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Methylcytosine dioxygenase TET1 (EC 1.14.11.n2) (CXXC-type zinc finger protein 6) (Leukemia-associated protein with a CXXC domain) (Ten-eleven translocation 1 gene protein)

 TET1_HUMAN              Reviewed;        2136 AA.
Q8NFU7; Q5VUP7; Q7Z6B6; Q8TCR1; Q9C0I7;
03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
03-OCT-2006, sequence version 2.
10-OCT-2018, entry version 128.
RecName: Full=Methylcytosine dioxygenase TET1;
EC=1.14.11.n2 {ECO:0000269|PubMed:19372391, ECO:0000269|PubMed:21496894};
AltName: Full=CXXC-type zinc finger protein 6;
AltName: Full=Leukemia-associated protein with a CXXC domain;
AltName: Full=Ten-eleven translocation 1 gene protein;
Name=TET1 {ECO:0000303|PubMed:28397838, ECO:0000312|HGNC:HGNC:29484};
Synonyms=CXXC6, KIAA1676, LCX;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], VARIANT MET-1123, FUNCTION, TISSUE
SPECIFICITY, AND CHROMOSOMAL TRANSLOCATION WITH KMT2A/MLL1.
TISSUE=Leukemia;
PubMed=12124344;
Ono R., Taki T., Taketani T., Taniwaki M., Kobayashi H., Hayashi Y.;
"LCX, leukemia-associated protein with a CXXC domain, is fused to MLL
in acute myeloid leukemia with trilineage dysplasia having
t(10;11)(q22;q23).";
Cancer Res. 62:4075-4080(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1402-2136.
TISSUE=Brain;
PubMed=11214970; DOI=10.1093/dnares/7.6.347;
Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIX.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 7:347-355(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1665-2074.
TISSUE=Brain;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1809-2136.
TISSUE=Uterus;
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).
[6]
CHROMOSOMAL TRANSLOCATION WITH KMT2A/MLL1, TISSUE SPECIFICITY, AND
INVOLVEMENT IN ACUTE LEUKEMIAS.
PubMed=12646957; DOI=10.1038/sj.leu.2402834;
Lorsbach R.B., Moore J., Mathew S., Raimondi S.C., Mukatira S.T.,
Downing J.R.;
"TET1, a member of a novel protein family, is fused to MLL in acute
myeloid leukemia containing the t(10;11)(q22;q23).";
Leukemia 17:637-641(2003).
[7]
FUNCTION.
PubMed=19372393; DOI=10.1126/science.1169786;
Kriaucionis S., Heintz N.;
"The nuclear DNA base 5-hydroxymethylcytosine is present in Purkinje
neurons and the brain.";
Science 324:929-930(2009).
[8]
FUNCTION, CATALYTIC ACTIVITY, DNA-BINDING, COFACTOR, AND MUTAGENESIS
OF HIS-1672 AND ASP-1674.
PubMed=19372391; DOI=10.1126/science.1170116;
Tahiliani M., Koh K.P., Shen Y., Pastor W.A., Bandukwala H.,
Brudno Y., Agarwal S., Iyer L.M., Liu D.R., Aravind L., Rao A.;
"Conversion of 5-methylcytosine to 5-hydroxymethylcytosine in
mammalian DNA by the MLL fusion partner TET1.";
Science 324:930-935(2009).
[9]
FUNCTION IN DNA DEMETHYLATION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF
HIS-1672 AND ASP-1674.
PubMed=21496894; DOI=10.1016/j.cell.2011.03.022;
Guo J.U., Su Y., Zhong C., Ming G.L., Song H.;
"Hydroxylation of 5-methylcytosine by TET1 promotes active DNA
demethylation in the adult brain.";
Cell 145:423-434(2011).
[10]
INTERACTION WITH SIN3A.
PubMed=21490601; DOI=10.1038/nature10066;
Williams K., Christensen J., Pedersen M.T., Johansen J.V., Cloos P.A.,
Rappsilber J., Helin K.;
"TET1 and hydroxymethylcytosine in transcription and DNA methylation
fidelity.";
Nature 473:343-348(2011).
