CIPKO_ARATH
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 03-AUG-2022, entry version 161.
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=10.2307/3871302;
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};
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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; 41.
DR DIP; DIP-34745N; -.
DR IntAct; Q9LDI3; 32.
DR STRING; 3702.AT5G35410.1; -.
DR iPTMnet; Q9LDI3; -.
DR PaxDb; Q9LDI3; -.
DR PRIDE; Q9LDI3; -.
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; locus:2155233; AT5G35410.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_59_0_1; -.
DR InParanoid; Q9LDI3; -.
DR OrthoDB; 1127668at2759; -.
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 Genevisible; Q9LDI3; AT.
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; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
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 Pfam; PF03822; NAF; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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.
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
