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Histone-lysine N-methyltransferase SETD1A (EC 2.1.1.43) (Lysine N-methyltransferase 2F) (SET domain-containing protein 1A) (hSET1A) (Set1/Ash2 histone methyltransferase complex subunit SET1)

 SET1A_HUMAN             Reviewed;        1707 AA.
O15047; A6NP62; Q6PIF3; Q8TAJ6;
21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
21-JUN-2005, sequence version 3.
25-OCT-2017, entry version 158.
RecName: Full=Histone-lysine N-methyltransferase SETD1A;
EC=2.1.1.43;
AltName: Full=Lysine N-methyltransferase 2F;
AltName: Full=SET domain-containing protein 1A;
Short=hSET1A;
AltName: Full=Set1/Ash2 histone methyltransferase complex subunit SET1;
Name=SETD1A;
Synonyms=KIAA0339 {ECO:0000312|EMBL:BAA20797.2}, KMT2F, SET1, SET1A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000312|EMBL:BAA20797.2}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain {ECO:0000312|EMBL:BAA20797.2};
PubMed=9205841; DOI=10.1093/dnares/4.2.141;
Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. VII.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 4:141-150(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[3] {ECO:0000305, ECO:0000312|EMBL:AAH27450.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-248 AND 1239-1707.
TISSUE=Brain {ECO:0000312|EMBL:AAH27450.1}, and
Duodenum {ECO:0000312|EMBL:AAH35795.1};
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).
[4] {ECO:0000305}
FUNCTION, AND INTERACTION WITH HCFC1.
PubMed=12670868; DOI=10.1101/gad.252103;
Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W.;
"Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4
methyltransferase are tethered together selectively by the cell-
proliferation factor HCF-1.";
Genes Dev. 17:896-911(2003).
[5]
IDENTIFICATION IN THE SET1 COMPLEX.
PubMed=16253997; DOI=10.1074/jbc.M508312200;
Lee J.-H., Skalnik D.G.;
"CpG-binding protein (CXXC finger protein 1) is a component of the
mammalian Set1 histone H3-Lys4 methyltransferase complex, the analogue
of the yeast Set1/COMPASS complex.";
J. Biol. Chem. 280:41725-41731(2005).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[7]
SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE SET1 COMPLEX.
PubMed=17355966; DOI=10.1074/jbc.M609809200;
Lee J.-H., Tate C.M., You J.-S., Skalnik D.G.;
"Identification and characterization of the human Set1B histone H3-
Lys4 methyltransferase complex.";
J. Biol. Chem. 282:13419-13428(2007).
[8]
IDENTIFICATION IN SET1 COMPLEX, AND INTERACTION WITH ASH2L; RBBP5;
CXXC1; HCFC1; WDR5; WDR82 AND POLR2A.
PubMed=17998332; DOI=10.1128/MCB.01356-07;
Lee J.H., Skalnik D.G.;
"Wdr82 is a C-terminal domain-binding protein that recruits the Setd1A
Histone H3-Lys4 methyltransferase complex to transcription start sites
of transcribed human genes.";
Mol. Cell. Biol. 28:609-618(2008).
[9]
IDENTIFICATION IN SET1 COMPLEX.
PubMed=18838538; DOI=10.1128/MCB.00976-08;
Wu M., Wang P.F., Lee J.S., Martin-Brown S., Florens L., Washburn M.,
Shilatifard A.;
"Molecular regulation of H3K4 trimethylation by Wdr82, a component of
human Set1/COMPASS.";
Mol. Cell. Biol. 28:7337-7344(2008).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[15]
INTERACTION WITH ZNF335.
PubMed=23178126; DOI=10.1016/j.cell.2012.10.043;
Yang Y.J., Baltus A.E., Mathew R.S., Murphy E.A., Evrony G.D.,
Gonzalez D.M., Wang E.P., Marshall-Walker C.A., Barry B.J., Murn J.,
Tatarakis A., Mahajan M.A., Samuels H.H., Shi Y., Golden J.A.,
Mahajnah M., Shenhav R., Walsh C.A.;
"Microcephaly gene links trithorax and REST/NRSF to control neural
stem cell proliferation and differentiation.";
Cell 151:1097-1112(2012).
