CDPK6_ARATH
ID CDPK6_ARATH Reviewed; 544 AA.
AC Q38872; Q39014;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Calcium-dependent protein kinase 6;
DE EC=2.7.11.1;
DE AltName: Full=Calcium-dependent protein kinase isoform CDPK3;
DE Short=AtCDPK3;
DE AltName: Full=Calmodulin-domain protein kinase CDPK isoform 6;
GN Name=CPK6; Synonyms=CDPK3; OrderedLocusNames=At2g17290; ORFNames=F5J6.13;
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 [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=8756605; DOI=10.1007/bf00021802;
RA Hrabak E.M., Dickmann L.J., Satterlee J.S., Sussman M.R.;
RT "Characterization of eight new members of the calmodulin-like domain
RT protein kinase gene family from Arabidopsis thaliana.";
RL Plant Mol. Biol. 31:405-412(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 NUCLEOTIDE SEQUENCE [MRNA] OF 26-544.
RC STRAIN=cv. Columbia;
RX PubMed=7972512; DOI=10.1104/pp.105.4.1461;
RA Urao T., Katagiri T., Mizoguchi T., Yamaguchi-Shinozaki K., Hayashida N.,
RA Shinozaki K.;
RT "An Arabidopsis thaliana cDNA encoding Ca(2+)-dependent protein kinase.";
RL Plant Physiol. 105:1461-1462(1994).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RA Harmon A.C., Gribskov M., Gubrium E., Harper J.F.;
RT "The CDPK superfamily of protein kinases.";
RL New Phytol. 151:175-183(2001).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12068094; DOI=10.1104/pp.005645;
RA Cheng S.-H., Willmann M.R., Chen H.-C., Sheen J.;
RT "Calcium signaling through protein kinases. The Arabidopsis calcium-
RT dependent protein kinase gene family.";
RL Plant Physiol. 129:469-485(2002).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12805596; DOI=10.1104/pp.102.011999;
RA Hrabak E.M., Chan C.W.M., Gribskov M., Harper J.F., Choi J.H., Halford N.,
RA Kudla J., Luan S., Nimmo H.G., Sussman M.R., Thomas M., Walker-Simmons K.,
RA Zhu J.-K., Harmon A.C.;
RT "The Arabidopsis CDPK-SnRK superfamily of protein kinases.";
RL Plant Physiol. 132:666-680(2003).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17032064; DOI=10.1371/journal.pbio.0040327;
RA Mori I.C., Murata Y., Yang Y., Munemasa S., Wang Y.-F., Andreoli S.,
RA Tiriac H., Alonso J.M., Harper J.F., Ecker J.R., Kwak J.M., Schroeder J.I.;
RT "CDPKs CPK6 and CPK3 function in ABA regulation of guard cell S-type
RT anion- and Ca(2+)-permeable channels and stomatal closure.";
RL PLoS Biol. 4:E327-E327(2006).
RN [10]
RP MYRISTOYLATION AT GLY-2, AND SUBCELLULAR LOCATION.
RX PubMed=19029837; DOI=10.4161/cc.7.23.7176;
RA Benetka W., Mehlmer N., Maurer-Stroh S., Sammer M., Koranda M.,
RA Neumueller R., Betschinger J., Knoblich J.A., Teige M., Eisenhaber F.;
RT "Experimental testing of predicted myristoylation targets involved in
RT asymmetric cell division and calcium-dependent signalling.";
RL Cell Cycle 7:3709-3719(2008).
RN [11]
RP INTERACTION WITH SLAC1.
RX PubMed=20385816; DOI=10.1073/pnas.0912030107;
RA Geiger D., Scherzer S., Mumm P., Marten I., Ache P., Matschi S., Liese A.,
RA Wellmann C., Al-Rasheid K.A.S., Grill E., Romeis T., Hedrich R.;
RT "Guard cell anion channel SLAC1 is regulated by CDPK protein kinases with
RT distinct Ca2+ affinities.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:8023-8028(2010).
RN [12]
RP FUNCTION, INTERACTION WITH FD, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY$.
RX PubMed=25661797; DOI=10.1038/srep08341;
RA Kawamoto N., Sasabe M., Endo M., Machida Y., Araki T.;
RT "Calcium-dependent protein kinases responsible for the phosphorylation of a
RT bZIP transcription factor FD crucial for the florigen complex formation.";
RL Sci. Rep. 5:8341-8341(2015).
CC -!- FUNCTION: May play a role in signal transduction pathways that involve
CC calcium as a second messenger. Functions in abscisic acid (ABA)
CC regulation of guard cell S-type anion- and Ca(2+)-permeable channels
CC and stomatal closure (PubMed:17032064). Phosphorylates FD
CC (PubMed:25661797). {ECO:0000269|PubMed:17032064,
CC ECO:0000269|PubMed:25661797}.
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 -!- 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;
CC -!- ACTIVITY REGULATION: Activated by calcium. Autophosphorylation may play
CC an important role in the regulation of the kinase activity (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SLAC1 (PubMed:20385816). Interacts with FD
CC (PubMed:25661797). {ECO:0000269|PubMed:20385816,
CC ECO:0000269|PubMed:25661797}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19029837};
CC Lipid-anchor {ECO:0000269|PubMed:19029837}. Nucleus
CC {ECO:0000269|PubMed:25661797}.
