ID P4KB1_ARATH Reviewed; 1121 AA.
AC Q9FMJ0; Q9ZPE1;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 159.
DE RecName: Full=Phosphatidylinositol 4-kinase beta 1 {ECO:0000303|PubMed:10026194, ECO:0000303|PubMed:12805633};
DE Short=PI4-kinase beta 1 {ECO:0000303|PubMed:10026194, ECO:0000303|PubMed:12805633};
DE Short=PtdIns-4-kinase beta 1 {ECO:0000303|PubMed:10026194, ECO:0000303|PubMed:12805633};
DE EC=2.7.1.67 {ECO:0000269|PubMed:10026194, ECO:0000269|PubMed:12805633};
DE AltName: Full=Phosphatidylinositol 4-OH kinase beta1 {ECO:0000303|PubMed:10026194, ECO:0000303|PubMed:12805633};
DE Short=AtPI4Kbeta1 {ECO:0000303|PubMed:10026194, ECO:0000303|PubMed:12805633};
DE Short=PI-4Kbeta1 {ECO:0000303|PubMed:10026194, ECO:0000303|PubMed:12805633};
GN Name=PI4KB1 {ECO:0000303|PubMed:10026194, ECO:0000303|PubMed:12805633};
GN Synonyms=PI4K, PI4KBETA1 {ECO:0000303|PubMed:10026194,
GN ECO:0000303|PubMed:12805633};
GN OrderedLocusNames=At5g64070 {ECO:0000312|Araport:AT5G64070};
GN ORFNames=MHJ24.5 {ECO:0000312|EMBL:BAB10275.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, REPEATS,
RP ACTIVITY REGULATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. C24; TISSUE=Hypocotyl;
RX PubMed=10026194; DOI=10.1074/jbc.274.9.5738;
RA Xue H.-W., Pical C., Brearley C., Elge S., Mueller-Roeber B.;
RT "A plant 126-kDa phosphatidylinositol 4-kinase with a novel repeat
RT structure. Cloning and functional expression in baculovirus-infected insect
RT cells.";
RL J. Biol. Chem. 274:5738-5745(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12226484; DOI=10.1104/pp.004770;
RA Mueller-Roeber B., Pical C.;
RT "Inositol phospholipid metabolism in Arabidopsis. Characterized and
RT putative isoforms of inositol phospholipid kinase and phosphoinositide-
RT specific phospholipase C.";
RL Plant Physiol. 130:22-46(2002).
RN [6]
RP ACTIVITY REGULATION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=12805633; DOI=10.1104/pp.103.021758;
RA Stevenson-Paulik J., Love J., Boss W.F.;
RT "Differential regulation of two Arabidopsis type III phosphatidylinositol
RT 4-kinase isoforms. A regulatory role for the pleckstrin homology domain.";
RL Plant Physiol. 132:1053-1064(2003).
RN [7]
RP INTERACTION WITH RABA4B AND CBL1, FUNCTION, DISRUPTION PHENOTYPE, AND
RP SUBCELLULAR LOCATION.
RX PubMed=16567499; DOI=10.1083/jcb.200508116;
RA Preuss M.L., Schmitz A.J., Thole J.M., Bonner H.K.S., Otegui M.S.,
RA Nielsen E.;
RT "A role for the RabA4b effector protein PI-4Kbeta1 in polarized expansion
RT of root hair cells in Arabidopsis thaliana.";
RL J. Cell Biol. 172:991-998(2006).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=16649109; DOI=10.1007/s11103-005-5548-x;
RA Lou Y., Ma H., Lin W.H., Chu Z.Q., Mueller-Roeber B., Xu Z.H., Xue H.W.;
RT "The highly charged region of plant beta-type phosphatidylinositol 4-kinase
RT is involved in membrane targeting and phospholipid binding.";
RL Plant Mol. Biol. 60:729-746(2006).
RN [9]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-449 AND
RP SER-454, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [10]
RP INTERACTION WITH AHK2.
