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Cyclin-dependent kinase 8 (EC 2.7.11.22) (EC 2.7.11.23) (Cell division protein kinase 8) (Mediator complex subunit CDK8) (Mediator of RNA polymerase II transcription subunit CDK8) (Protein kinase K35)

 CDK8_HUMAN              Reviewed;         464 AA.
P49336; Q5VUF3; Q6ISB5;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
22-NOV-2017, entry version 167.
RecName: Full=Cyclin-dependent kinase 8;
EC=2.7.11.22;
EC=2.7.11.23;
AltName: Full=Cell division protein kinase 8;
AltName: Full=Mediator complex subunit CDK8;
AltName: Full=Mediator of RNA polymerase II transcription subunit CDK8;
AltName: Full=Protein kinase K35;
Name=CDK8;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=7568034; DOI=10.1073/pnas.92.19.8871;
Tassan J.-P., Jaquenoud M., Leopold P., Schultz S.J., Nigg E.A.;
"Identification of human cyclin-dependent kinase 8, a putative protein
kinase partner for cyclin C.";
Proc. Natl. Acad. Sci. U.S.A. 92:8871-8875(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
MEDIATOR COMPLEX.
PubMed=9734358; DOI=10.1016/S1097-2765(00)80131-8;
Sun X., Zhang Y., Cho H., Rickert P., Lees E., Lane W.S., Reinberg D.;
"NAT, a human complex containing Srb polypeptides that functions as a
negative regulator of activated transcription.";
Mol. Cell 2:213-222(1998).
[6]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SMCC
COMPLEX.
PubMed=10024883; DOI=10.1016/S1097-2765(00)80178-1;
Gu W., Malik S., Ito M., Yuan C.-X., Fondell J.D., Zhang X.,
Martinez E., Qin J., Roeder R.G.;
"A novel human SRB/MED-containing cofactor complex, SMCC, involved in
transcription regulation.";
Mol. Cell 3:97-108(1999).
[7]
ERRATUM.
Gu W., Malik S., Ito M., Yuan C.-X., Fondell J.D., Zhang X.,
Martinez E., Qin J., Roeder R.G.;
Mol. Cell 3:541-541(1999).
[8]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-173.
PubMed=10993082; DOI=10.1038/35024111;
Akoulitchev S., Chuikov S., Reinberg D.;
"TFIIH is negatively regulated by cdk8-containing mediator
complexes.";
Nature 407:102-106(2000).
[9]
FUNCTION, AND INTERACTION WITH MAML1.
PubMed=15546612; DOI=10.1016/j.molcel.2004.10.014;
Fryer C.J., White J.B., Jones K.A.;
"Mastermind recruits CycC:CDK8 to phosphorylate the Notch ICD and
coordinate activation with turnover.";
Mol. Cell 16:509-520(2004).
[10]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
MEDIATOR COMPLEX.
PubMed=15175163; DOI=10.1016/j.molcel.2004.05.006;
Sato S., Tomomori-Sato C., Parmely T.J., Florens L., Zybailov B.,
Swanson S.K., Banks C.A.S., Jin J., Cai Y., Washburn M.P.,
Conaway J.W., Conaway R.C.;
"A set of consensus mammalian mediator subunits identified by
multidimensional protein identification technology.";
Mol. Cell 14:685-691(2004).
[11]
IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR
COMPLEX, AND ASSOCIATION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE
II.
PubMed=15989967; DOI=10.1016/j.molcel.2005.05.015;
Zhang X., Krutchinsky A., Fukuda A., Chen W., Yamamura S., Chait B.T.,
Roeder R.G.;
"MED1/TRAP220 exists predominantly in a TRAP/Mediator subpopulation
enriched in RNA polymerase II and is required for ER-mediated
transcription.";
Mol. Cell 19:89-100(2005).
[12]
INTERACTION WITH CTNNB1; GLI3; MED1; MED6; MED12 AND MED23.
PubMed=17000779; DOI=10.1128/MCB.00443-06;
Zhou H., Kim S., Ishii S., Boyer T.G.;
"Mediator modulates Gli3-dependent Sonic hedgehog signaling.";
Mol. Cell. Biol. 26:8667-8682(2006).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[14]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-403 IN COMPLEX WITH CCNC
AND INHIBITOR.
