KC1D_RAT
ID KC1D_RAT Reviewed; 415 AA.
AC Q06486; Q99KK4;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Casein kinase I isoform delta;
DE Short=CKI-delta;
DE EC=2.7.11.1 {ECO:0000269|PubMed:15961172};
DE AltName: Full=Tau-protein kinase CSNK1D;
DE EC=2.7.11.26 {ECO:0000250|UniProtKB:P48730};
GN Name=Csnk1d; Synonyms=Hckid;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND PROTEIN SEQUENCE OF 1-6.
RC TISSUE=Testis;
RX PubMed=8454611; DOI=10.1016/s0021-9258(18)53265-8;
RA Graves P.R., Haas D.W., Hagedorn C.H., Depaoli-Roach A.A., Roach P.J.;
RT "Molecular cloning, expression, and characterization of a 49-kilodalton
RT casein kinase I isoform from rat testis.";
RL J. Biol. Chem. 268:6394-6401(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Takano A., Nagai K.;
RT "Casein kinase 1 delta rat.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP AUTOPHOSPHORYLATION, AND AUTOINHIBITORY DOMAIN.
RX PubMed=7665585; DOI=10.1074/jbc.270.37.21689;
RA Graves P.R., Roach P.J.;
RT "Role of COOH-terminal phosphorylation in the regulation of casein kinase I
RT delta.";
RL J. Biol. Chem. 270:21689-21694(1995).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=11165242; DOI=10.1016/s0014-5793(00)02434-0;
RA Camacho F., Cilio M., Guo Y., Virshup D.M., Patel K., Khorkova O.,
RA Styren S., Morse B., Yao Z., Keesler G.A.;
RT "Human casein kinase Idelta phosphorylation of human circadian clock
RT proteins period 1 and 2.";
RL FEBS Lett. 489:159-165(2001).
RN [5]
RP FUNCTION AS MAP1A KINASE, INTERACTION WITH MAP1A, AND CATALYTIC ACTIVITY.
RX PubMed=15961172; DOI=10.1016/j.bbamcr.2005.05.004;
RA Wolff S., Xiao Z., Wittau M., Suessner N., Stoeter M., Knippschild U.;
RT "Interaction of casein kinase 1 delta (CK1 delta) with the light chain LC2
RT of microtubule associated protein 1A (MAP1A).";
RL Biochim. Biophys. Acta 1745:196-206(2005).
RN [6]
RP PHOSPHORYLATION AT SER-370 BY PKA.
RX PubMed=17594292; DOI=10.1042/bj20070091;
RA Giamas G., Hirner H., Shoshiashvili L., Grothey A., Gessert S., Kuehl M.,
RA Henne-Bruns D., Vorgias C.E., Knippschild U.;
RT "Phosphorylation of CK1delta: identification of Ser370 as the major
RT phosphorylation site targeted by PKA in vitro and in vivo.";
RL Biochem. J. 406:389-398(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-317, AND ACTIVE SITE.
RX PubMed=8648628; DOI=10.1006/jmbi.1996.0189;
RA Longenecker K.L., Roach P.J., Hurley T.D.;
RT "Three-dimensional structure of mammalian casein kinase I: molecular basis
RT for phosphate recognition.";
RL J. Mol. Biol. 257:618-631(1996).
CC -!- FUNCTION: Essential serine/threonine-protein kinase that regulates
CC diverse cellular growth and survival processes including Wnt signaling,
CC DNA repair and circadian rhythms. It can phosphorylate a large number
CC of proteins. Casein kinases are operationally defined by their
CC preferential utilization of acidic proteins such as caseins as
CC substrates. Phosphorylates connexin-43/GJA1, MAP1A, SNAPIN, MAPT/TAU,
CC TOP2A, DCK, HIF1A, EIF6, p53/TP53, DVL2, DVL3, ESR1, AIB1/NCOA3, DNMT1,
CC PKD2, YAP1, PER1 and PER2. Central component of the circadian clock. In
CC balance with PP1, determines the circadian period length through the
CC regulation of the speed and rhythmicity of PER1 and PER2
CC phosphorylation. Controls PER1 and PER2 nuclear transport and
CC degradation. YAP1 phosphorylation promotes its SCF(beta-TRCP) E3
CC ubiquitin ligase-mediated ubiquitination and subsequent degradation.
