CIPKN_ARATH
ID CIPKN_ARATH Reviewed; 482 AA.
AC Q93VD3; Q9C753;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=CBL-interacting serine/threonine-protein kinase 23;
DE EC=2.7.11.1;
DE AltName: Full=Protein LOW-K(+)-SENSITIVE 1;
DE AltName: Full=SNF1-related kinase 3.23;
DE AltName: Full=SOS2-like protein kinase PKS17;
GN Name=CIPK23; Synonyms=LKS1, PKS17, SnRK3.23; OrderedLocusNames=At1g30270;
GN ORFNames=F12P21.6;
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].
RA Weinl S., Albrecht V., Kudla J.;
RT "Molecular characterization of the CIPK gene family from Arabidopsis
RT thaliana.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
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.
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 [6]
RP INTERACTION WITH 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 [7]
RP REVIEW.
RX PubMed=16814705; DOI=10.1016/j.cell.2006.06.017;
RA Hedrich R., Kudla J.;
RT "Calcium signaling networks channel plant K+ uptake.";
RL Cell 125:1221-1223(2006).
RN [8]
RP FUNCTION, MUTAGENESIS OF ALA-199 AND LEU-447, INTERACTION WITH AKT1; CBL1;
RP CBL2; CBL3; CBL5; CBL8 AND CBL9, TISSUE SPECIFICITY, INDUCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=16814720; DOI=10.1016/j.cell.2006.06.011;
RA Xu J., Li H.-D., Chen L.-Q., Wang Y., Liu L.-L., He L., Wu W.-H.;
RT "A protein kinase, interacting with two calcineurin B-like proteins,
RT regulates K+ transporter AKT1 in Arabidopsis.";
RL Cell 125:1347-1360(2006).
RN [9]
RP FUNCTION, INTERACTION WITH AKT1, AND AUTOPHOSPHORYLATION.
RX PubMed=16895985; DOI=10.1073/pnas.0605129103;
RA Li L., Kim B.-G., Cheong Y.H., Pandey G.K., Luan S.;
RT "A Ca(2)+ signaling pathway regulates a K(+) channel for low-K response in
RT Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:12625-12630(2006).
RN [10]
RP FUNCTION, INTERACTION WITH CBL1 AND CBL9, TISSUE SPECIFICITY, INDUCTION,
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=17922773; DOI=10.1111/j.1365-313x.2007.03236.x;
RA Cheong Y.H., Pandey G.K., Grant J.J., Batistic O., Li L., Kim B.-G.,
RA Lee S.-C., Kudla J., Luan S.;
RT "Two calcineurin B-like calcium sensors, interacting with protein kinase
RT CIPK23, regulate leaf transpiration and root potassium uptake in
RT Arabidopsis.";
RL Plant J. 52:223-239(2007).
RN [11]
RP FUNCTION, AND INTERACTION WITH AKT1; CBL1; CBL2; CBL3 AND CBL9.
RX PubMed=17898163; DOI=10.1073/pnas.0707912104;
RA Lee S.-C., Lan W.-Z., Kim B.-G., Li L., Cheong Y.H., Pandey G.K., Lu G.,
RA Buchanan B.B., Luan S.;
RT "A protein phosphorylation/dephosphorylation network regulates a plant
RT potassium channel.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:15959-15964(2007).
RN [12]
RP FUNCTION, INDUCTION BY NITRATE, AND INTERACTION WITH NRT1.1.
RX PubMed=19766570; DOI=10.1016/j.cell.2009.07.004;
RA Ho C.H., Lin S.H., Hu H.C., Tsay Y.F.;
RT "CHL1 functions as a nitrate sensor in plants.";
RL Cell 138:1184-1194(2009).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP PHOSPHORYLATION.
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).
CC -!- FUNCTION: CIPK serine-threonine protein kinases interact with CBL
CC proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK
CC protein leads to activation of the kinase in a calcium-dependent
CC manner. Downstream of CBL1, CBL2, CBL3 and CBL9, regulates by
CC phosphorylation the K(+) conductance and uptake of AKT1 in low K(+)
CC condition, in response to calcium signaling and during the stomatal
CC opening regulation by monitoring the turgor pressure in guard cells. In
CC response to low nitrate concentration, phosphorylates NRT1.1, switching
CC it from a low-affinity nitrate transporter to a high-affinity
CC transporter. Confers tolerance to low potassium conditions. Involved in
CC drought sensitivity and leaf transpiration.
