ID CIPKO_ARATH Reviewed; 446 AA. AC Q9LDI3; Q9LKR2; DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 169. DE RecName: Full=CBL-interacting serine/threonine-protein kinase 24; DE EC=2.7.11.1; DE AltName: Full=Protein SALT OVERLY SENSITIVE 2; DE AltName: Full=SNF1-related kinase 3.11; GN Name=CIPK24; Synonyms=SnRK3.11, SOS2; OrderedLocusNames=At5g35410; GN ORFNames=F6I13.1, K21B8.3; 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], CHARACTERIZATION, AND MUTAGENESIS OF RP LYS-40 AND GLY-197. RC STRAIN=cv. Columbia; RX PubMed=10725382; DOI=10.1073/pnas.97.7.3730; RA Liu J., Ishitani M., Halfter U., Kim C.-S., Zhu J.-K.; RT "The Arabidopsis thaliana SOS2 gene encodes a protein kinase that is RT required for salt tolerance."; RL Proc. Natl. Acad. Sci. U.S.A. 97:3730-3734(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Weinl S., Albrecht V., Kudla J.; RT "Molecular characterization of the CIPK gene family from Arabidopsis RT thaliana."; RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H., RA Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI."; RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases. RN [4] 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 [5] 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 [6] 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 [7] RP FUNCTION, INTERACTION WITH CBL4, AND MUTAGENESIS OF THR-168. RX PubMed=10725350; DOI=10.1073/pnas.97.7.3735; RA Halfter U., Ishitani M., Zhu J.-K.; RT "The Arabidopsis SOS2 protein kinase physically interacts with and is RT activated by the calcium-binding protein SOS3."; RL Proc. Natl. Acad. Sci. U.S.A. 97:3735-3740(2000). RN [8] RP ACTIVATION DOMAINS. RX PubMed=11402167; DOI=10.1105/tpc.13.6.1383; RA Guo Y., Halfter U., Ishitani M., Zhu J.-K.; RT "Molecular characterization of functional domains in the protein kinase RT SOS2 that is required for plant salt tolerance."; RL Plant Cell 13:1383-1400(2001). RN [9] RP FUNCTION. RX PubMed=12034882; DOI=10.1073/pnas.122224699; RA Qiu Q.-S., Guo Y., Dietrich M.A., Schumaker K.S., Zhu J.-K.; RT "Regulation of SOS1, a plasma membrane Na(+)/H(+) exchanger in Arabidopsis RT thaliana, by SOS2 and SOS3."; RL Proc. Natl. Acad. Sci. U.S.A. 99:8436-8441(2002). RN [10] RP MUTAGENESIS OF SER-156 AND TYR-175. RX PubMed=12226505; DOI=10.1104/pp.004507; RA Gong D., Guo Y., Jagendorf A.T., Zhu J.-K.; RT "Biochemical characterization of the Arabidopsis protein kinase SOS2 that RT functions in salt tolerance."; RL Plant Physiol. 130:256-264(2002). RN [11] RP INTERACTION WITH ABI2. RX PubMed=14504388; DOI=10.1073/pnas.2034853100; RA Ohta M., Guo Y., Halfter U., Zhu J.-K.; RT "A novel domain in the protein kinase SOS2 mediates interaction with the RT protein phosphatase 2C ABI2."; RL Proc. Natl. Acad. Sci. U.S.A. 100:11771-11776(2003). RN [12] 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 [13] RP FUNCTION. RX PubMed=14583601; DOI=10.1074/jbc.m309084200; RA Cheng N.-H., Pittman J.K., Zhu J.-K., Hirschi K.D.; RT "The protein kinase SOS2 activates the Arabidopsis H(+)/Ca(2+) antiporter RT CAX1 to integrate calcium transport and salt tolerance."; RL J. Biol. Chem. 279:2922-2926(2004). RN [14] RP INTERACTION WITH CBL1 AND CBL9. RX PubMed=14730064; DOI=10.1104/pp.103.033068; RA Kolukisaoglu U., Weinl S., Blazevic D., Batistic O., Kudla J.; RT "Calcium sensors and their interacting protein kinases: genomics of the RT Arabidopsis and rice CBL-CIPK signaling networks."; RL Plant Physiol. 