[11]
FUNCTION.
PubMed=21778364; DOI=10.1126/science.1210597;
Ito S., Shen L., Dai Q., Wu S.C., Collins L.B., Swenberg J.A., He C.,
Zhang Y.;
"Tet proteins can convert 5-methylcytosine to 5-formylcytosine and 5-
carboxylcytosine.";
Science 333:1300-1303(2011).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-871, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=25284789; DOI=10.1016/j.celrep.2014.08.071;
Takai H., Masuda K., Sato T., Sakaguchi Y., Suzuki T., Suzuki T.,
Koyama-Nasu R., Nasu-Nishimura Y., Katou Y., Ogawa H., Morishita Y.,
Kozuka-Hata H., Oyama M., Todo T., Ino Y., Mukasa A., Saito N.,
Toyoshima C., Shirahige K., Akiyama T.;
"5-Hydroxymethylcytosine plays a critical role in glioblastomagenesis
by recruiting the CHTOP-methylosome complex.";
Cell Rep. 9:48-60(2014).
[14]
VARIANT ASN-2056.
PubMed=28397838; DOI=10.1038/mp.2017.60;
Harripaul R., Vasli N., Mikhailov A., Rafiq M.A., Mittal K.,
Windpassinger C., Sheikh T.I., Noor A., Mahmood H., Downey S.,
Johnson M., Vleuten K., Bell L., Ilyas M., Khan F.S., Khan V.,
Moradi M., Ayaz M., Naeem F., Heidari A., Ahmed I., Ghadami S.,
Agha Z., Zeinali S., Qamar R., Mozhdehipanah H., John P., Mir A.,
Ansar M., French L., Ayub M., Vincent J.B.;
"Mapping autosomal recessive intellectual disability: combined
microarray and exome sequencing identifies 26 novel candidate genes in
192 consanguineous families.";
Mol. Psychiatry 23:973-984(2018).
-!- FUNCTION: Dioxygenase that catalyzes the conversion of the
modified genomic base 5-methylcytosine (5mC) into 5-
hydroxymethylcytosine (5hmC) and plays a key role in active DNA
demethylation. Also mediates subsequent conversion of 5hmC into 5-
formylcytosine (5fC), and conversion of 5fC to 5-carboxylcytosine
(5caC). Conversion of 5mC into 5hmC, 5fC and 5caC probably
constitutes the first step in cytosine demethylation. Methylation
at the C5 position of cytosine bases is an epigenetic modification
of the mammalian genome which plays an important role in
transcriptional regulation. In addition to its role in DNA
demethylation, plays a more general role in chromatin regulation.
Preferentially binds to CpG-rich sequences at promoters of both
transcriptionally active and Polycomb-repressed genes. Involved in
the recruitment of the O-GlcNAc transferase OGT to CpG-rich
transcription start sites of active genes, thereby promoting
histone H2B GlcNAcylation by OGT. Also involved in transcription
repression of a subset of genes through recruitment of
transcriptional repressors to promoters. Involved in the balance
between pluripotency and lineage commitment of cells it plays a
role in embryonic stem cells maintenance and inner cell mass cell
specification. Plays an important role in the tumorigenicity of
glioblastoma cells. TET1-mediated production of 5hmC acts as a
recruitment signal for the CHTOP-methylosome complex to selective
sites on the chromosome, where it methylates H4R3 and activates
the transcription of genes involved in glioblastomagenesis
(PubMed:25284789). {ECO:0000269|PubMed:12124344,
ECO:0000269|PubMed:19372391, ECO:0000269|PubMed:19372393,
ECO:0000269|PubMed:21496894, ECO:0000269|PubMed:21778364,
ECO:0000269|PubMed:25284789}.
-!- CATALYTIC ACTIVITY: DNA 5-methylcytosine + 2-oxoglutarate + O(2) =
DNA 5-hydroxymethylcytosine + succinate + CO(2).
{ECO:0000269|PubMed:19372391, ECO:0000269|PubMed:21496894}.