RX PubMed=18642946; DOI=10.1021/pr0703831;
RA Dortay H., Gruhn N., Pfeifer A., Schwerdtner M., Schmuelling T., Heyl A.;
RT "Toward an interaction map of the two-component signaling pathway of
RT Arabidopsis thaliana.";
RL J. Proteome Res. 7:3649-3660(2008).
RN [11]
RP INTERACTION WITH RABA4D, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19208902; DOI=10.1105/tpc.108.060277;
RA Szumlanski A.L., Nielsen E.;
RT "The Rab GTPase RabA4d regulates pollen tube tip growth in Arabidopsis
RT thaliana.";
RL Plant Cell 21:526-544(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-449, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [13]
RP FUNCTION, AND MUTAGENESIS OF LYS-864.
RX PubMed=20603382; DOI=10.1093/mp/ssq031;
RA Ischebeck T., Vu L.H., Jin X., Stenzel I., Loefke C., Heilmann I.;
RT "Functional cooperativity of enzymes of phosphoinositide conversion
RT according to synergistic effects on pectin secretion in tobacco pollen
RT tubes.";
RL Mol. Plant 3:870-881(2010).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21134079; DOI=10.1111/j.1600-0854.2010.01146.x;
RA Kang B.H., Nielsen E., Preuss M.L., Mastronarde D., Staehelin L.A.;
RT "Electron tomography of RabA4b- and PI-4Kbeta1-labeled trans Golgi network
RT compartments in Arabidopsis.";
RL Traffic 12:313-329(2011).
RN [15]
RP FUNCTION.
RX PubMed=22318862; DOI=10.1093/pcp/pcs011;
RA Delage E., Ruelland E., Guillas I., Zachowski A., Puyaubert J.;
RT "Arabidopsis type-III phosphatidylinositol 4-kinases beta1 and beta2 are
RT upstream of the phospholipase C pathway triggered by cold exposure.";
RL Plant Cell Physiol. 53:565-576(2012).
RN [16]
RP REVIEW.
RX PubMed=22899063; DOI=10.4161/psb.21305;
RA Delage E., Ruelland E., Zachowski A., Puyaubert J.;
RT "Eat in or take away? How phosphatidylinositol 4-kinases feed the
RT phospholipase C pathway with substrate.";
RL Plant Signal. Behav. 7:1197-1199(2012).
CC -!- FUNCTION: Acts on phosphatidylinositol (PtdIns) in the first committed
CC step in the production of the second messenger inositol-1,4,5-
CC trisphosphate. Necessary for proper organization of the trans-Golgi
CC network (TGN) and post-Golgi secretion in root hairs. Together with
CC PI4KB2, required during polarized root hair expansion and pollen tube
CC elongation. Functions redundantly with PI4KB2 upstream of the cold
CC response phosphoinositide-dependent phospholipase C (PI-PLC) pathway.
CC {ECO:0000269|PubMed:10026194, ECO:0000269|PubMed:16567499,
CC ECO:0000269|PubMed:19208902, ECO:0000269|PubMed:20603382,
CC ECO:0000269|PubMed:21134079, ECO:0000269|PubMed:22318862}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP +
CC H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216;
CC EC=2.7.1.67; Evidence={ECO:0000269|PubMed:10026194,
CC ECO:0000269|PubMed:12805633};
CC -!- ACTIVITY REGULATION: Stimulated by phosphatidylinositol 4-phosphate
CC (PtdIns4P). Slightly repressed by phosphatidyl-choline (PtdCho),
CC wortmannin and adenosine. {ECO:0000269|PubMed:10026194,
CC ECO:0000269|PubMed:12805633}.
CC -!- SUBUNIT: Interacts with AHK2, CBL1 and RABA4D.
CC {ECO:0000269|PubMed:16567499, ECO:0000269|PubMed:18642946,
CC ECO:0000269|PubMed:19208902}.
CC -!- INTERACTION:
CC Q9FMJ0; Q9C5U2: AHK2; NbExp=2; IntAct=EBI-1807432, EBI-1100634;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16649109,
CC ECO:0000269|PubMed:21134079}. Golgi apparatus, trans-Golgi network
CC {ECO:0000269|PubMed:16567499, ECO:0000269|PubMed:21134079}. Cytoplasmic
CC vesicle membrane {ECO:0000269|PubMed:12805633}; Peripheral membrane
CC protein {ECO:0000269|PubMed:12805633}; Cytoplasmic side
CC {ECO:0000269|PubMed:12805633, ECO:0000269|PubMed:18433157}.