134:43-58(2004). RN [15] RP INTERACTION WITH CBL1; CBL2; CBL5 AND CBL10, AND SUBCELLULAR LOCATION. RX PubMed=17825054; DOI=10.1111/j.1365-313x.2007.03249.x; RA Kim B.G., Waadt R., Cheong Y.H., Pandey G.K., Dominguez-Solis J.R., RA Schueltke S., Lee S.C., Kudla J., Luan S.; RT "The calcium sensor CBL10 mediates salt tolerance by regulating ion RT homeostasis in Arabidopsis."; RL Plant J. 52:473-484(2007). RN [16] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, RP PHOSPHORYLATION, INTERACTION WITH CBL1; CBL4 AND CBL10, AND DOMAIN. RX PubMed=22253446; DOI=10.1074/jbc.m111.279331; RA Hashimoto K., Eckert C., Anschuetz U., Scholz M., Held K., Waadt R., RA Reyer A., Hippler M., Becker D., Kudla J.; RT "Phosphorylation of calcineurin B-like (CBL) calcium sensor proteins by RT their CBL-interacting protein kinases (CIPKs) is required for full activity RT of CBL-CIPK complexes toward their target proteins."; RL J. Biol. Chem. 287:7956-7968(2012). RN [17] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 304-446 IN COMPLEX WITH SOS3, AND RP INTERACTION WITH SOS3 AND ABI2. RX PubMed=17499048; DOI=10.1016/j.molcel.2007.04.013; RA Sanchez-Barrena M.J., Fujii H., Angulo I., Martinez-Ripoll M., Zhu J.-K., RA Albert A.; RT "The structure of the C-terminal domain of the protein kinase AtSOS2 bound RT to the calcium sensor AtSOS3."; RL Mol. Cell 26:427-435(2007). CC -!- FUNCTION: Involved in the regulatory pathway for the control of CC intracellular Na(+) and K(+) homeostasis and salt tolerance. Activates CC the vacuolar H(+)/Ca(2+) antiporter CAX1 and operates in synergy with CC CBL4/SOS3 to activate the plasma membrane Na(+)/H(+) antiporter SOS1. CC CIPK serine-threonine protein kinases interact with CBL proteins. CC Binding of a CBL protein to the regulatory NAF domain of CIPK protein CC lead to the activation of the kinase in a calcium-dependent manner. CC Phosphorylates CBL1, CBL4 and CBL10. {ECO:0000269|PubMed:10725350, CC ECO:0000269|PubMed:12034882, ECO:0000269|PubMed:14583601, CC ECO:0000269|PubMed:22253446}. 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:22253446}; 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:22253446}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:22253446}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=131.2 uM for synthetic substrate {ECO:0000269|PubMed:22253446}; CC Vmax=1304 pmol/min/mg enzyme {ECO:0000269|PubMed:22253446}; CC -!- SUBUNIT: Interacts with CBL1, CBL2, CBL4/SOS3, CBL5, CBL9, CBL10 and CC with the protein phosphatase 2C ABI2. {ECO:0000269|PubMed:10725350, CC ECO:0000269|PubMed:14504388, ECO:0000269|PubMed:14730064, CC ECO:0000269|PubMed:17499048, ECO:0000269|PubMed:17825054, CC ECO:0000269|PubMed:22253446}. CC -!- INTERACTION: CC Q9LDI3; O04719: ABI2; NbExp=4; IntAct=EBI-537551, EBI-537680; CC Q9LDI3; P25854: CAM4; NbExp=2; IntAct=EBI-537551, EBI-1235664; CC Q9LDI3; P59220: CAM7; NbExp=2; IntAct=EBI-537551, EBI-1236031; CC Q9LDI3; O81445: CBL1; NbExp=6; IntAct=EBI-537551, EBI-974530; CC Q9LDI3; Q7FRS8: CBL10; NbExp=5; IntAct=EBI-537551, EBI-2026616; CC Q9LDI3; Q7FRS8-2: CBL10; NbExp=4; IntAct=EBI-537551, EBI-2026677; CC Q9LDI3; O81223: CBL4; NbExp=10; IntAct=EBI-537551, EBI-537541; CC Q9LDI3; Q9LTB8: CBL9; NbExp=8; IntAct=EBI-537551, EBI-637381; CC Q9LDI3; Q9S744: CML9; NbExp=2; IntAct=EBI-537551, EBI-1236048; CC Q9LDI3; O64903: NDPK2; NbExp=3; IntAct=EBI-537551, EBI-349517; CC Q9LDI3; Q9LKW9: NHX7; NbExp=4; IntAct=EBI-537551, EBI-2368285; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17825054}. Nucleus CC {ECO:0000269|PubMed:17825054}. Note=Targeted to the cell membrane when CC interacting with CBL1 or CBL5 and to the tonoplast when interacting CC with CBL2 orCBL10. CC -!