PDPK1_ARATH
ID PDPK1_ARATH Reviewed; 491 AA.
AC Q9XF67; Q9LZ74;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=3-phosphoinositide-dependent protein kinase 1;
DE Short=AtPDK1;
DE EC=2.7.11.1;
GN Name=PDPK1; Synonyms=PDK1; OrderedLocusNames=At5g04510;
GN ORFNames=T32M21.110;
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 FUNCTION, AND LIPID-BINDING.
RX PubMed=10371193; DOI=10.1016/s0014-5793(99)00556-6;
RA Deak M., Casamayor A., Currie R.A., Downes C.P., Alessi D.R.;
RT "Characterisation of a plant 3-phosphoinositide-dependent protein kinase-1
RT homologue which contains a pleckstrin homology domain.";
RL FEBS Lett. 451:220-226(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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 REVIEW.
RX PubMed=13678909; DOI=10.1016/s1360-1385(03)00188-2;
RA Boegre L., Okresz L., Henriques R., Anthony R.G.;
RT "Growth signalling pathways in Arabidopsis and the AGC protein kinases.";
RL Trends Plant Sci. 8:424-431(2003).
RN [6]
RP CATALYTIC ACTIVITY, AND AUTOPHOSPHORYLATION.
RX PubMed=15358101; DOI=10.1016/j.bbrc.2004.07.031;
RA Silber J., Antal T.L., Gammeltoft S., Rasmussen T.E.;
RT "Phosphoinositide-dependent kinase-1 orthologues from five eukaryotes are
RT activated by the hydrophobic motif in AGC kinases.";
RL Biochem. Biophys. Res. Commun. 321:823-827(2004).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH D6PK AND OXI1.
RX PubMed=14749726; DOI=10.1038/sj.emboj.7600068;
RA Anthony R.G., Henriques R., Helfer A., Meszaros T., Rios G., Testerink C.,
RA Munnik T., Deak M., Koncz C., Boegre L.;
RT "A protein kinase target of a PDK1 signalling pathway is involved in root
RT hair growth in Arabidopsis.";
RL EMBO J. 23:572-581(2004).
RN [8]
RP PHOSPHORYLATION AT SER-177; SER-276; SER-382 AND THR-211, IDENTIFICATION BY
RP MASS SPECTROMETRY, AND MUTAGENESIS OF ASP-167; THR-176; SER-177; THR-211;
RP SER-276 AND SER-382.
RX PubMed=16125835; DOI=10.1016/j.biochi.2005.07.005;
RA Otterhag L., Gustavsson N., Alsterfjord M., Pical C., Lehrach H., Gobom J.,
RA Sommarin M.;
RT "Arabidopsis PDK1: identification of sites important for activity and
RT downstream phosphorylation of S6 kinase.";
RL Biochimie 88:11-21(2006).
RN [9]
RP FUNCTION, AND INTERACTION WITH AGC1-5 AND AGC1-7.
RX PubMed=16973627; DOI=10.1074/jbc.m605167200;
RA Zegzouti H., Li W., Lorenz T.C., Xie M., Payne C.T., Smith K., Glenny S.,
RA Payne G.S., Christensen S.K.;
RT "Structural and functional insights into the regulation of Arabidopsis AGC
RT VIIIa kinases.";
RL J. Biol. Chem. 281:35520-35530(2006).
RN [10]
RP ACTIVITY REGULATION.
RX PubMed=17040918; DOI=10.1074/jbc.m607341200;
RA Anthony R.G., Khan S., Costa J., Pais M.S., Boegre L.;
RT "The Arabidopsis protein kinase PTI1-2 is activated by convergent
RT phosphatidic acid and oxidative stress signaling pathways downstream of
RT PDK1 and OXI1.";
RL J. Biol. Chem. 281:37536-37546(2006).
RN [11]
RP FUNCTION, AND INTERACTION WITH PID.
RX PubMed=16601102; DOI=10.1073/pnas.0510283103;
RA Zegzouti H., Anthony R.G., Jahchan N., Boegre L., Christensen S.K.;
RT "Phosphorylation and activation of PINOID by the phospholipid signaling
RT kinase 3-phosphoinositide-dependent protein kinase 1 (PDK1) in
RT Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6404-6409(2006).
RN [12]
RP FUNCTION.
RX PubMed=16377759; DOI=10.1105/tpc.105.035931;
RA Mahfouz M.M., Kim S., Delauney A.J., Verma D.P.;
RT "Arabidopsis TARGET OF RAPAMYCIN interacts with RAPTOR, which regulates the
RT activity of S6 kinase in response to osmotic stress signals.";
RL Plant Cell 18:477-490(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337, 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).