CC Note=Associated to tip-localized membranes in growing root hairs.
CC {ECO:0000269|PubMed:16567499}.
CC -!- TISSUE SPECIFICITY: Expressed constitutively in leaves, roots, flowers,
CC and stems. {ECO:0000269|PubMed:10026194}.
CC -!- DOMAIN: The PPC (Plant PI4K Charged) region is involved in membrane
CC targeting and phospholipid binding. {ECO:0000269|PubMed:16649109}.
CC -!- DISRUPTION PHENOTYPE: When associated with PI4KB2 disruption: aberrant
CC root hair morphologies, and short and wavy pollen tubes.
CC {ECO:0000269|PubMed:16567499, ECO:0000269|PubMed:19208902}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000305}.
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DR EMBL; AJ002685; CAB37928.1; -; Genomic_DNA.
DR EMBL; AB008266; BAB10275.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97836.1; -; Genomic_DNA.
DR EMBL; AF462854; AAL58940.1; -; mRNA.
DR EMBL; AY139795; AAM98101.1; -; mRNA.
DR PIR; T52631; T52631.
DR RefSeq; NP_201212.1; NM_125803.4.
DR AlphaFoldDB; Q9FMJ0; -.
DR SMR; Q9FMJ0; -.
DR BioGRID; 21770; 5.
DR IntAct; Q9FMJ0; 1.
DR STRING; 3702.Q9FMJ0; -.
DR iPTMnet; Q9FMJ0; -.
DR PaxDb; 3702-AT5G64070-1; -.
DR ProteomicsDB; 250979; -.
DR EnsemblPlants; AT5G64070.1; AT5G64070.1; AT5G64070.
DR GeneID; 836528; -.
DR Gramene; AT5G64070.1; AT5G64070.1; AT5G64070.
DR KEGG; ath:AT5G64070; -.
DR Araport; AT5G64070; -.
DR TAIR; AT5G64070; PI-4KBETA1.
DR eggNOG; KOG0903; Eukaryota.
DR HOGENOM; CLU_002446_4_1_1; -.
DR InParanoid; Q9FMJ0; -.
DR OMA; AYPLWTV; -.
DR OrthoDB; 147843at2759; -.
DR PhylomeDB; Q9FMJ0; -.
DR BioCyc; ARA:AT5G64070-MONOMER; -.
DR PRO; PR:Q9FMJ0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FMJ0; baseline and differential.
DR Genevisible; Q9FMJ0; AT.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0035619; C:root hair tip; IDA:TAIR.
DR GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; IDA:UniProtKB.
DR GO; GO:0043424; F:protein histidine kinase binding; IPI:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009860; P:pollen tube growth; IGI:TAIR.
DR GO; GO:0048768; P:root hair cell tip growth; IGI:TAIR.
DR CDD; cd05168; PI4Kc_III_beta; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR049160; PI4KB-PIK1_PIK.
DR InterPro; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048:SF22; PHOSPHATIDYLINOSITOL 4-KINASE BETA; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF21245; PI4KB-PIK1_PIK; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasmic vesicle; Developmental protein; Golgi apparatus;
KW Kinase; Membrane; Phosphoprotein; Reference proteome; Repeat; Transferase.
