CDPKB_ARATH
ID CDPKB_ARATH Reviewed; 495 AA.
AC Q39016; Q949P0; Q9LQH7;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Calcium-dependent protein kinase 11;
DE EC=2.7.11.1;
DE AltName: Full=Calcium-dependent protein kinase isoform CDPK2;
DE Short=AtCDPK2;
GN Name=CPK11; Synonyms=CDPK2; OrderedLocusNames=At1g35670; ORFNames=F15O4.8;
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], FUNCTION, AND INDUCTION.
RX PubMed=8078458; DOI=10.1007/bf00286684;
RA Urao T., Katagiri T., Mizoguchi T., Yamaguchi-Shinozaki K., Hayashida N.,
RA Shinozaki K.;
RT "Two genes that encode Ca(2+)-dependent protein kinases are induced by
RT drought and high-salt stresses in Arabidopsis thaliana.";
RL Mol. Gen. Genet. 244:331-340(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 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 [6]
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 [7]
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 [8]
RP INTERACTION WITH DI19, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-150;
RP ASP-171 AND PHE-306.
RX PubMed=16438971; DOI=10.1016/j.febslet.2006.01.013;
RA Rodriguez Milla M.A., Uno Y., Chang I.-F., Townsend J., Maher E.A.,
RA Quilici D., Cushman J.C.;
RT "A novel yeast two-hybrid approach to identify CDPK substrates:
RT characterization of the interaction between AtCPK11 and AtDi19, a nuclear
RT zinc finger protein.";
RL FEBS Lett. 580:904-911(2006).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17921317; DOI=10.1105/tpc.107.050666;
RA Zhu S.-Y., Yu X.-C., Wang X.-J., Zhao R., Li Y., Fan R.-C., Shang Y.,
RA Du S.-Y., Wang X.-F., Wu F.-Q., Xu Y.-H., Zhang X.-Y., Zhang D.-P.;
RT "Two calcium-dependent protein kinases, CPK4 and CPK11, regulate abscisic
RT acid signal transduction in Arabidopsis.";
RL Plant Cell 19:3019-3036(2007).
CC -!- FUNCTION: May play a role in signal transduction pathways that involve
CC calcium as a second messenger. Functions as regulator of the calcium-
CC mediated abscisic acid (ABA) signaling pathway. Phosphorylates ABA-
CC responsive transcription factors ABF1 and ABF4 in vitro.
CC {ECO:0000269|PubMed:17921317, ECO:0000269|PubMed:8078458}.
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 Di19. {ECO:0000269|PubMed:16438971}.
CC -!- INTERACTION:
CC Q39016; Q9ZSK4: ADF3; NbExp=5; IntAct=EBI-979321, EBI-2009725;
CC Q39016; Q9C944: At1g52740; NbExp=9; IntAct=EBI-979321, EBI-1537419;
CC Q39016; Q27GK5: At3g26510; NbExp=5; IntAct=EBI-979321, EBI-2297208;
CC Q39016; Q940C2: At5g52550; NbExp=6; IntAct=EBI-979321, EBI-2298422;
CC Q39016; Q94BN0: BT2; NbExp=7; IntAct=EBI-979321, EBI-540986;
CC Q39016; Q9CA67: CHLP; NbExp=5; IntAct=EBI-979321, EBI-2298544;
CC Q39016; Q39083: DI19-1; NbExp=25; IntAct=EBI-979321, EBI-979339;
CC Q39016; O23338: dl3455w; NbExp=6; IntAct=EBI-979321, EBI-2296482;
CC Q39016; O80800: MTACP2; NbExp=4; IntAct=EBI-979321, EBI-2298689;
CC Q39016; O23680: TOC33; NbExp=4; IntAct=EBI-979321, EBI-639377;
CC Q39016; O04482: UCH2; NbExp=4; IntAct=EBI-979321, EBI-2298606;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16438971}. Nucleus
CC {ECO:0000269|PubMed:16438971}.
CC -!- INDUCTION: By drought and high-slat stress, but not by low-temperature,
CC heat stress or abscisic acid treatment. {ECO:0000269|PubMed:8078458}.
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 (290-320) inactivates kinase
CC activity under calcium-free conditions (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mutant cpk11-2 shows reduced ABA and salt
CC responsiveness in seed germination. {ECO:0000269|PubMed:17921317}.