CC DNMT1 phosphorylation reduces its DNA-binding activity. Phosphorylation
CC of ESR1 and AIB1/NCOA3 stimulates their activity and coactivation.
CC Phosphorylation of DVL2 and DVL3 regulates WNT3A signaling pathway that
CC controls neurite outgrowth. EIF6 phosphorylation promotes its nuclear
CC export. Triggers down-regulation of dopamine receptors in the
CC forebrain. Activates DCK in vitro by phosphorylation. TOP2A
CC phosphorylation favors DNA cleavable complex formation. May regulate
CC the formation of the mitotic spindle apparatus in extravillous
CC trophoblast. Modulates connexin-43/GJA1 gap junction assembly by
CC phosphorylation. Probably involved in lymphocyte physiology. Regulates
CC fast synaptic transmission mediated by glutamate (By similarity).
CC {ECO:0000250|UniProtKB:P48730, ECO:0000269|PubMed:15961172}.
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:15961172};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000305|PubMed:15961172};
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:15961172};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000305|PubMed:15961172};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl-
CC [tau protein]; Xref=Rhea:RHEA:12801, Rhea:RHEA-COMP:13701, Rhea:RHEA-
CC COMP:13702, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.26;
CC Evidence={ECO:0000250|UniProtKB:P48730};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12802;
CC Evidence={ECO:0000250|UniProtKB:P48730};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[tau protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[tau protein]; Xref=Rhea:RHEA:53904, Rhea:RHEA-COMP:13703,
CC Rhea:RHEA-COMP:13704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.26; Evidence={ECO:0000250|UniProtKB:P48730};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53905;
CC Evidence={ECO:0000250|UniProtKB:P48730};
CC -!- ACTIVITY REGULATION: Drug-mediated inhibition leads to a delay of the
CC oscillations with the magnitude of this effect dependent upon the
CC timing of drug administration. Inhibited by phosphorylation (By
CC similarity). Exhibits substrate-dependent heparin activation.
CC {ECO:0000250|UniProtKB:P48730}.
CC -!- SUBUNIT: Monomer (By similarity). Component of the circadian core
CC oscillator, which includes the CRY proteins, CLOCK, or NPAS2,
CC ARTNL/BMAL1 or ARTNL2/BMAL2, CSNK1D and/or CSNK1E, TIMELESS and the PER
CC proteins (By similarity). Interacts with DNMT1 (By similarity).
CC Interacts directly with PER1 and PER2 which may lead to their
CC degradation (By similarity). Interacts with MAPT/TAU, SNAPIN, DBNDD2,
CC AIB1/NCOA3 and ESR1 (By similarity). Interacts with AKAP9/AKAP450; this
CC interaction promotes centrosomal subcellular location (By similarity).
CC Binds to tubulins in mitotic cells upon DNA damage (By similarity).
CC Interacts with GJA1 (By similarity). Interacts with MAP1A
CC (PubMed:15961172). Interacts with DDX3X; this interaction enhances
CC CSNK1D kinase activity in vitro, but it is unclear whether this
CC interaction is physiologically relevant (By similarity).
CC {ECO:0000250|UniProtKB:P48730, ECO:0000250|UniProtKB:Q9DC28,
CC ECO:0000269|PubMed:15961172}.
CC -!- INTERACTION:
CC Q06486; Q00987: MDM2; Xeno; NbExp=2; IntAct=EBI-2910316, EBI-389668;
CC Q06486-2; Q9Z266: Snapin; Xeno; NbExp=4; IntAct=EBI-7088890, EBI-6170320;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell
CC membrane {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}.