-!- CATALYTIC ACTIVITY: DNA 5-hydroxymethylcytosine + 2-oxoglutarate +
O(2) = DNA 5-formylcytosine + succinate + CO(2).
{ECO:0000305|PubMed:21778364}.
-!- CATALYTIC ACTIVITY: DNA 5-formylcytosine + 2-oxoglutarate + O(2) =
DNA 5-carboxylcytosine + succinate + CO(2).
{ECO:0000305|PubMed:21778364}.
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000269|PubMed:19372391};
Note=Binds 1 Fe(2+) ion per subunit.
{ECO:0000269|PubMed:19372391};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 3 zinc ions per subunit. The zinc ions have a
structural role. {ECO:0000250};
-!- SUBUNIT: Interacts with HCFC1 and OGT (By similarity). Interacts
with SIN3A; recruits the transcriptional corepressor SIN3A to gene
promoters (PubMed:21490601). Found in a complex composed of at
least SINHCAF, SIN3A, HDAC1, SAP30, RBBP4, OGT and TET1 (By
similarity). {ECO:0000250|UniProtKB:Q3URK3,
ECO:0000269|PubMed:21490601}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed in fetal heart, lung and brain, and
in adult skeletal muscle, thymus and ovary. Not detected in adult
heart, lung or brain. Up-regulated in glioblastoma cells (at
protein level) (PubMed:25284789). {ECO:0000269|PubMed:12124344,
ECO:0000269|PubMed:12646957, ECO:0000269|PubMed:25284789}.
-!- PTM: Glycosylated. Interaction with OGT leads to GlcNAcylation (By
similarity). {ECO:0000250}.
-!- DISEASE: Note=A chromosomal aberration involving TET1 may be a
cause of acute leukemias (PubMed:12646957). Translocation
t(10;11)(q22;q23) with KMT2A/MLL1. This is a rare chromosomal
translocation 5' KMT2A/MLL1-TET1 3' (PubMed:12124344,
PubMed:12646957). {ECO:0000269|PubMed:12124344,
ECO:0000269|PubMed:12646957}.
-!- SIMILARITY: Belongs to the TET family. {ECO:0000305}.
-!- CAUTION: Subsequent steps in cytosine demethylation are subject to
discussion. According to a first model cytosine demethylation
occurs through deamination of 5hmC into 5-hydroxymethyluracil
(5hmU) and subsequent replacement by unmethylated cytosine by the
base excision repair system (PubMed:21496894). According to
another model, cytosine demethylation is rather mediated via
conversion of 5hmC into 5fC and 5caC, followed by excision by TDG
and replacement by unmethylated cytosine.
{ECO:0000305|PubMed:21496894}.
-!- SEQUENCE CAUTION:
Sequence=CAD28467.3; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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EMBL; AF430147; AAM88301.1; -; mRNA.
EMBL; AL513534; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL713888; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AB051463; BAB21767.1; -; mRNA.
EMBL; AL713658; CAD28467.3; ALT_SEQ; mRNA.
EMBL; BC053905; AAH53905.1; -; mRNA.
CCDS; CCDS7281.1; -.
RefSeq; NP_085128.2; NM_030625.2.
UniGene; Hs.258855; -.
UniGene; Hs.567594; -.
UniGene; Hs.598166; -.
UniGene; Hs.708977; -.
PDB; 6ASD; X-ray; 1.85 A; C=587-632.
PDBsum; 6ASD; -.
ProteinModelPortal; Q8NFU7; -.
SMR; Q8NFU7; -.
BioGrid; 123225; 3.
ComplexPortal; CPX-3323; SIN3A histone deacetylase complex, ES cell-specific variant.
IntAct; Q8NFU7; 2.
MINT; Q8NFU7; -.
STRING; 9606.ENSP00000362748; -.
iPTMnet; Q8NFU7; -.
PhosphoSitePlus; Q8NFU7; -.
BioMuta; TET1; -.
DMDM; 115502139; -.
EPD; Q8NFU7; -.
PaxDb; Q8NFU7; -.