PubMed=21806996; DOI=10.1016/j.jmb.2011.07.020;
Schneider E.V., Bottcher J., Blaesse M., Neumann L., Huber R.,
Maskos K.;
"The structure of CDK8/CycC implicates specificity in the CDK/cyclin
family and reveals interaction with a deep pocket binder.";
J. Mol. Biol. 412:251-266(2011).
[15]
VARIANTS [LARGE SCALE ANALYSIS] ASN-189 AND CYS-424.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Component of the Mediator complex, a coactivator
involved in regulated gene transcription of nearly all RNA
polymerase II-dependent genes. Mediator functions as a bridge to
convey information from gene-specific regulatory proteins to the
basal RNA polymerase II transcription machinery. Mediator is
recruited to promoters by direct interactions with regulatory
proteins and serves as a scaffold for the assembly of a functional
preinitiation complex with RNA polymerase II and the general
transcription factors. Phosphorylates the CTD (C-terminal domain)
of the large subunit of RNA polymerase II (RNAp II), which may
inhibit the formation of a transcription initiation complex.
Phosphorylates CCNH leading to down-regulation of the TFIIH
complex and transcriptional repression. Recruited through
interaction with MAML1 to hyperphosphorylate the intracellular
domain of NOTCH, leading to its degradation.
{ECO:0000269|PubMed:10993082, ECO:0000269|PubMed:15546612}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:10993082}.
-!- CATALYTIC ACTIVITY: ATP + [DNA-directed RNA polymerase] = ADP +
[DNA-directed RNA polymerase] phosphate.
{ECO:0000269|PubMed:10993082}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- SUBUNIT: Component of the Mediator complex, which is composed of
MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13,
MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21,
MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31,
CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8
subunits form a distinct module termed the CDK8 module. Mediator
containing the CDK8 module is less active than Mediator lacking
this module in supporting transcriptional activation. Individual
preparations of the Mediator complex lacking one or more distinct
subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and
TRAP. The cylin/CDK pair formed by CCNC/CDK8 also associates with
the large subunit of RNA polymerase II. Interacts with CTNNB1,
GLI3 and MAML1. {ECO:0000269|PubMed:10024883,
ECO:0000269|PubMed:15175163, ECO:0000269|PubMed:15546612,
ECO:0000269|PubMed:15989967, ECO:0000269|PubMed:17000779,
ECO:0000269|PubMed:21806996, ECO:0000269|PubMed:9734358}.
-!- INTERACTION:
P24863:CCNC; NbExp=28; IntAct=EBI-394377, EBI-395261;
Q01094:E2F1; NbExp=3; IntAct=EBI-394377, EBI-448924;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P49336-1; Sequence=Displayed;
Name=2;
IsoId=P49336-2; Sequence=VSP_029970;
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
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EMBL; X85753; CAA59754.1; -; mRNA.
EMBL; AL590108; CAH72300.1; -; Genomic_DNA.
EMBL; AL159159; CAH72300.1; JOINED; Genomic_DNA.
EMBL; AL159159; CAI16960.1; -; Genomic_DNA.
EMBL; AL590108; CAI16960.1; JOINED; Genomic_DNA.
EMBL; CH471075; EAX08386.1; -; Genomic_DNA.
EMBL; CH471075; EAX08387.1; -; Genomic_DNA.
EMBL; BC069634; AAH69634.1; -; mRNA.
EMBL; BC104492; AAI04493.1; -; mRNA.
EMBL; BC105950; AAI05951.1; -; mRNA.
EMBL; BC107601; AAI07602.1; -; mRNA.
CCDS; CCDS9317.1; -. [P49336-1]
PIR; I37227; I37227.
RefSeq; NP_001251.1; NM_001260.2. [P49336-1]
RefSeq; NP_001305297.1; NM_001318368.1. [P49336-2]
UniGene; Hs.382306; -.
UniGene; Hs.695166; -.
PDB; 3RGF; X-ray; 2.20 A; A=1-403.
PDB; 4CRL; X-ray; 2.40 A; A=1-403.
PDB; 4F6S; X-ray; 2.60 A; A=1-403.
PDB; 4F6U; X-ray; 2.10 A; A=1-403.
PDB; 4F6W; X-ray; 2.39 A; A=1-403.
PDB; 4F70; X-ray; 3.00 A; A=1-403.
PDB; 4F7J; X-ray; 2.60 A; A=1-403.
PDB; 4F7L; X-ray; 2.90 A; A=1-403.
PDB; 4F7N; X-ray; 2.65 A; A=1-403.
PDB; 4F7S; X-ray; 2.20 A; A=1-403.
PDB; 4G6L; X-ray; 2.70 A; A=1-403.
PDB; 5BNJ; X-ray; 2.64 A; A=1-403.
PDB; 5CEI; X-ray; 2.24 A; A=1-403.