[16]
INTERACTION WITH SUPT6H.
PubMed=22843687; DOI=10.1074/jbc.M112.351569;
Begum N.A., Stanlie A., Nakata M., Akiyama H., Honjo T.;
"The histone chaperone Spt6 is required for activation-induced
cytidine deaminase target determination through H3K4me3 regulation.";
J. Biol. Chem. 287:32415-32429(2012).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-459; SER-464; SER-565
AND SER-915, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1103, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Histone methyltransferase that specifically methylates
'Lys-4' of histone H3, when part of the SET1 histone
methyltransferase (HMT) complex, but not if the neighboring 'Lys-
9' residue is already methylated. H3 'Lys-4' methylation
represents a specific tag for epigenetic transcriptional
activation. The non-overlapping localization with SETD1B suggests
that SETD1A and SETD1B make non-redundant contributions to the
epigenetic control of chromatin structure and gene expression.
{ECO:0000269|PubMed:12670868}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
-!- SUBUNIT: Component of the SET1 complex, at least composed of the
catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5,
ASH2L/ASH2, CXXC1/CFP1, HCFC1 and DPY30. Interacts with HCFC1.
Interacts with ASH2/ASH2L, CXXC1/CFP1, WDR5 and RBBP5. Interacts
(via the RRM domain) with WDR82. Interacts (via the RRM domain)
with hyperphosphorylated C-terminal domain (CTD) of RNA polymerase
II large subunit (POLR2A) only in the presence of WDR82. Binds
specifically to CTD heptad repeats phosphorylated on 'Ser-5' of
each heptad. Interacts with ZNF335. Interacts with SUPT6H.
{ECO:0000269|PubMed:12670868, ECO:0000269|PubMed:16253997,
ECO:0000269|PubMed:17355966, ECO:0000269|PubMed:17998332,
ECO:0000269|PubMed:18838538, ECO:0000269|PubMed:22843687,
ECO:0000269|PubMed:23178126}.
-!- INTERACTION:
Q9UBL3-3:ASH2L; NbExp=2; IntAct=EBI-540779, EBI-16130425;
Q02248:Ctnnb1 (xeno); NbExp=2; IntAct=EBI-540779, EBI-397872;
P51610:HCFC1; NbExp=2; IntAct=EBI-540779, EBI-396176;
Q15291:RBBP5; NbExp=3; IntAct=EBI-540779, EBI-592823;
-!- SUBCELLULAR LOCATION: Nucleus speckle
{ECO:0000269|PubMed:17355966}. Chromosome
{ECO:0000269|PubMed:17355966}. Note=Localizes to a largely non-
overlapping set of euchromatic nuclear speckles with SETD1B,
suggesting that SETD1A and SETD1B each bind to a unique set of
target genes.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
-!- SEQUENCE CAUTION:
Sequence=AAH35795.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=BAA20797.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AB002337; BAA20797.2; ALT_INIT; mRNA.
EMBL; AC135048; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC027450; AAH27450.1; -; mRNA.
EMBL; BC035795; AAH35795.1; ALT_SEQ; mRNA.
CCDS; CCDS32435.1; -.
RefSeq; NP_055527.1; NM_014712.2.
RefSeq; XP_005255780.1; XM_005255723.1.
RefSeq; XP_006721169.1; XM_006721106.3.
RefSeq; XP_016879398.1; XM_017023909.1.
UniGene; Hs.297483; -.
PDB; 3S8S; X-ray; 1.30 A; A=89-197.
PDB; 3UVN; X-ray; 1.79 A; B/D=1492-1502.
PDB; 4EWR; X-ray; 1.50 A; C=1488-1501.
PDBsum; 3S8S; -.
PDBsum; 3UVN; -.
PDBsum; 4EWR; -.
ProteinModelPortal; O15047; -.
SMR; O15047; -.
BioGrid; 115088; 42.
CORUM; O15047; -.
DIP; DIP-33494N; -.
ELM; O15047; -.
IntAct; O15047; 20.
STRING; 9606.ENSP00000262519; -.
iPTMnet; O15047; -.
PhosphoSitePlus; O15047; -.