- INDUCTION: Up-regulated in roots by salt stress. CC -!- DOMAIN: The activation loop within the kinase domain is the target of CC phosphorylation/activation by upstream protein kinases. The PPI motif CC mediates the interaction with the ABI (abscisic acid-insensitive) CC phosphatases. The C-terminal part (309-446) of the protein is required CC for the phosphorylation of CBL, but is not involved in CC autophosphorylation. {ECO:0000269|PubMed:22253446}. CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:22253446}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr CC protein kinase family. SNF1 subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF67384.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF237670; AAF62923.1; -; Genomic_DNA. DR EMBL; AF395081; AAK72257.1; -; mRNA. DR EMBL; AB025611; BAA98146.1; -; Genomic_DNA. DR EMBL; AF262044; AAF67384.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002688; AED93966.1; -; Genomic_DNA. DR EMBL; AY099621; AAM20472.1; -; mRNA. DR EMBL; BT002138; AAN72149.1; -; mRNA. DR RefSeq; NP_198391.1; NM_122932.5. DR PDB; 2EHB; X-ray; 2.10 A; D=304-446. DR PDB; 4D28; X-ray; 3.30 A; A/B/C/D=1-446. DR PDBsum; 2EHB; -. DR PDBsum; 4D28; -. DR AlphaFoldDB; Q9LDI3; -. DR SMR; Q9LDI3; -. DR BioGRID; 18756; 42. DR DIP; DIP-34745N; -. DR IntAct; Q9LDI3; 32. DR STRING; 3702.Q9LDI3; -. DR iPTMnet; Q9LDI3; -. DR PaxDb; 3702-AT5G35410-1; -. DR ProteomicsDB; 246690; -. DR EnsemblPlants; AT5G35410.1; AT5G35410.1; AT5G35410. DR GeneID; 833502; -. DR Gramene; AT5G35410.1; AT5G35410.1; AT5G35410. DR KEGG; ath:AT5G35410; -. DR Araport; AT5G35410; -. DR TAIR; AT5G35410; SOS2. DR eggNOG; KOG0583; Eukaryota. DR HOGENOM; CLU_000288_59_0_1; -. DR InParanoid; Q9LDI3; -. DR OrthoDB; 5388562at2759; -. DR PhylomeDB; Q9LDI3; -. DR SABIO-RK; Q9LDI3; -. DR EvolutionaryTrace; Q9LDI3; -. DR PRO; PR:Q9LDI3; -. DR Proteomes; UP000006548; Chromosome 5. DR ExpressionAtlas; Q9LDI3; baseline and differential. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 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; IEA:UniProtKB-KW. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0009651; P:response to salt stress; IMP:TAIR. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR CDD; cd12195; CIPK_C; 1. DR Gene3D; 3.30.310.80; Kinase associated domain 1, KA1; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR018451; NAF/FISL_domain. DR InterPro; IPR004041; NAF_dom. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR43895; CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE KINASE-RELATED; 1. DR PANTHER; PTHR43895:SF168; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF03822; NAF; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50816; NAF; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; Q9LDI3; AT. