PLCD4_RAT
ID PLCD4_RAT Reviewed; 772 AA.
AC Q62711; Q63693;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-4 {ECO:0000305};
DE EC=3.1.4.11 {ECO:0000269|PubMed:8550586};
DE AltName: Full=Phosphoinositide phospholipase C-delta-4;
DE AltName: Full=Phospholipase C-delta-4;
DE Short=PLC-delta-4;
GN Name=Plcd4 {ECO:0000312|RGD:621025};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, ENZYME
RP ACTIVITY, COFACTOR, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8550568; DOI=10.1074/jbc.271.1.25;
RA Lee S.B., Rhee S.-G.;
RT "Molecular cloning, splice variants, expression, and purification of
RT phospholipase C-delta 4.";
RL J. Biol. Chem. 271:25-31(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION, AND CATALYTIC
RP ACTIVITY.
RC STRAIN=Donryu;
RX PubMed=8550586; DOI=10.1074/jbc.271.1.355;
RA Liu N., Fukami K., Yu H., Takenawa T.;
RT "A new phospholipase C delta 4 is induced at S-phase of the cell cycle and
RT appears in the nucleus.";
RL J. Biol. Chem. 271:355-360(1996).
RN [3]
RP ALTERNATIVE SPLICING (ISOFORM 4), FUNCTION (ISOFORM 4), AND MUTAGENESIS OF
RP ARG-36.
RX PubMed=9915823; DOI=10.1074/jbc.274.5.2872;
RA Nagano K., Fukami K., Minagawa T., Watanabe Y., Ozaki C., Takenawa T.;
RT "A novel phospholipase C delta4 (PLCdelta4) splice variant as a negative
RT regulator of PLC.";
RL J. Biol. Chem. 274:2872-2879(1999).
RN [4]
RP DOMAIN C2, AND MUTAGENESIS OF LYS-714; SER-717 AND ARG-718.
RX PubMed=11706040; DOI=10.1074/jbc.m109705200;
RA Ananthanarayanan B., Das S., Rhee S.-G., Murray D., Cho W.;
RT "Membrane targeting of C2 domains of phospholipase C-delta isoforms.";
RL J. Biol. Chem. 277:3568-3575(2002).
RN [5]
RP DOMAIN PH, AND SUBCELLULAR LOCATION.
RX PubMed=15037625; DOI=10.1074/jbc.m312772200;
RA Lee S.B., Varnai P., Balla A., Jalink K., Rhee S.G., Balla T.;
RT "The pleckstrin homology domain of phosphoinositide-specific phospholipase
RT Cdelta4 is not a critical determinant of the membrane localization of the
RT enzyme.";
RL J. Biol. Chem. 279:24362-24371(2004).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=17063484; DOI=10.1002/jcb.21048;
RA Lo Vasco V.R., Fabrizi C., Artico M., Cocco L., Billi A.M., Fumagalli L.,
RA Manzoli F.A.;
RT "Expression of phosphoinositide-specific phospholipase C isoenzymes in
RT cultured astrocytes.";
RL J. Cell. Biochem. 100:952-959(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445 AND SER-458, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Hydrolyzes the phosphatidylinositol 4,5-bisphosphate (PIP2)
CC to generate 2 second messenger molecules diacylglycerol (DAG) and
CC inositol 1,4,5-trisphosphate (IP3). DAG mediates the activation of
CC protein kinase C (PKC), while IP3 releases Ca(2+) from intracellular
CC stores. Required for acrosome reaction in sperm during fertilization,
CC probably by acting as an important enzyme for intracellular Ca(2+)
CC mobilization in the zona pellucida-induced acrosome reaction. May play
CC a role in cell growth. Modulates the liver regeneration in cooperation
CC with nuclear PKC. Overexpression up-regulates the Erk signaling pathway
CC and proliferation. {ECO:0000269|PubMed:8550568}.
CC -!- FUNCTION: [Isoform 4]: Has no enzyme activity and acts as a negative
CC regulator of phospholipase C, with a preference for thePLC-delta
CC family. {ECO:0000269|PubMed:9915823}.
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:0000269|PubMed:8550586};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC Evidence={ECO:0000305|PubMed:8550586};
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:Q9BRC7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43485;
CC Evidence={ECO:0000250|UniProtKB:Q9BRC7};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000305|PubMed:8550568};
CC Note=Binds 3 Ca(2+) ions per subunit. Two of the Ca(2+) ions are bound
CC to the C2 domain. {ECO:0000305|PubMed:8550568};
CC -!- SUBUNIT: Interacts with GRIP1 (By similarity). Interacts (via GBA
CC motif) with guanine nucleotide-binding protein G(i) alpha subunit GNAI3
CC (inactive GDP-bound form); low-affinity interaction (By similarity).