CC -!- FUNCTION: May couple lipid signals to the activation-loop
CC phosphorylation of several protein kinases of the so-called AGC kinase
CC family. Interacts via its pleckstrin homology domain with phosphatidic
CC acid, PtdIns3P and PtdIns(3,4)P2 and to a lesser extent with
CC PtdIns(4,5)P2 and PtdIns4P. May play a general role in signaling
CC processes controlling the pathogen/stress response, polar auxin
CC transport and development. Transphosphorylates the AGC protein kinases
CC OXI1/AGC2-1, PK1/S6K1, PK19/S6K2 and PID resulting in their activation.
CC {ECO:0000269|PubMed:10371193, ECO:0000269|PubMed:14749726,
CC ECO:0000269|PubMed:16377759, ECO:0000269|PubMed:16601102,
CC ECO:0000269|PubMed:16973627}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:15358101};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:15358101};
CC -!- ACTIVITY REGULATION: Activated by phosphatidic acid (PA) and in
CC response to the fungal elicitor xylanase.
CC {ECO:0000269|PubMed:17040918}.
CC -!- SUBUNIT: Interacts with AGC1-5 and AGC1-7 (PubMed:16973627). Interacts
CC with the C-terminal PIF domain of the protein kinases D6PK/AGC1-1,
CC OXI1/AGC2-1 and PID (PubMed:14749726, PubMed:16601102).
CC {ECO:0000269|PubMed:14749726, ECO:0000269|PubMed:16601102,
CC ECO:0000269|PubMed:16973627}.
CC -!- INTERACTION:
CC Q9XF67; Q9LTW5: AGC1-5; NbExp=3; IntAct=EBI-1103587, EBI-1103747;
CC Q9XF67; Q1PFB9: AGC1-7; NbExp=2; IntAct=EBI-1103587, EBI-1103730;
CC Q9XF67; Q9FG74: D6PK; NbExp=2; IntAct=EBI-1103587, EBI-1103570;
CC Q9XF67; Q9SUA3: D6PKL1; NbExp=3; IntAct=EBI-1103587, EBI-1103605;
CC Q9XF67; Q39183: D6PKL2; NbExp=4; IntAct=EBI-1103587, EBI-1103628;
CC Q9XF67; Q05999: D6PKL3; NbExp=2; IntAct=EBI-1103587, EBI-1103648;
CC Q9XF67; Q9SJM3: KIPK2; NbExp=2; IntAct=EBI-1103587, EBI-1103882;
CC Q9XF67; Q9LUK3: MUD12.10; NbExp=2; IntAct=EBI-1103587, EBI-1103691;
CC Q9XF67; O64682: PID; NbExp=3; IntAct=EBI-1103587, EBI-1393382;
CC Q9XF67; Q64FQ2: PID2; NbExp=2; IntAct=EBI-1103587, EBI-1103769;
CC Q9XF67; F4I4F2: RHS3; NbExp=2; IntAct=EBI-1103587, EBI-1103713;
CC Q9XF67; Q9M1P3: T18B22.10; NbExp=2; IntAct=EBI-1103587, EBI-1103792;
CC Q9XF67; Q8RY37; NbExp=2; IntAct=EBI-1103587, EBI-1103670;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Note=Membrane-associated
CC after cell stimulation. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9XF67-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:14749726}.
CC -!- DOMAIN: The PH domain is responsible for the interaction with the 3-
CC phosphoinositides. The activation loop within the kinase domain is the
CC target of phosphorylation. The PIF-binding region in the kinase domain
CC of PDK1 acts as a docking site, enabling it to interact with and
CC enhance the phosphorylation of substrates containing the PIF motif.
CC -!- DOMAIN: The PIF-pocket is a small lobe in the catalytic domain required
CC by the enzyme for the binding to the hydrophobic motif of its
CC substrates. It is an allosteric regulatory site that can accommodate
CC small compounds acting as allosteric inhibitors.
CC {ECO:0000250|UniProtKB:O15530}.
CC -!- PTM: Phosphorylation on Thr-211 in the activation loop is required for
CC full activity. PDK1 itself can autophosphorylate Thr-211, leading to
CC its own activation. {ECO:0000269|PubMed:16125835}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PDPK1 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB85557.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF132742; AAD37165.1; -; mRNA.
DR EMBL; AL162875; CAB85557.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED90755.1; -; Genomic_DNA.
DR EMBL; AF360326; AAK26036.1; -; mRNA.
DR EMBL; AY056336; AAL07185.1; -; mRNA.
DR PIR; T48447; T48447.
DR RefSeq; NP_568138.1; NM_120533.5. [Q9XF67-1]
DR AlphaFoldDB; Q9XF67; -.