CC -!- TISSUE SPECIFICITY: Expressed in both guard cells and mesophyll cells
CC (PubMed:17032064). Expressed in the shoot apical meristem
CC (PubMed:25661797). {ECO:0000269|PubMed:17032064,
CC ECO:0000269|PubMed:25661797}.
CC -!- DOMAIN: There are 3 contiguous domains conserved in the CDPK subfamily:
CC a kinase domain, an autoinhibitory (junction) domain and a calmodulin-
CC like domain. The autoinhibitory domain (349-379) inactivates kinase
CC activity under calcium-free conditions (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDPK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA05918.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U31835; AAB03246.1; -; mRNA.
DR EMBL; CP002685; AEC06609.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61864.1; -; Genomic_DNA.
DR EMBL; AY140007; AAM98149.1; -; mRNA.
DR EMBL; BT002600; AAO00960.1; -; mRNA.
DR EMBL; D28582; BAA05918.1; ALT_SEQ; mRNA.
DR PIR; D84550; D84550.
DR RefSeq; NP_001324056.1; NM_001335545.1.
DR RefSeq; NP_565411.2; NM_127284.3.
DR AlphaFoldDB; Q38872; -.
DR SMR; Q38872; -.
DR BioGRID; 1592; 7.
DR DIP; DIP-59319N; -.
DR IntAct; Q38872; 3.
DR STRING; 3702.AT2G17290.1; -.
DR iPTMnet; Q38872; -.
DR PaxDb; Q38872; -.
DR PRIDE; Q38872; -.
DR ProteomicsDB; 220467; -.
DR EnsemblPlants; AT2G17290.1; AT2G17290.1; AT2G17290.
DR EnsemblPlants; AT2G17290.2; AT2G17290.2; AT2G17290.
DR GeneID; 816235; -.
DR Gramene; AT2G17290.1; AT2G17290.1; AT2G17290.
DR Gramene; AT2G17290.2; AT2G17290.2; AT2G17290.
DR KEGG; ath:AT2G17290; -.
DR Araport; AT2G17290; -.
DR TAIR; locus:2827528; AT2G17290.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_000288_37_4_1; -.
DR InParanoid; Q38872; -.
DR OMA; PIMRRNV; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; Q38872; -.
DR PRO; PR:Q38872; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q38872; baseline and differential.
DR Genevisible; Q38872; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016020; C:membrane; TAS:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0009931; F:calcium-dependent protein serine/threonine kinase activity; IDA:TAIR.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
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:0009738; P:abscisic acid-activated signaling pathway; IMP: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:0046777; P:protein autophosphorylation; HDA:TAIR.
DR GO; GO:0010359; P:regulation of anion channel activity; IMP:TAIR.
DR GO; GO:0010119; P:regulation of stomatal movement; IMP:TAIR.
DR GO; GO:1902456; P:regulation of stomatal opening; IMP:TAIR.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13499; EF-hand_7; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00054; EFh; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00018; EF_HAND_1; 4.
DR PROSITE; PS50222; EF_HAND_2; 4.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Calcium; Cell membrane; Kinase; Lipoprotein; Membrane;
KW Metal-binding; Myristate; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..544
FT /note="Calcium-dependent protein kinase 6"
FT /id="PRO_0000363332"
FT DOMAIN 85..343
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 386..421
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 422..457
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 458..493
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 497..527
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..379
FT /note="Autoinhibitory domain"
FT /evidence="ECO:0000250"
FT COMPBIAS 23..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 209
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 91..99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 399
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 401
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 403
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 410
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 435
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 437
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 439
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 441
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 446
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 471
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 473
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 475
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 477
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 482
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 505
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 507
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 509
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 511
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 516
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FKW4"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:19029837"
FT CONFLICT 163
FT /note="M -> I (in Ref. 5; BAA05918)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="A -> P (in Ref. 5; BAA05918)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="D -> A (in Ref. 5; BAA05918)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="R -> K (in Ref. 5; BAA05918)"
FT /evidence="ECO:0000305"
FT CONFLICT 423..424
FT /note="KD -> ES (in Ref. 5; BAA05918)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="R -> H (in Ref. 5; BAA05918)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="E -> D (in Ref. 5; BAA05918)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 544 AA; 61111 MW; EA4F047BEE985E4F CRC64;
MGNSCRGSFK DKIYEGNHSR PEENSKSTTT TVSSVHSPTT DQDFSKQNTN PALVIPVKEP
IMRRNVDNQS YYVLGHKTPN IRDLYTLSRK LGQGQFGTTY LCTDIATGVD YACKSISKRK
LISKEDVEDV RREIQIMHHL AGHKNIVTIK GAYEDPLYVH IVMELCAGGE LFDRIIHRGH
YSERKAAELT KIIVGVVEAC HSLGVMHRDL KPENFLLVNK DDDFSLKAID FGLSVFFKPG
QIFKDVVGSP YYVAPEVLLK HYGPEADVWT AGVILYILLS GVPPFWAETQ QGIFDAVLKG
YIDFDTDPWP VISDSAKDLI RKMLCSSPSE RLTAHEVLRH PWICENGVAP DRALDPAVLS
RLKQFSAMNK LKKMALKVIA ESLSEEEIAG LRAMFEAMDT DNSGAITFDE LKAGLRRYGS
TLKDTEIRDL MEAADVDNSG TIDYSEFIAA TIHLNKLERE EHLVSAFQYF DKDGSGYITI
DELQQSCIEH GMTDVFLEDI IKEVDQDNDG RIDYEEFVAM MQKGNAGVGR RTMKNSLNIS
MRDV
