHHG
     YTLTSKILFR DVVETINKHA FVKNEFPVIL SIENHCSIQQ QRKIAQYLKG ILQDKLDLSS
     VDTGECRQLP SPQSLKGKIL VKGKKLPYHL GDDAEEGEVS DEDSADEIED ECKFKLHYSN
     GTTEHQVESF IRKKLESLLK ESQIRDKEDP DSFTVRALLK ATHEGLNAHL KQNLDVKESG
     KKSHGRSLMA NFGKHKQKAT KSRSKSYSTD DEDDSLQNPG KEGGQLYRLG RRRRTMKLCR
     ELSDLVVYTN SVAAQDIVDD GTTGNVLSFS ETRAHQVVQQ KSEQFMIYNQ KQLTRIYPSA
     YRIDSSNFNP LPYWNAGCQL VALNYQSEGR MMQINRAKFK ANGNCGYILK PQQMCKGTFN
     PFSGDPLPAN PKKQLILKVI SGQQLPKPPD SMFGDRGEII DPFVEVEIIG LPVDCCKDQT
     RVVDDNGFNP VWEETLTFTV HMPEIALVRF LVWDHDPIGR DFVGQRTVTF SSLVPGYRHV
     YLEGLTEASI FVHITINEIF GKWSPLILNP SYTILHFLGA TKNRQLQGLK GLFNKNPRHA
     SSENNSHYVR KRSIGDRILR RTASAPAKGR KKSKVGFQEM VEIKDSVSEA SRDQDGVLRR
     TTRSLQVRPV SMPVDKSLLG ALSLPISEAA KDTDGKENCL AGDKDDRRKG AATRKDPHFS
     NFNKKLSSSS SALLHKDANQ GPTASVSNPE QCGGRGAKSE RIKPNMTNDC QENHNPPKFL
     SPRKHLALDP ATKGLQERLH GMKTNEKEHA EGFLGEKSML SGSVLSQSSL EVENLEGSRA
     KGRAATSFSL SDVSALCSDI PDLHSTAILQ DTEISNLIDD VTLTNENQSG SSISALIGQF
     EESNHPANVT VVSHLSTSGA SGSAPFQTPF KHGLSQGNQK ASFLCSSPEL NKLSSVETTK
     LANNAVPCGV IGSPISTPKP GDDPSDKAKT RVIEGNLPGF PDASPGQFPK SPTHGEDHSQ
     VMNSPALSTE LAIEDIIADP ALSINSAESS LVEIDGESEN LSLTTCDYRE EAPSQLVSPL
     KLQQSQEMVE HIQRGLRNGY CKETLLPSEI FNNIPGVKNH SISHLTYQGA GFVYNHFSSS
     DAKTNQICEP QQPRAPDMHA PTPTPSTHAP LAALKLPSPC KSKSLGDLTS EDIACNFESK
     YQCISRSFVT NGIRDKSVTM KTKSLEPLDA LTEQLRKLVS FDQEDSCQVL YSKQDVNQCP
     RALVRKLSSR SQSRVRNIAS RAKEKQEAGK QKAMAQSTRG GVVLRSKPPA PALAVNRHST
     GSYIASYLRN MKAGGLEGRG IPEGACTALR YGYMDQFCSD NSVLQTEPSS EDKPEIYFLL
     RL
//