DR SMR; Q9XF67; -.
DR BioGRID; 15609; 7.
DR DIP; DIP-39596N; -.
DR ELM; Q9XF67; -.
DR IntAct; Q9XF67; 16.
DR STRING; 3702.AT5G04510.1; -.
DR iPTMnet; Q9XF67; -.
DR PaxDb; Q9XF67; -.
DR PRIDE; Q9XF67; -.
DR ProteomicsDB; 251347; -. [Q9XF67-1]
DR DNASU; 830330; -.
DR EnsemblPlants; AT5G04510.1; AT5G04510.1; AT5G04510. [Q9XF67-1]
DR GeneID; 830330; -.
DR Gramene; AT5G04510.1; AT5G04510.1; AT5G04510. [Q9XF67-1]
DR KEGG; ath:AT5G04510; -.
DR Araport; AT5G04510; -.
DR TAIR; locus:2184357; AT5G04510.
DR eggNOG; KOG0592; Eukaryota.
DR HOGENOM; CLU_000288_63_9_1; -.
DR InParanoid; Q9XF67; -.
DR OrthoDB; 1157543at2759; -.
DR PhylomeDB; Q9XF67; -.
DR PRO; PR:Q9XF67; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9XF67; baseline and differential.
DR Genevisible; Q9XF67; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; ISS:TAIR.
DR GO; GO:0070300; F:phosphatidic acid binding; IDA:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:TAIR.
DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; HDA:TAIR.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:TAIR.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR CDD; cd05581; STKc_PDK1; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033931; PDK1-typ_PH.
DR InterPro; IPR039046; PDPK1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF14593; PH_3; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..491
FT /note="3-phosphoinositide-dependent protein kinase 1"
FT /id="PRO_0000399902"
FT DOMAIN 44..311
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 386..491
FT /note="PH"
FT REGION 75..119
FT /note="PIF-pocket"
FT /evidence="ECO:0000250|UniProtKB:O15530"
FT REGION 77..112
FT /note="PIF-binding"
FT /evidence="ECO:0000255"
FT REGION 185..222
FT /note="Activation loop"
FT REGION 321..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 54..56
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O15530"
FT BINDING 73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O15530"
FT BINDING 122..124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O15530"
FT BINDING 128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O15530"
FT BINDING 171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O15530"
FT BINDING 185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O15530"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16125835"
FT MOD_RES 211
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:16125835"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16125835"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16125835"
FT MUTAGEN 167
FT /note="D->A: Abolishes autophosphorylation."
FT /evidence="ECO:0000269|PubMed:16125835"
FT MUTAGEN 176
FT /note="T->A: Strongly reduces autophosphorylation."
FT /evidence="ECO:0000269|PubMed:16125835"
FT MUTAGEN 177
FT /note="S->A: Reduces autophosphorylation."
FT /evidence="ECO:0000269|PubMed:16125835"
FT MUTAGEN 211
FT /note="T->A: Strongly reduces autophosphorylation."
FT /evidence="ECO:0000269|PubMed:16125835"
FT MUTAGEN 276
FT /note="S->A: Abolishes autophosphorylation."
FT /evidence="ECO:0000269|PubMed:16125835"
FT MUTAGEN 382
FT /note="S->A: Slightly reduces autophosphorylation."
FT /evidence="ECO:0000269|PubMed:16125835"
SQ SEQUENCE 491 AA; 54711 MW; 2319EE69CDB5CB38 CRC64;
MLAMEKEFDS KLVLQGNSSN GANVSRSKSF SFKAPQENFT SHDFEFGKIY GVGSYSKVVR
AKKKETGTVY ALKIMDKKFI TKENKTAYVK LERIVLDQLE HPGIIKLYFT FQDTSSLYMA
LESCEGGELF DQITRKGRLS EDEARFYTAE VVDALEYIHS MGLIHRDIKP ENLLLTSDGH
IKIADFGSVK PMQDSQITVL PNAASDDKAC TFVGTAAYVP PEVLNSSPAT FGNDLWALGC
TLYQMLSGTS PFKDASEWLI FQRIIARDIK FPNHFSEAAR DLIDRLLDTE PSRRPGAGSE
GYVALKRHPF FNGVDWKNLR SQTPPKLAPD PASQTASPER DDTHGSPWNL THIGDSLATQ
NEGHSAPPTS SESSGSITRL ASIDSFDSRW QQFLEPGESV LMISAVKKLQ KITSKKVQLI
LTNKPKLIYV DPSKLVVKGN IIWSDNSNDL NVVVTSPSHF KICTPKKVLS FEDAKQRASV
WKKAIETLQN R