CC Golgi apparatus {ECO:0000250}. Note=Localized at mitotic spindle
CC microtubules, and at the centrosomes and interphase in interphase
CC cells. Recruited to the spindle apparatus and the centrosomes in
CC response to DNA-damage. Correct subcellular localization requires
CC kinase activity (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q06486-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q06486-2; Sequence=VSP_010255;
CC -!- TISSUE SPECIFICITY: Expressed in most tissues, including heart, brain,
CC testis, kidney, spleen and lung. {ECO:0000269|PubMed:11165242}.
CC -!- DOMAIN: The autoinhibitory domain is involved in regulating enzyme
CC activity through autophosphorylation and possibly, through heparin
CC binding.
CC -!- PTM: Autophosphorylated on serine and threonine residues; this
CC autophosphorylation represses activity. Reactivated by phosphatase-
CC mediated dephosphorylation. May be dephosphorylated by PP1.
CC {ECO:0000269|PubMed:17594292}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC protein kinase family. Casein kinase I subfamily. {ECO:0000305}.
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DR EMBL; L07578; AAA40934.1; -; mRNA.
DR EMBL; AB063114; BAB60852.1; -; mRNA.
DR PIR; A46002; A46002.
DR RefSeq; NP_620691.2; NM_139060.3. [Q06486-1]
DR PDB; 1CKI; X-ray; 2.30 A; A/B=1-317.
DR PDB; 1CKJ; X-ray; 2.46 A; A/B=1-317.
DR PDBsum; 1CKI; -.
DR PDBsum; 1CKJ; -.
DR AlphaFoldDB; Q06486; -.
DR SMR; Q06486; -.
DR BioGRID; 249077; 14.
DR IntAct; Q06486; 12.
DR MINT; Q06486; -.
DR STRING; 10116.ENSRNOP00000015178; -.
DR BindingDB; Q06486; -.
DR ChEMBL; CHEMBL4484; -.
DR iPTMnet; Q06486; -.
DR PhosphoSitePlus; Q06486; -.
DR jPOST; Q06486; -.
DR PaxDb; Q06486; -.
DR PRIDE; Q06486; -.
DR Ensembl; ENSRNOT00000015178; ENSRNOP00000015178; ENSRNOG00000036676. [Q06486-2]
DR GeneID; 64462; -.
DR KEGG; rno:64462; -.
DR CTD; 1453; -.
DR RGD; 71031; Csnk1d.
DR VEuPathDB; HostDB:ENSRNOG00000036676; -.
DR eggNOG; KOG1164; Eukaryota.
DR GeneTree; ENSGT00940000153536; -.
DR HOGENOM; CLU_019279_2_2_1; -.
DR InParanoid; Q06486; -.
DR OMA; IFDWTFL; -.
DR OrthoDB; 1097975at2759; -.
DR PhylomeDB; Q06486; -.
DR BRENDA; 2.7.11.1; 5301.
DR Reactome; R-RNO-204005; COPII-mediated vesicle transport.
DR Reactome; R-RNO-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-RNO-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-RNO-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-RNO-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-RNO-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-RNO-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-RNO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-RNO-8854518; AURKA Activation by TPX2.
DR EvolutionaryTrace; Q06486; -.
DR PRO; PR:Q06486; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000036676; Expressed in testis and 19 other tissues.
DR Genevisible; Q06486; RN.
DR GO; GO:0005813; C:centrosome; IDA:RGD.
DR GO; GO:0036064; C:ciliary basal body; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0005819; C:spindle; ISO:RGD.
DR GO; GO:0005876; C:spindle microtubule; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IDA:RGD.
DR GO; GO:0004672; F:protein kinase activity; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; ISO:RGD.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0050321; F:tau-protein kinase activity; ISO:RGD.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEP:RGD.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; ISO:RGD.
DR GO; GO:0007020; P:microtubule nucleation; ISO:RGD.