PeptideAtlas; Q8NFU7; -.
PRIDE; Q8NFU7; -.
ProteomicsDB; 73363; -.
DNASU; 80312; -.
Ensembl; ENST00000373644; ENSP00000362748; ENSG00000138336.
GeneID; 80312; -.
KEGG; hsa:80312; -.
UCSC; uc001jok.5; human.
CTD; 80312; -.
DisGeNET; 80312; -.
EuPathDB; HostDB:ENSG00000138336.8; -.
GeneCards; TET1; -.
HGNC; HGNC:29484; TET1.
HPA; HPA019032; -.
HPA; HPA057273; -.
MIM; 607790; gene.
neXtProt; NX_Q8NFU7; -.
OpenTargets; ENSG00000138336; -.
PharmGKB; PA162405605; -.
eggNOG; ENOG410IE22; Eukaryota.
eggNOG; ENOG410XPWW; LUCA.
GeneTree; ENSGT00910000144072; -.
HOGENOM; HOG000154549; -.
InParanoid; Q8NFU7; -.
KO; K13097; -.
OMA; NQKAHPL; -.
OrthoDB; EOG091G007O; -.
PhylomeDB; Q8NFU7; -.
TreeFam; TF324004; -.
Reactome; R-HSA-5221030; TET1,2,3 and TDG demethylate DNA.
ChiTaRS; TET1; human.
GeneWiki; Tet_methylcytosine_dioxygenase_1; -.
GenomeRNAi; 80312; -.
PRO; PR:Q8NFU7; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000138336; Expressed in 103 organ(s), highest expression level in heart.
CleanEx; HS_TET1; -.
Genevisible; Q8NFU7; HS.
GO; GO:0005634; C:nucleus; IC:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
GO; GO:0070579; F:methylcytosine dioxygenase activity; IDA:UniProtKB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
GO; GO:0080111; P:DNA demethylation; IMP:UniProtKB.
GO; GO:0001826; P:inner cell mass cell differentiation; ISS:UniProtKB.
GO; GO:0090310; P:negative regulation of methylation-dependent chromatin silencing; IMP:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0031062; P:positive regulation of histone methylation; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0006493; P:protein O-linked glycosylation; ISS:UniProtKB.
GO; GO:0019827; P:stem cell population maintenance; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR024779; 2OGFeDO_noxygenase_dom.
InterPro; IPR002857; Znf_CXXC.
Pfam; PF12851; Tet_JBP; 1.
Pfam; PF02008; zf-CXXC; 1.
SMART; SM01333; Tet_JBP; 1.
PROSITE; PS51058; ZF_CXXC; 1.
1: Evidence at protein level;
3D-structure; Activator; Chromatin regulator;
Chromosomal rearrangement; Complete proteome; Dioxygenase;
DNA-binding; Glycoprotein; Iron; Metal-binding; Nucleus;
Oxidoreductase; Phosphoprotein; Polymorphism; Reference proteome;
Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
CHAIN 1 2136 Methylcytosine dioxygenase TET1.
/FTId=PRO_0000251949.
ZN_FING 584 625 CXXC-type. {ECO:0000255|PROSITE-
ProRule:PRU00509}.
REGION 528 674 Sufficient for binding to genomic CpG
islands.
REGION 1580 1593 Interaction with DNA. {ECO:0000250}.
REGION 2043 2045 2-oxoglutarate binding. {ECO:0000250}.
REGION 2049 2051 Substrate binding. {ECO:0000250}.
METAL 1422 1422 Zinc 1. {ECO:0000250}.
METAL 1424 1424 Zinc 1. {ECO:0000250}.
METAL 1482 1482 Zinc 2. {ECO:0000250}.
METAL 1508 1508 Zinc 1; via pros nitrogen. {ECO:0000250}.
METAL 1510 1510 Zinc 1. {ECO:0000250}.
METAL 1561 1561 Zinc 2. {ECO:0000250}.
METAL 1563 1563 Zinc 2. {ECO:0000250}.
METAL 1579 1579 Zinc 3. {ECO:0000250}.