CC {ECO:0000250|UniProtKB:Q8K3R3, ECO:0000250|UniProtKB:Q9BRC7}.
CC -!- SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane protein.
CC Nucleus. Cytoplasm. Endoplasmic reticulum. Note=Localizes primarily to
CC intracellular membranes mostly to the endoplasmic reticulum.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q62711-1; Sequence=Displayed;
CC Name=2; Synonyms=ALT I;
CC IsoId=Q62711-2; Sequence=VSP_028508;
CC Name=3; Synonyms=ALT II;
CC IsoId=Q62711-3; Sequence=VSP_028509;
CC Name=4; Synonyms=ALT III;
CC IsoId=Q62711-4; Sequence=VSP_028507;
CC -!- TISSUE SPECIFICITY: Present at high level in testis. Also present in
CC brain > skeletal muscle > thyroid gland > stomach > thymus > aorta >
CC heart (at protein level). Highly expressed in regenerating liver.
CC Isoform 4 is weakly expressed compared to other isoforms but is
CC expressed at high level in some neural cells.
CC {ECO:0000269|PubMed:8550568, ECO:0000269|PubMed:8550586}.
CC -!- DEVELOPMENTAL STAGE: Increases at the transition from G1- to S-phase,
CC and the continues to the end of M-phase. Almost disappears when cells
CC reenter the next G1-phase. {ECO:0000269|PubMed:8550586}.
CC -!- INDUCTION: By serum treatment. {ECO:0000269|PubMed:8550586}.
CC -!- DOMAIN: The PDZ-binding motif mediates the interaction with GRIP1.
CC {ECO:0000250}.
CC -!- DOMAIN: The C2 domain mediates pre-localization to the membrane prior
CC to Ca(2+) import and non-selective Ca(2+)-mediated targeting to various
CC cellular membranes.
CC -!- DOMAIN: The PH domain is not a critical determinant of the membrane
CC localization. The PH domain of isoform 4 is necessary and sufficient to
CC inhibit enzyme activity of other PLC-delta enzymes.
CC -!- DOMAIN: The GBA (G-alpha binding and activating) motif mediates binding
CC to the alpha subunits of guanine nucleotide-binding proteins (G
CC proteins). {ECO:0000250|UniProtKB:Q9BRC7}.
CC -!- MISCELLANEOUS: [Isoform 4]: Inactive. {ECO:0000305}.
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DR EMBL; U16655; AAC52346.1; -; mRNA.
DR EMBL; D50455; BAA09046.1; -; mRNA.
DR RefSeq; NP_542419.1; NM_080688.1. [Q62711-1]
DR AlphaFoldDB; Q62711; -.
DR SMR; Q62711; -.
DR STRING; 10116.ENSRNOP00000022234; -.
DR BindingDB; Q62711; -.
DR SwissLipids; SLP:000001069; -.
DR iPTMnet; Q62711; -.
DR PhosphoSitePlus; Q62711; -.
DR PaxDb; Q62711; -.
DR GeneID; 140693; -.
DR KEGG; rno:140693; -.
DR UCSC; RGD:621025; rat. [Q62711-1]
DR CTD; 84812; -.
DR RGD; 621025; Plcd4.
DR VEuPathDB; HostDB:ENSRNOG00000016361; -.
DR eggNOG; KOG0169; Eukaryota.
DR HOGENOM; CLU_002738_0_2_1; -.
DR InParanoid; Q62711; -.
DR OrthoDB; 368239at2759; -.
DR PhylomeDB; Q62711; -.
DR BRENDA; 3.1.4.11; 5301.
DR Reactome; R-RNO-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR PRO; PR:Q62711; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000016361; Expressed in skeletal muscle tissue and 19 other tissues.
DR ExpressionAtlas; Q62711; baseline and differential.
DR Genevisible; Q62711; RN.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; ISS:UniProtKB.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IDA:RGD.
DR GO; GO:0007340; P:acrosome reaction; ISO:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; TAS:RGD.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:InterPro.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR Gene3D; 3.20.20.190; -; 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; IPR028387; PLC-delta4.
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:SF31; PTHR10336:SF31; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF09279; EF-hand_like; 1.
DR Pfam; PF00169; PH; 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; 3.
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 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cytoplasm; Endoplasmic reticulum; Hydrolase;
KW Lipid degradation; Lipid metabolism; Membrane; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transducer.