PDB; 5FGK; X-ray; 2.36 A; A=1-362.
PDB; 5HBE; X-ray; 2.38 A; A=1-362.
PDB; 5HBH; X-ray; 2.50 A; A=1-362.
PDB; 5HBJ; X-ray; 3.00 A; A=1-362.
PDB; 5HNB; X-ray; 2.35 A; A=1-362.
PDB; 5HVY; X-ray; 2.39 A; A=1-403.
PDB; 5I5Z; X-ray; 2.60 A; A=1-362.
PDB; 5ICP; X-ray; 2.18 A; A=1-362.
PDB; 5IDN; X-ray; 2.26 A; A=1-364.
PDB; 5IDP; X-ray; 2.65 A; A=1-364.
PDB; 5XQX; X-ray; 2.30 A; A=1-371.
PDB; 5XS2; X-ray; 2.04 A; A=1-371.
PDBsum; 3RGF; -.
PDBsum; 4CRL; -.
PDBsum; 4F6S; -.
PDBsum; 4F6U; -.
PDBsum; 4F6W; -.
PDBsum; 4F70; -.
PDBsum; 4F7J; -.
PDBsum; 4F7L; -.
PDBsum; 4F7N; -.
PDBsum; 4F7S; -.
PDBsum; 4G6L; -.
PDBsum; 5BNJ; -.
PDBsum; 5CEI; -.
PDBsum; 5FGK; -.
PDBsum; 5HBE; -.
PDBsum; 5HBH; -.
PDBsum; 5HBJ; -.
PDBsum; 5HNB; -.
PDBsum; 5HVY; -.
PDBsum; 5I5Z; -.
PDBsum; 5ICP; -.
PDBsum; 5IDN; -.
PDBsum; 5IDP; -.
PDBsum; 5XQX; -.
PDBsum; 5XS2; -.
ProteinModelPortal; P49336; -.
SMR; P49336; -.
BioGrid; 107458; 109.
CORUM; P49336; -.
DIP; DIP-32595N; -.
IntAct; P49336; 81.
MINT; MINT-3017285; -.
STRING; 9606.ENSP00000370938; -.
BindingDB; P49336; -.
ChEMBL; CHEMBL5719; -.
DrugBank; DB03496; Flavopiridol.
GuidetoPHARMACOLOGY; 1980; -.
iPTMnet; P49336; -.
PhosphoSitePlus; P49336; -.
BioMuta; CDK8; -.
DMDM; 1345718; -.
EPD; P49336; -.
MaxQB; P49336; -.
PaxDb; P49336; -.
PeptideAtlas; P49336; -.
PRIDE; P49336; -.
DNASU; 1024; -.
Ensembl; ENST00000381527; ENSP00000370938; ENSG00000132964. [P49336-1]
GeneID; 1024; -.
KEGG; hsa:1024; -.
UCSC; uc001uqr.2; human. [P49336-1]
CTD; 1024; -.
DisGeNET; 1024; -.
EuPathDB; HostDB:ENSG00000132964.11; -.
GeneCards; CDK8; -.
HGNC; HGNC:1779; CDK8.
HPA; HPA044721; -.
MIM; 603184; gene.
neXtProt; NX_P49336; -.
OpenTargets; ENSG00000132964; -.
PharmGKB; PA26315; -.
eggNOG; KOG0666; Eukaryota.
eggNOG; ENOG410XPPA; LUCA.
GeneTree; ENSGT00530000064012; -.
HOGENOM; HOG000233024; -.
HOVERGEN; HBG014652; -.
InParanoid; P49336; -.
KO; K02208; -.
OMA; FMVFEYA; -.
OrthoDB; EOG091G0812; -.
PhylomeDB; P49336; -.
TreeFam; TF101025; -.
BRENDA; 2.7.11.22; 2681.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
Reactome; R-HSA-212436; Generic Transcription Pathway.
Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
SignaLink; P49336; -.
SIGNOR; P49336; -.
ChiTaRS; CDK8; human.
GeneWiki; Cyclin-dependent_kinase_8; -.
GenomeRNAi; 1024; -.
PRO; PR:P49336; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000132964; -.
CleanEx; HS_CDK8; -.
ExpressionAtlas; P49336; baseline and differential.
Genevisible; P49336; HS.
GO; GO:0016592; C:mediator complex; IDA:MGI.
GO; GO:0005730; C:nucleolus; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0043234; C:protein complex; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0004672; F:protein kinase activity; TAS:ProtInc.
GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:Reactome.