METAL 1588 1588 Zinc 3. {ECO:0000250}.
METAL 1648 1648 Zinc 3. {ECO:0000250}.
METAL 1670 1670 Zinc 2; via tele nitrogen. {ECO:0000250}.
METAL 1672 1672 Iron; catalytic.
METAL 1674 1674 Iron; catalytic.
METAL 2028 2028 Iron; catalytic. {ECO:0000250}.
METAL 2059 2059 Zinc 3; via pros nitrogen. {ECO:0000250}.
BINDING 1551 1551 2-oxoglutarate. {ECO:0000250}.
BINDING 1664 1664 2-oxoglutarate. {ECO:0000250}.
BINDING 1677 1677 Substrate. {ECO:0000250}.
BINDING 1706 1706 2-oxoglutarate. {ECO:0000250}.
SITE 1608 1609 Breakpoint for translocation to form
KMT2A/MLL1-TET1 oncogene.
MOD_RES 871 871 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VARIANT 162 162 D -> G (in dbSNP:rs10823229).
/FTId=VAR_027734.
VARIANT 193 193 S -> T (in dbSNP:rs12773594).
/FTId=VAR_027735.
VARIANT 256 256 A -> V (in dbSNP:rs12221107).
/FTId=VAR_027736.
VARIANT 1018 1018 N -> S (in dbSNP:rs16925541).
/FTId=VAR_027737.
VARIANT 1123 1123 I -> M (in dbSNP:rs3998860).
{ECO:0000269|PubMed:12124344}.
/FTId=VAR_027738.
VARIANT 2056 2056 K -> N (found in a consanguineous family
with intellectual disability; unknown
pathological significance).
{ECO:0000269|PubMed:28397838}.
/FTId=VAR_080763.
MUTAGEN 1672 1672 H->Y: Loss of catalytic activity and loss
of the ability to induce DNA
demethylation.
{ECO:0000269|PubMed:19372391,
ECO:0000269|PubMed:21496894}.
MUTAGEN 1674 1674 D->A: Loss of catalytic activity and loss
of the ability to induce DNA
demethylation.
{ECO:0000269|PubMed:19372391,
ECO:0000269|PubMed:21496894}.
CONFLICT 2001 2001 F -> L (in Ref. 4; CAD28467).
{ECO:0000305}.
HELIX 595 598 {ECO:0000244|PDB:6ASD}.
STRAND 604 606 {ECO:0000244|PDB:6ASD}.
HELIX 607 610 {ECO:0000244|PDB:6ASD}.
TURN 611 614 {ECO:0000244|PDB:6ASD}.
TURN 620 622 {ECO:0000244|PDB:6ASD}.
HELIX 625 628 {ECO:0000244|PDB:6ASD}.
SEQUENCE 2136 AA; 235309 MW; 66E24EF0594A964C CRC64;
MSRSRHARPS RLVRKEDVNK KKKNSQLRKT TKGANKNVAS VKTLSPGKLK QLIQERDVKK
KTEPKPPVPV RSLLTRAGAA RMNLDRTEVL FQNPESLTCN GFTMALRSTS LSRRLSQPPL
VVAKSKKVPL SKGLEKQHDC DYKILPALGV KHSENDSVPM QDTQVLPDIE TLIGVQNPSL
LKGKSQETTQ FWSQRVEDSK INIPTHSGPA AEILPGPLEG TRCGEGLFSE ETLNDTSGSP