FT CHAIN 1..772
FT /note="1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase delta-4"
FT /id="PRO_0000306829"
FT DOMAIN 16..124
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 134..169
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 170..205
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 203..237
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 290..435
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 503..619
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 619..746
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 26..53
FT /note="Substrate binding"
FT /evidence="ECO:0000250"
FT REGION 445..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 213..243
FT /note="GBA"
FT /evidence="ECO:0000250|UniProtKB:Q9BRC7"
FT MOTIF 741..744
FT /note="PDZ-binding"
FT COMPBIAS 468..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 305
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 350
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT BINDING 147
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 149
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 151
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 183
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 185
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 189
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 194
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 306
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 433
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 435
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 532
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 559
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 662
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 686
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 715
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT BINDING 716
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 424..487
FT /note="EQLRGKILVKGKKLRTIEVVESDKEEEELEKDEGSDLDPASAELDMQSQPES
FT QEQASGNKSKNK -> VMKCPMSCLLICVHVLAQAPNSIPESILLPKR (in
FT isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_028507"
FT VAR_SEQ 487
FT /note="K -> KVMKCPMSCLLICVHVLAQAPNSIPESILLP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8550568"
FT /id="VSP_028508"
FT VAR_SEQ 487
FT /note="K -> KAPNSIPESILLP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8550568"
FT /id="VSP_028509"
FT MUTAGEN 36
FT /note="R->G: Only retains weak enzyme activity and
FT abolishes the ability of isoform 4 to act as a negative
FT regulator."
FT /evidence="ECO:0000269|PubMed:9915823"
FT MUTAGEN 714
FT /note="K->E: Abolishes affinity for POPC/POPS in the
FT absence of Ca(2+); when associated with E-718."
FT /evidence="ECO:0000269|PubMed:11706040"
FT MUTAGEN 717
FT /note="S->D: Induces a larger Ca(2+)-dependence."
FT /evidence="ECO:0000269|PubMed:11706040"
FT MUTAGEN 718
FT /note="R->E: Abolishes affinity for POPC/POPS in the
FT absence of Ca(2+); when associated with E-714."
FT /evidence="ECO:0000269|PubMed:11706040"
FT CONFLICT 395
FT /note="M -> ML (in Ref. 2; BAA09046)"
FT /evidence="ECO:0000305"
FT CONFLICT 416
FT /note="Missing (in Ref. 2; BAA09046)"
FT /evidence="ECO:0000305"
FT CONFLICT 425
FT /note="Missing (in Ref. 2; BAA09046)"
FT /evidence="ECO:0000305"
FT CONFLICT 757
FT /note="I -> H (in Ref. 2; BAA09046)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 772 AA; 88967 MW; 5DD56D1D4AA21356 CRC64;
MASQIQKLLT TNQDLLLMQK GTMMRKVRTK SWKKLRYFRL QDDGMTVWHG RHLESISKPT
FSISDVERIR KGQDSELLRY LVEEFPLEQG FTIVFNGRRP NLDLVANSVE EAQTWMRGLQ
LLVDLVARMN YQEQLDQMLR EWFQQADRNQ DSRMSFREAQ RLLLLMNVEM DEEYAFSLFQ
EADVSQSNTL DSEEFVQFYK ALTKRTEIEE LFENFSSDKQ KLTLLEFVDF LREEQKESDH
SSDLALKLID RYEPSENGRL LRVLSKDGFL SYLCSADGNI FNPDCLPIYQ DMTQPLSHYY
INSSHNTYLL GDQFCGQSSV EGYIRALKRG CRCVEVDTWD GPDGEPVVYH GRTLTSRILF
KDVLATLAQY AFQSSDYPLI LSLDNHCTWE QQKTMAHHLI AILGEQLLST TLEEQLIDIM
PSPEQLRGKI LVKGKKLRTI EVVESDKEEE ELEKDEGSDL DPASAELDMQ SQPESQEQAS
GNKSKNKKKF LLQSSTTILC PDLSALVVYL RTAPFCSFTH SKENYHIYDI SSFSESKAKN
LIREAGNEFV QHNARQLCRV YPSGLRTDSS NYNPQEHWNV GCQMVAMNMQ TAGSAMDICD
GLFRQNGGSG YVLKPEFLRD TQSSFNPMKP VSLYKAQILV VQVISGQRLP KVDKTKETTV
VDPLVRVELY GVPEDTKQQE TSYVENNGIN PYWGETFYFQ IQVPELAMLR FVVKDYSRTS
RNNFIGQYTL PWTCMKHGYR HVSLLSKDGT SLHPASIFVY TCMQEDLDMD EP