GO; GO:0008353; F:RNA polymerase II carboxy-terminal domain kinase activity; IEA:UniProtKB-EC.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; ATP-binding;
Complete proteome; Kinase; Nucleotide-binding; Nucleus; Polymorphism;
Reference proteome; Repressor; Serine/threonine-protein kinase;
Transcription; Transcription regulation; Transferase.
CHAIN 1 464 Cyclin-dependent kinase 8.
/FTId=PRO_0000085797.
DOMAIN 21 335 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 27 35 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 1 15 Interaction with CCNC.
COMPBIAS 373 377 Poly-Gln.
ACT_SITE 151 151 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 52 52 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
VAR_SEQ 370 370 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_029970.
VARIANT 189 189 D -> N (in a lung neuroendocrine
carcinoma sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041980.
VARIANT 424 424 R -> C (in a colorectal adenocarcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041981.
MUTAGEN 173 173 D->A: Abrogates kinase activity and
TFIIH-dependent transcriptional
repression.
{ECO:0000269|PubMed:10993082}.
HELIX 3 12 {ECO:0000244|PDB:5XS2}.
HELIX 16 19 {ECO:0000244|PDB:5XS2}.
STRAND 26 30 {ECO:0000244|PDB:5XS2}.
STRAND 33 44 {ECO:0000244|PDB:5XS2}.
STRAND 49 58 {ECO:0000244|PDB:5XS2}.
HELIX 61 72 {ECO:0000244|PDB:5XS2}.
STRAND 83 87 {ECO:0000244|PDB:5XS2}.
TURN 88 91 {ECO:0000244|PDB:5XS2}.
STRAND 92 98 {ECO:0000244|PDB:5XS2}.
STRAND 101 103 {ECO:0000244|PDB:5XS2}.
HELIX 104 115 {ECO:0000244|PDB:5XS2}.
TURN 116 118 {ECO:0000244|PDB:5XS2}.
HELIX 125 144 {ECO:0000244|PDB:5XS2}.
HELIX 154 156 {ECO:0000244|PDB:5XS2}.
STRAND 157 159 {ECO:0000244|PDB:5XS2}.
TURN 164 167 {ECO:0000244|PDB:5XS2}.
STRAND 169 171 {ECO:0000244|PDB:5XS2}.
HELIX 179 181 {ECO:0000244|PDB:5ICP}.
STRAND 186 188 {ECO:0000244|PDB:5XS2}.
HELIX 202 205 {ECO:0000244|PDB:5XS2}.
HELIX 213 229 {ECO:0000244|PDB:5XS2}.
HELIX 249 259 {ECO:0000244|PDB:5XS2}.
TURN 264 266 {ECO:0000244|PDB:5XS2}.
HELIX 268 272 {ECO:0000244|PDB:5XS2}.
HELIX 276 282 {ECO:0000244|PDB:5XS2}.
HELIX 285 288 {ECO:0000244|PDB:5XS2}.
HELIX 293 299 {ECO:0000244|PDB:5XS2}.
HELIX 307 315 {ECO:0000244|PDB:5XS2}.
HELIX 320 322 {ECO:0000244|PDB:5XS2}.
HELIX 326 330 {ECO:0000244|PDB:5XS2}.
HELIX 333 335 {ECO:0000244|PDB:5XS2}.
STRAND 337 339 {ECO:0000244|PDB:5XS2}.
TURN 345 348 {ECO:0000244|PDB:5XS2}.
SEQUENCE 464 AA; 53284 MW; 00CBAB6CE354605F CRC64;
MDYDFKVKLS SERERVEDLF EYEGCKVGRG TYGHVYKAKR KDGKDDKDYA LKQIEGTGIS
MSACREIALL RELKHPNVIS LQKVFLSHAD RKVWLLFDYA EHDLWHIIKF HRASKANKKP
VQLPRGMVKS LLYQILDGIH YLHANWVLHR DLKPANILVM GEGPERGRVK IADMGFARLF
NSPLKPLADL DPVVVTFWYR APELLLGARH YTKAIDIWAI GCIFAELLTS EPIFHCRQED
IKTSNPYHHD QLDRIFNVMG FPADKDWEDI KKMPEHSTLM KDFRRNTYTN CSLIKYMEKH
KVKPDSKAFH LLQKLLTMDP IKRITSEQAM QDPYFLEDPL PTSDVFAGCQ IPYPKREFLT
EEEPDDKGDK KNQQQQQGNN HTNGTGHPGN QDSSHTQGPP LKKVRVVPPT TTSGGLIMTS
DYQRSNPHAA YPNPGPSTSQ PQSSMGYSAT SQQPPQYSHQ THRY


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