CC {ECO:0000269|PubMed:16814720, ECO:0000269|PubMed:16895985,
CC ECO:0000269|PubMed:17898163, ECO:0000269|PubMed:17922773,
CC ECO:0000269|PubMed:19766570, 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=43.2 uM for synthetic substrate {ECO:0000269|PubMed:22253446};
CC Vmax=147.7 pmol/min/mg enzyme {ECO:0000269|PubMed:22253446};
CC -!- SUBUNIT: Part of a K(+)-channel calcium-sensing kinase/phosphatase
CC complex composed by a calcium sensor CBL (CBL1, CBL2, CBL3 or CBL9), a
CC kinase CIPK (CIPK6, CIPK16 or CIPK23), a phosphatase PP2C (AIP1) and a
CC K(+)-channel (AKT1). Interacts with AKT1, CBL1, CBL2, CBL3, CBL5, CBL8,
CC CBL9 and NRT1.1. {ECO:0000269|PubMed:14730064,
CC ECO:0000269|PubMed:16814720, ECO:0000269|PubMed:16895985,
CC ECO:0000269|PubMed:17898163, ECO:0000269|PubMed:17922773,
CC ECO:0000269|PubMed:19766570}.
CC -!- INTERACTION:
CC Q93VD3; Q38998: AKT1; NbExp=6; IntAct=EBI-974277, EBI-974289;
CC Q93VD3; O81445: CBL1; NbExp=6; IntAct=EBI-974277, EBI-974530;
CC Q93VD3; Q9LTB8: CBL9; NbExp=13; IntAct=EBI-974277, EBI-637381;
CC Q93VD3; Q05085: NPF6.3; NbExp=3; IntAct=EBI-974277, EBI-2463703;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16814720,
CC ECO:0000269|PubMed:17922773}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16814720, ECO:0000269|PubMed:17922773}.
CC Note=Associated to the plasma membrane when associated with AKT1, CBL1
CC and CBL9.
CC -!- TISSUE SPECIFICITY: In seedlings, mostly in vascular bundles, and in
CC roots, especially in cortex and endodermis cells. In adult plants,
CC mostly expressed in flowers, and, to a lower extent, in roots, leaves,
CC stems and siliques, particularly in vascular tissues. Also detected in
CC guard cells and root hairs. {ECO:0000269|PubMed:16814720,
CC ECO:0000269|PubMed:17922773}.
CC -!- INDUCTION: In roots under low K(+) conditions and transiently by
CC nitrate. {ECO:0000269|PubMed:16814720, ECO:0000269|PubMed:17922773,
CC ECO:0000269|PubMed:19766570}.
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 (By similarity). {ECO:0000250}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:22253446}.
CC -!- DISRUPTION PHENOTYPE: Plants exhibit an increased drought tolerance and
CC an enhanced sensitivity to abscisic acid (ABA) during the stomatal
CC regulation. {ECO:0000269|PubMed:17922773}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG50566.1; 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; AY035226; AAK61494.1; -; mRNA.
DR EMBL; AC073506; AAG50566.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31201.1; -; Genomic_DNA.
DR EMBL; AY056419; AAL08275.1; -; mRNA.
DR EMBL; AY090322; AAL90983.1; -; mRNA.
DR PIR; A86427; A86427.
DR RefSeq; NP_564353.1; NM_102766.6.
DR PDB; 4CZT; X-ray; 2.30 A; A/B/C/D=25-482.
DR PDB; 4CZU; X-ray; 1.90 A; A/B/C/D=25-482.
DR PDBsum; 4CZT; -.
DR PDBsum; 4CZU; -.
DR AlphaFoldDB; Q93VD3; -.
DR SMR; Q93VD3; -.
DR BioGRID; 25142; 11.
DR DIP; DIP-36761N; -.
DR IntAct; Q93VD3; 9.
DR STRING; 3702.AT1G30270.1; -.
DR iPTMnet; Q93VD3; -.
DR PaxDb; Q93VD3; -.
DR PRIDE; Q93VD3; -.
DR ProteomicsDB; 246689; -.
DR EnsemblPlants; AT1G30270.1; AT1G30270.1; AT1G30270.
DR GeneID; 839907; -.
DR Gramene; AT1G30270.1; AT1G30270.1; AT1G30270.