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=AAF79386.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; D21806; BAA04830.1; -; mRNA.
DR EMBL; AC007887; AAF79386.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31822.1; -; Genomic_DNA.
DR EMBL; AY050981; AAK93658.1; -; mRNA.
DR EMBL; AY113986; AAM45034.1; -; mRNA.
DR PIR; S46284; S46284.
DR RefSeq; NP_174807.1; NM_103271.4.
DR AlphaFoldDB; Q39016; -.
DR SMR; Q39016; -.
DR BioGRID; 25703; 35.
DR IntAct; Q39016; 25.
DR MINT; Q39016; -.
DR STRING; 3702.AT1G35670.1; -.
DR iPTMnet; Q39016; -.
DR PaxDb; Q39016; -.
DR PRIDE; Q39016; -.
DR ProteomicsDB; 224453; -.
DR EnsemblPlants; AT1G35670.1; AT1G35670.1; AT1G35670.
DR GeneID; 840471; -.
DR Gramene; AT1G35670.1; AT1G35670.1; AT1G35670.
DR KEGG; ath:AT1G35670; -.
DR Araport; AT1G35670; -.
DR TAIR; locus:2014691; AT1G35670.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_000288_37_4_1; -.
DR InParanoid; Q39016; -.
DR OMA; RKHYGHE; -.
DR OrthoDB; 330091at2759; -.
DR PRO; PR:Q39016; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q39016; baseline and differential.
DR Genevisible; Q39016; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
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; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IDA:TAIR.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
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:0009789; P:positive regulation of abscisic acid-activated signaling pathway; IMP:TAIR.
DR GO; GO:0046777; P:protein autophosphorylation; HDA:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IDA:TAIR.
DR GO; GO:1901979; P:regulation of inward rectifier potassium channel activity; IDA:TAIR.
DR GO; GO:0080092; P:regulation of pollen tube growth; IMP:TAIR.
DR CDD; cd00051; EFh; 1.
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; Cytoplasm; Kinase; Metal-binding; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..495
FT /note="Calcium-dependent protein kinase 11"
FT /id="PRO_0000304513"
FT DOMAIN 26..284
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 327..362
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 363..398
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 399..434
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 438..468
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 290..320
FT /note="Autoinhibitory domain"
FT /evidence="ECO:0000250"
FT ACT_SITE 150
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 32..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 340
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 342
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 344
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 346
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 351
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 376
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 378
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 380
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 382
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 387
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 412
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 414
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 416
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 418
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 423
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 446
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 448
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 450
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 452
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 457
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FKW4"
FT MUTAGEN 150
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16438971"
FT MUTAGEN 171
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16438971"
FT MUTAGEN 306
FT /note="F->A: Constitutive activity."
FT /evidence="ECO:0000269|PubMed:16438971"
FT CONFLICT 403
FT /note="N -> I (in Ref. 1; BAA04830)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="Y -> D (in Ref. 1; BAA04830)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 495 AA; 55916 MW; 2DD0ED8C234EF2F7 CRC64;
METKPNPRRP SNTVLPYQTP RLRDHYLLGK KLGQGQFGTT YLCTEKSTSA NYACKSIPKR
KLVCREDYED VWREIQIMHH LSEHPNVVRI KGTYEDSVFV HIVMEVCEGG ELFDRIVSKG
HFSEREAVKL IKTILGVVEA CHSLGVMHRD LKPENFLFDS PKDDAKLKAT DFGLSVFYKP
GQYLYDVVGS PYYVAPEVLK KCYGPEIDVW SAGVILYILL SGVPPFWAET ESGIFRQILQ
GKLDFKSDPW PTISEAAKDL IYKMLERSPK KRISAHEALC HPWIVDEQAA PDKPLDPAVL
SRLKQFSQMN KIKKMALRVI AERLSEEEIG GLKELFKMID TDNSGTITFE ELKAGLKRVG
SELMESEIKS LMDAADIDNS GTIDYGEFLA ATLHMNKMER EENLVAAFSY FDKDGSGYIT
IDELQSACTE FGLCDTPLDD MIKEIDLDND GKIDFSEFTA MMRKGDGVGR SRTMMKNLNF
NIADAFGVDG EKSDD
