PLCH1_MOUSE
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 03-AUG-2022, entry version 147.
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;
CC Evidence={ECO:0000255|PROSITE-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; Q4KWH5; -.
DR PeptideAtlas; Q4KWH5; -.
DR PRIDE; 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; 83 antibodies from 23 providers.
DR DNASU; 269437; -.
DR Ensembl; ENSMUST00000084105; ENSMUSP00000081122; ENSMUSG00000036834. [Q4KWH5-1]
DR Ensembl; ENSMUST00000159676; ENSMUSP00000124632; ENSMUSG00000036834. [Q4KWH5-3]
DR Ensembl; ENSMUST00000162269; ENSMUSP00000124463; ENSMUSG00000036834. [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 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; 368239at2759; -.
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 74 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 154 other tissues.
DR ExpressionAtlas; Q4KWH5; baseline and differential.
DR Genevisible; Q4KWH5; MM.
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; ISO:MGI.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR Gene3D; 3.20.20.190; -; 2.
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.
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; PTHR10336; 1.
DR PANTHER; PTHR10336:SF51; PTHR10336:SF51; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF09279; EF-hand_like; 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; SSF47473; SSF47473; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF51695; SSF51695; 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.
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