BioMuta; SETD1A; -.
EPD; O15047; -.
MaxQB; O15047; -.
PaxDb; O15047; -.
PeptideAtlas; O15047; -.
PRIDE; O15047; -.
DNASU; 9739; -.
Ensembl; ENST00000262519; ENSP00000262519; ENSG00000099381.
GeneID; 9739; -.
KEGG; hsa:9739; -.
UCSC; uc002ead.2; human.
CTD; 9739; -.
DisGeNET; 9739; -.
EuPathDB; HostDB:ENSG00000099381.16; -.
GeneCards; SETD1A; -.
HGNC; HGNC:29010; SETD1A.
HPA; HPA020646; -.
HPA; HPA058376; -.
MalaCards; SETD1A; -.
MIM; 611052; gene.
neXtProt; NX_O15047; -.
OpenTargets; ENSG00000099381; -.
PharmGKB; PA128394556; -.
eggNOG; KOG1080; Eukaryota.
eggNOG; COG2940; LUCA.
GeneTree; ENSGT00760000119228; -.
HOGENOM; HOG000154291; -.
HOVERGEN; HBG067119; -.
InParanoid; O15047; -.
KO; K11422; -.
OMA; QNQASPC; -.
OrthoDB; EOG091G00IV; -.
PhylomeDB; O15047; -.
TreeFam; TF106436; -.
BRENDA; 2.1.1.43; 2681.
Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
ChiTaRS; SETD1A; human.
GenomeRNAi; 9739; -.
PRO; PR:O15047; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000099381; -.
CleanEx; HS_SETD1A; -.
ExpressionAtlas; O15047; baseline and differential.
Genevisible; O15047; HS.
GO; GO:0035097; C:histone methyltransferase complex; IDA:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; IDA:ParkinsonsUK-UCL.
GO; GO:0005719; C:nuclear euchromatin; IEA:Ensembl.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0048188; C:Set1C/COMPASS complex; IDA:UniProtKB.
GO; GO:0008013; F:beta-catenin binding; IDA:BHF-UCL.
GO; GO:1990188; F:euchromatin binding; IEA:Ensembl.
GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IDA:UniProtKB.
GO; GO:0018024; F:histone-lysine N-methyltransferase activity; TAS:Reactome.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0008134; F:transcription factor binding; IPI:ParkinsonsUK-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; IEA:Ensembl.
GO; GO:2000648; P:positive regulation of stem cell proliferation; IEA:Ensembl.
GO; GO:1902275; P:regulation of chromatin organization; IDA:ParkinsonsUK-UCL.
GO; GO:0045646; P:regulation of erythrocyte differentiation; IEA:Ensembl.
GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; IDA:ParkinsonsUK-UCL.
GO; GO:0045652; P:regulation of megakaryocyte differentiation; TAS:Reactome.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0019827; P:stem cell population maintenance; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd12548; RRM_Set1A; 1.
InterPro; IPR024657; COMPASS_Set1_N-SET.
InterPro; IPR003616; Post-SET_dom.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
InterPro; IPR034467; Set1A_RRM.
InterPro; IPR001214; SET_dom.
Pfam; PF11764; N-SET; 1.
Pfam; PF00076; RRM_1; 1.
Pfam; PF00856; SET; 1.
SMART; SM01291; N-SET; 1.
SMART; SM00508; PostSET; 1.
SMART; SM00360; RRM; 1.
SMART; SM00317; SET; 1.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50868; POST_SET; 1.
PROSITE; PS50102; RRM; 1.
PROSITE; PS50280; SET; 1.
1: Evidence at protein level;
3D-structure; Activator; Chromatin regulator; Chromosome;
Complete proteome; Methyltransferase; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; RNA-binding;
S-adenosyl-L-methionine; Transcription; Transcription regulation;
Transferase.
CHAIN 1 1707 Histone-lysine N-methyltransferase
SETD1A.
/FTId=PRO_0000186056.
DOMAIN 84 172 RRM. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 1568 1685 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
DOMAIN 1691 1707 Post-SET. {ECO:0000255|PROSITE-
ProRule:PRU00155}.
REGION 1415 1450 Interaction with CFP1.