DR GO; GO:1905515; P:non-motile cilium assembly; ISO:RGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:2000052; P:positive regulation of non-canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISO:RGD.
DR GO; GO:0071539; P:protein localization to centrosome; ISO:RGD.
DR GO; GO:0061512; P:protein localization to cilium; ISO:RGD.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0051225; P:spindle assembly; ISO:RGD.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR DisProt; DP03052; -.
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; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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; Alternative splicing; ATP-binding; Biological rhythms;
KW Cell membrane; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Golgi apparatus; Kinase; Membrane; Methylation; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Wnt signaling pathway.
FT CHAIN 1..415
FT /note="Casein kinase I isoform delta"
FT /id="PRO_0000192836"
FT DOMAIN 9..277
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 278..364
FT /note="Centrosomal localization signal (CLS)"
FT /evidence="ECO:0000250"
FT REGION 301..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..342
FT /note="Autoinhibitory"
FT COMPBIAS 301..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 128
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027,
FT ECO:0000269|PubMed:8648628"
FT BINDING 15..23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48730"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48730"
FT MOD_RES 370
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:17594292"
FT MOD_RES 375
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9DC28"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48730"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48730"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48730"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48730"
FT VAR_SEQ 400..415
FT /note="IPGRVASSGLQSVVHR -> RSRDMASLRLHAARQGARCRPQRPRRTTY
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8454611"
FT /id="VSP_010255"
FT TURN 6..8
FT /evidence="ECO:0007829|PDB:1CKI"
FT STRAND 9..17
FT /evidence="ECO:0007829|PDB:1CKI"
FT STRAND 19..28
FT /evidence="ECO:0007829|PDB:1CKI"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:1CKI"
FT STRAND 34..42
FT /evidence="ECO:0007829|PDB:1CKI"
FT HELIX 49..58
FT /evidence="ECO:0007829|PDB:1CKI"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:1CKI"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:1CKI"
FT HELIX 89..95
FT /evidence="ECO:0007829|PDB:1CKI"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:1CKI"
FT HELIX 102..121
FT /evidence="ECO:0007829|PDB:1CKI"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:1CKI"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:1CKI"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:1CKI"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:1CKI"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:1CKI"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:1CKI"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:1CKI"
FT HELIX 192..208
FT /evidence="ECO:0007829|PDB:1CKI"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:1CKJ"
FT HELIX 225..234
FT /evidence="ECO:0007829|PDB:1CKI"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:1CKI"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:1CKI"
FT HELIX 246..257
FT /evidence="ECO:0007829|PDB:1CKI"
FT HELIX 266..279
FT /evidence="ECO:0007829|PDB:1CKI"
FT HELIX 289..292
FT /evidence="ECO:0007829|PDB:1CKI"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:1CKI"
SQ SEQUENCE 415 AA; 47316 MW; B97F04AF9EB466D2 CRC64;
MELRVGNRYR LGRKIGSGSF GDIYLGTDIA AGEEVAIKLE CVKTKHPQLH IESKIYKMMQ
GGVGIPTIRW CGAEGDYNVM VMELLGPSLE DLFNFCSRKF SLKTVLLLAD QMISRIEYIH
SKNFIHRDVK PDNFLMGLGK KGNLVYIIDF GLAKKYRDAR THQHIPYREN KNLTGTARYA
SINTHLGIEQ SRRDDLESLG YVLMYFNLGS LPWQGLKAAT KRQKYERISE KKMSTPIEVL
CKGYPSEFAT YLNFCRSLRF DDKPDYSYLR QLFRNLFHRQ GFSYDYVFDW NMLKFGASRA
ADDAERERRD REERLRHSRN PATRGLPSTA SGRLRGTQEV APPTPLTPTS HTANTSPRPV
SGMERERKVS MRLHRGAPVN VSSSDLTGRQ DTSRMSTSQI PGRVASSGLQ SVVHR