FT CHAIN 1..1121
FT /note="Phosphatidylinositol 4-kinase beta 1"
FT /id="PRO_0000398594"
FT DOMAIN 1..143
FT /note="PIK helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT REPEAT 212..231
FT /note="1"
FT /evidence="ECO:0000269|PubMed:10026194"
FT REPEAT 244..263
FT /note="2"
FT /evidence="ECO:0000269|PubMed:10026194"
FT REPEAT 266..285
FT /note="3"
FT /evidence="ECO:0000269|PubMed:10026194"
FT REPEAT 288..306
FT /note="4"
FT /evidence="ECO:0000269|PubMed:10026194"
FT REPEAT 309..328
FT /note="5"
FT /evidence="ECO:0000269|PubMed:10026194"
FT REPEAT 331..350
FT /note="6"
FT /evidence="ECO:0000269|PubMed:10026194"
FT REPEAT 353..372
FT /note="7"
FT /evidence="ECO:0000269|PubMed:10026194"
FT REPEAT 380..398
FT /note="8"
FT /evidence="ECO:0000269|PubMed:10026194"
FT REPEAT 420..438
FT /note="9"
FT /evidence="ECO:0000269|PubMed:10026194"
FT REPEAT 454..472
FT /note="10"
FT /evidence="ECO:0000269|PubMed:10026194"
FT REPEAT 489..508
FT /note="11"
FT /evidence="ECO:0000269|PubMed:10026194"
FT DOMAIN 835..1106
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 187..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..508
FT /note="11 X 20 AA approximate repeats (PPC)"
FT REGION 343..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..847
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 969..977
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 988..1012
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT COMPBIAS 187..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 449
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT MUTAGEN 864
FT /note="K->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:20603382"
FT CONFLICT 116..117
FT /note="VH -> AS (in Ref. 1; CAB37928)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1121 AA; 126375 MW; 686C994E431BBDB2 CRC64;
MPMGRFLSLV RGDSAESPRE ITSQSNIIGD TGSNGWLIRF FDSAFFCEWI AVSYLYKHPH
AGVRDYLCNR MYTLPLSGIE SYLFQICYMM VHKPSPSLDK FVIDICGKSL KIALKVHWFL
LAELEDADDN EGISRIQEKC QIAATLMGEW SPLMRPQNEV STPGSKNQVL NRLLSSKQKL
FSLKLSPPTQ KSLSFSPSPG TNVQDDGSQL PAEDNKIFKK LIPSPKVRDA LMFRKSADKD
DEESEKEGFF KRLLRDSKGE GDEPIPNSEG FFKRLLKDNK SEDEDITNSS EGFFKRLLSS
KGESEELTSS SDGLFKRLLR DNKGDEEELG ANSDSFFKRL LRESKNEDEE SNPNSEGFFK
KLFRDSKPED DKVPKEVDDE DKDGFLKKLF REKNDDKRHG SEKNEANGTV YADKKSGEED
EREGFFKKFF KEKSDDKKDI VKVDDGNESE GDESPEFSLF KRLFRIHPED AKPTSENENS
SNGLVESSPG TENFFRKLFR DRDQSVEDSE LFGSKKHKEK RPGSPKQRDD TPSGKPPLPN
NTASQFRKGA YHESLEFVQA LCETSYGLVD IFPIEDRKIG LRESLAEINF HLSEAEITGG
ICFPMGRGVF RVVHIPEDEC ILLNSREKAP YMISVEVLKA ETPSAKESSN SQKLSKGGIP
LANGDAFLQK PPPWAYPLWT TQEVYRNSAD RMSLSTAQAI DQAMTPKSEV KVKLVNVSLS
VEDRTSALES FGDPIDDVLG EAPRTGLNND LEWVRVVVTA DPGLRMESIP DPSVPRKKEH
RRVPSTVAME EVRAAAAKGE APPGLPLKGA GQDSSDAQPR ANGGMLKEGD ALSGELWEGK
RDRIRKASIY GKLPGWDLRS IIVKSGDDCR QEHLAVQLIS HFYDIFQEAG LPLWLRPYEV
LVTSSYTALI ETIPDTASIH SIKSRYPNIT SLRDFFVAKY KENSPSFKLA QRNFVESMAG
YSLVCYLLQV KDRHNGNLLL DEEGHIIHID FGFMLSNSPG GVNFESAPFK LTRELLEVMD
SDADGVPSEF FDYFKVLCIQ GFLTCRKHAE RIILLVEMLQ DSGFPCFKGG PRTIQNLRKR
FHLSLTEEQC VSLVLSLISS SLDAWRTRQY DYYQRVLNGI L
//