DR KEGG; ath:AT1G30270; -.
DR Araport; AT1G30270; -.
DR TAIR; locus:2009812; AT1G30270.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_59_0_1; -.
DR InParanoid; Q93VD3; -.
DR OrthoDB; 1127668at2759; -.
DR PhylomeDB; Q93VD3; -.
DR SABIO-RK; Q93VD3; -.
DR PRO; PR:Q93VD3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q93VD3; baseline and differential.
DR Genevisible; Q93VD3; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IPI:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005267; F:potassium channel activity; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:TAIR.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0010119; P:regulation of stomatal movement; IMP:TAIR.
DR GO; GO:0007584; P:response to nutrient; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR GO; GO:0010118; P:stomatal movement; 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; Cell membrane; Ion channel; Ion transport;
KW Kinase; Manganese; Membrane; Nucleotide-binding; Phosphoprotein; Potassium;
KW Potassium channel; Potassium transport; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Transport.
FT CHAIN 1..482
FT /note="CBL-interacting serine/threonine-protein kinase 23"
FT /id="PRO_0000337224"
FT DOMAIN 31..286
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 328..352
FT /note="NAF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00256"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..201
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT REGION 359..388
FT /note="PPI"
FT /evidence="ECO:0000250"
FT REGION 459..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 154
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 37..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93V58"
FT MOD_RES 190
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q38997"
FT MUTAGEN 199
FT /note="A->V: In lks1-1; enhanced sensitivity to low K(+)."
FT /evidence="ECO:0000269|PubMed:16814720"
FT MUTAGEN 447
FT /note="L->F: In lks1-2; enhanced sensitivity to low K(+)."
FT /evidence="ECO:0000269|PubMed:16814720"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:4CZU"
FT STRAND 31..39
FT /evidence="ECO:0007829|PDB:4CZU"
FT STRAND 41..50
FT /evidence="ECO:0007829|PDB:4CZU"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:4CZU"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:4CZU"
FT HELIX 64..68
FT /evidence="ECO:0007829|PDB:4CZU"
FT HELIX 73..85
FT /evidence="ECO:0007829|PDB:4CZU"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:4CZU"
FT STRAND 101..108
FT /evidence="ECO:0007829|PDB:4CZU"
FT HELIX 117..123
FT /evidence="ECO:0007829|PDB:4CZU"
FT HELIX 128..147
FT /evidence="ECO:0007829|PDB:4CZU"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:4CZU"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:4CZU"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:4CZU"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:4CZU"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:4CZU"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:4CZU"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:4CZU"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:4CZU"
FT HELIX 210..227
FT /evidence="ECO:0007829|PDB:4CZU"
FT HELIX 237..246
FT /evidence="ECO:0007829|PDB:4CZU"
FT HELIX 257..266
FT /evidence="ECO:0007829|PDB:4CZU"
FT TURN 271..273
FT /evidence="ECO:0007829|PDB:4CZU"
FT HELIX 277..281
FT /evidence="ECO:0007829|PDB:4CZU"
FT TURN 284..289
FT /evidence="ECO:0007829|PDB:4CZU"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:4CZU"
SQ SEQUENCE 482 AA; 53514 MW; CAA1B526B955F5F2 CRC64;
MASRTTPSRS TPSRSTPSGS SSGGRTRVGK YELGRTLGEG TFAKVKFARN VENGDNVAIK
VIDKEKVLKN KMIAQIKREI STMKLIKHPN VIRMFEVMAS KTKIYFVLEF VTGGELFDKI
SSNGRLKEDE ARKYFQQLIN AVDYCHSRGV YHRDLKPENL LLDANGALKV SDFGLSALPQ
QVREDGLLHT TCGTPNYVAP EVINNKGYDG AKADLWSCGV ILFVLMAGYL PFEDSNLTSL
YKKIFKAEFT CPPWFSASAK KLIKRILDPN PATRITFAEV IENEWFKKGY KAPKFENADV
SLDDVDAIFD DSGESKNLVV ERREEGLKTP VTMNAFELIS TSQGLNLGSL FEKQMGLVKR
KTRFTSKSSA NEIVTKIEAA AAPMGFDVKT NNYKMKLTGE KSGRKGQLAV ATEVFQVAPS
LYMVEMRKSG GDTLEFHKFY KNLTTGLKDI VWKTIDEEKE EGTDGGGTNG AMANRTIAKQ
ST