KMFAQDTVCA PFPQRATPKV TSQGNPSIQL EELGSRVESL KLSDSYLDPI KSEHDCYPTS
SLNKVIPDLN LRNCLALGGS TSPTSVIKFL LAGSKQATLG AKPDHQEAFE ATANQQEVSD
TTSFLGQAFG AIPHQWELPG ADPVHGEALG ETPDLPEIPG AIPVQGEVFG TILDQQETLG
MSGSVVPDLP VFLPVPPNPI ATFNAPSKWP EPQSTVSYGL AVQGAIQILP LGSGHTPQSS
SNSEKNSLPP VMAISNVENE KQVHISFLPA NTQGFPLAPE RGLFHASLGI AQLSQAGPSK
SDRGSSQVSV TSTVHVVNTT VVTMPVPMVS TSSSSYTTLL PTLEKKKRKR CGVCEPCQQK
TNCGECTYCK NRKNSHQICK KRKCEELKKK PSVVVPLEVI KENKRPQREK KPKVLKADFD
NKPVNGPKSE SMDYSRCGHG EEQKLELNPH TVENVTKNED SMTGIEVEKW TQNKKSQLTD
HVKGDFSANV PEAEKSKNSE VDKKRTKSPK LFVQTVRNGI KHVHCLPAET NVSFKKFNIE
EFGKTLENNS YKFLKDTANH KNAMSSVATD MSCDHLKGRS NVLVFQQPGF NCSSIPHSSH
SIINHHASIH NEGDQPKTPE NIPSKEPKDG SPVQPSLLSL MKDRRLTLEQ VVAIEALTQL
SEAPSENSSP SKSEKDEESE QRTASLLNSC KAILYTVRKD LQDPNLQGEP PKLNHCPSLE
KQSSCNTVVF NGQTTTLSNS HINSATNQAS TKSHEYSKVT NSLSLFIPKS NSSKIDTNKS
IAQGIITLDN CSNDLHQLPP RNNEVEYCNQ LLDSSKKLDS DDLSCQDATH TQIEEDVATQ
LTQLASIIKI NYIKPEDKKV ESTPTSLVTC NVQQKYNQEK GTIQQKPPSS VHNNHGSSLT
KQKNPTQKKT KSTPSRDRRK KKPTVVSYQE NDRQKWEKLS YMYGTICDIW IASKFQNFGQ
FCPHDFPTVF GKISSSTKIW KPLAQTRSIM QPKTVFPPLT QIKLQRYPES AEEKVKVEPL
DSLSLFHLKT ESNGKAFTDK AYNSQVQLTV NANQKAHPLT QPSSPPNQCA NVMAGDDQIR
FQQVVKEQLM HQRLPTLPGI SHETPLPESA LTLRNVNVVC SGGITVVSTK SEEEVCSSSF
GTSEFSTVDS AQKNFNDYAM NFFTNPTKNL VSITKDSELP TCSCLDRVIQ KDKGPYYTHL
GAGPSVAAVR EIMENRYGQK GNAIRIEIVV YTGKEGKSSH GCPIAKWVLR RSSDEEKVLC
LVRQRTGHHC PTAVMVVLIM VWDGIPLPMA DRLYTELTEN LKSYNGHPTD RRCTLNENRT
CTCQGIDPET CGASFSFGCS WSMYFNGCKF GRSPSPRRFR IDPSSPLHEK NLEDNLQSLA
TRLAPIYKQY APVAYQNQVE YENVARECRL GSKEGRPFSG VTACLDFCAH PHRDIHNMNN
GSTVVCTLTR EDNRSLGVIP QDEQLHVLPL YKLSDTDEFG SKEGMEAKIK SGAIEVLAPR
RKKRTCFTQP VPRSGKKRAA MMTEVLAHKI RAVEKKPIPR IKRKNNSTTT NNSKPSSLPT
LGSNTETVQP EVKSETEPHF ILKSSDNTKT YSLMPSAPHP VKEASPGFSW SPKTASATPA
PLKNDATASC GFSERSSTPH CTMPSGRLSG ANAAAADGPG ISQLGEVAPL PTLSAPVMEP
LINSEPSTGV TEPLTPHQPN HQPSFLTSPQ DLASSPMEED EQHSEADEPP SDEPLSDDPL
SPAEEKLPHI DEYWSDSEHI FLDANIGGVA IAPAHGSVLI ECARRELHAT TPVEHPNRNH
PTRLSLVFYQ HKNLNKPQHG FELNKIKFEA KEAKNKKMKA SEQKDQAANE GPEQSSEVNE
LNQIPSHKAL TLTHDNVVTV SPYALTHVAG PYNHWV


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