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cytoplasm; Kinase; Manganese; KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1..446 FT /note="CBL-interacting serine/threonine-protein kinase 24" FT /id="PRO_0000085877" FT DOMAIN 11..264 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT DOMAIN 305..329 FT /note="NAF" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00256" FT REGION 152..179 FT /note="Activation loop" FT REGION 336..365 FT /note="PPI" FT ACT_SITE 134 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 17..25 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 40 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 156 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q93V58" FT MOD_RES 168 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q38997" FT MUTAGEN 40 FT /note="K->N: Abolishes autophosphorylation." FT /evidence="ECO:0000269|PubMed:10725382" FT MUTAGEN 156 FT /note="S->D: Increases kinase activity." FT /evidence="ECO:0000269|PubMed:12226505" FT MUTAGEN 168 FT /note="T->D: Increases kinase activity." FT /evidence="ECO:0000269|PubMed:10725350" FT MUTAGEN 175 FT /note="Y->D: Increases kinase activity." FT /evidence="ECO:0000269|PubMed:12226505" FT MUTAGEN 197 FT /note="G->E: Abolishes autophosphorylation." FT /evidence="ECO:0000269|PubMed:10725382" FT STRAND 11..13 FT /evidence="ECO:0007829|PDB:4D28" FT STRAND 24..30 FT /evidence="ECO:0007829|PDB:4D28" FT TURN 31..34 FT /evidence="ECO:0007829|PDB:4D28" FT STRAND 35..43 FT /evidence="ECO:0007829|PDB:4D28" FT HELIX 44..48 FT /evidence="ECO:0007829|PDB:4D28" FT HELIX 53..65 FT /evidence="ECO:0007829|PDB:4D28" FT STRAND 77..79 FT /evidence="ECO:0007829|PDB:4D28" FT STRAND 81..88 FT /evidence="ECO:0007829|PDB:4D28" FT STRAND 92..95 FT /evidence="ECO:0007829|PDB:4D28" FT HELIX 97..103 FT /evidence="ECO:0007829|PDB:4D28" FT HELIX 108..127 FT /evidence="ECO:0007829|PDB:4D28" FT TURN 137..139 FT /evidence="ECO:0007829|PDB:4D28" FT STRAND 140..142 FT /evidence="ECO:0007829|PDB:4D28" FT STRAND 148..150 FT /evidence="ECO:0007829|PDB:4D28" FT STRAND 173..176 FT /evidence="ECO:0007829|PDB:4D28" FT HELIX 178..182 FT /evidence="ECO:0007829|PDB:4D28" FT HELIX 188..205 FT /evidence="ECO:0007829|PDB:4D28" FT STRAND 212..214 FT /evidence="ECO:0007829|PDB:4D28" FT HELIX 215..224 FT /evidence="ECO:0007829|PDB:4D28" FT HELIX 235..244 FT /evidence="ECO:0007829|PDB:4D28" FT TURN 249..251 FT /evidence="ECO:0007829|PDB:4D28" FT HELIX 255..260 FT /evidence="ECO:0007829|PDB:4D28" FT HELIX 262..265 FT /evidence="ECO:0007829|PDB:4D28" FT HELIX 281..286 FT /evidence="ECO:0007829|PDB:4D28" FT HELIX 312..316 FT /evidence="ECO:0007829|PDB:2EHB" FT TURN 320..322 FT /evidence="ECO:0007829|PDB:2EHB" FT HELIX 324..328 FT /evidence="ECO:0007829|PDB:2EHB" FT STRAND 340..343 FT /evidence="ECO:0007829|PDB:2EHB" FT HELIX 347..360 FT /evidence="ECO:0007829|PDB:2EHB" FT STRAND 363..376 FT /evidence="ECO:0007829|PDB:2EHB" FT HELIX 381..383 FT /evidence="ECO:0007829|PDB:2EHB" FT STRAND 386..395 FT /evidence="ECO:0007829|PDB:2EHB" FT STRAND 398..408 FT /evidence="ECO:0007829|PDB:2EHB" FT HELIX 410..423 FT /evidence="ECO:0007829|PDB:2EHB" FT TURN 425..427 FT /evidence="ECO:0007829|PDB:2EHB" SQ SEQUENCE 446 AA; 50635 MW; 99FDF3A778E1093D CRC64; MTKKMRRVGK YEVGRTIGEG TFAKVKFARN TDTGDNVAIK IMAKSTILKN RMVDQIKREI SIMKIVRHPN IVRLYEVLAS PSKIYIVLEF VTGGELFDRI VHKGRLEESE SRKYFQQLVD AVAHCHCKGV YHRDLKPENL LLDTNGNLKV SDFGLSALPQ EGVELLRTTC GTPNYVAPEV LSGQGYDGSA ADIWSCGVIL FVILAGYLPF SETDLPGLYR KINAAEFSCP PWFSAEVKFL IHRILDPNPK TRIQIQGIKK DPWFRLNYVP IRAREEEEVN LDDIRAVFDG IEGSYVAENV ERNDEGPLMM NAFEMITLSQ GLNLSALFDR RQDFVKRQTR FVSRREPSEI IANIEAVANS MGFKSHTRNF KTRLEGLSSI KAGQLAVVIE IYEVAPSLFM VDVRKAAGET LEYHKFYKKL CSKLENIIWR ATEGIPKSEI LRTITF //