REGION 1450 1537 Interaction with ASH2L, RBBP5 and WDR5.
{ECO:0000269|PubMed:17998332}.
MOTIF 1299 1303 HCFC1-binding motif (HBM).
COMPBIAS 244 362 Ser-rich. {ECO:0000255}.
COMPBIAS 383 654 Pro-rich. {ECO:0000255}.
COMPBIAS 899 1010 Glu-rich. {ECO:0000255}.
COMPBIAS 1011 1062 Ser-rich. {ECO:0000255}.
COMPBIAS 1071 1194 Pro-rich. {ECO:0000255}.
COMPBIAS 1334 1375 Glu-rich. {ECO:0000255}.
COMPBIAS 1403 1417 Pro-rich. {ECO:0000255}.
MOD_RES 459 459 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 464 464 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 508 508 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 565 565 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 915 915 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1103 1103 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
VARIANT 639 639 D -> N (in dbSNP:rs897985).
/FTId=VAR_059318.
CONFLICT 242 248 PCSQDTS -> ACPVTHV (in Ref. 3; AAH35795).
{ECO:0000305}.
CONFLICT 1240 1242 TEE -> FLG (in Ref. 3; AAH27450).
{ECO:0000305}.
STRAND 95 100 {ECO:0000244|PDB:3S8S}.
HELIX 107 114 {ECO:0000244|PDB:3S8S}.
TURN 115 117 {ECO:0000244|PDB:3S8S}.
STRAND 120 127 {ECO:0000244|PDB:3S8S}.
TURN 129 131 {ECO:0000244|PDB:3S8S}.
STRAND 134 144 {ECO:0000244|PDB:3S8S}.
HELIX 145 155 {ECO:0000244|PDB:3S8S}.
STRAND 166 169 {ECO:0000244|PDB:3S8S}.
HELIX 174 184 {ECO:0000244|PDB:3S8S}.
TURN 190 192 {ECO:0000244|PDB:3S8S}.
HELIX 1494 1497 {ECO:0000244|PDB:4EWR}.
SEQUENCE 1707 AA; 186034 MW; 0084217B0D425050 CRC64;
MDQEGGGDGQ KAPSFQWRNY KLIVDPALDP ALRRPSQKVY RYDGVHFSVN DSKYIPVEDL
QDPRCHVRSK NRDFSLPVPK FKLDEFYIGQ IPLKEVTFAR LNDNVRETFL KDMCRKYGEV
EEVEILLHPR TRKHLGLARV LFTSTRGAKE TVKNLHLTSV MGNIIHAQLD IKGQQRMKYY
ELIVNGSYTP QTVPTGGKAL SEKFQGSGAA TETAESRRRS SSDTAAYPAG TTAVGTPGNG
TPCSQDTSFS SSRQDTPSSF GQFTPQSSQG TPYTSRGSTP YSQDSAYSSS TTSTSFKPRR
SENSYQDAFS RRHFSASSAS TTASTAIAAT TAATASSSAS SSSLSSSSSS SSSSSSSQFR
SSDANYPAYY ESWNRYQRHT SYPPRRATRE EPPGAPFAEN TAERFPPSYT SYLPPEPSRP
TDQDYRPPAS EAPPPEPPEP GGGGGGGGPS PEREEVRTSP RPASPARSGS PAPETTNESV
PFAQHSSLDS RIEMLLKEQR SKFSFLASDT EEEEENSSMV LGARDTGSEV PSGSGHGPCT
PPPAPANFED VAPTGSGEPG ATRESPKANG QNQASPCSSG DDMEISDDDR GGSPPPAPTP
PQQPPPPPPP PPPPPPYLAS LPLGYPPHQP AYLLPPRPDG PPPPEYPPPP PPPPHIYDFV
NSLELMDRLG AQWGGMPMSF QMQTQMLTRL HQLRQGKGLI AASAGPPGGA FGEAFLPFPP
PQEAAYGLPY ALYAQGQEGR GAYSREAYHL PMPMAAEPLP SSSVSGEEAR LPPREEAELA
EGKTLPTAGT VGRVLAMLVQ EMKSIMQRDL NRKMVENVAF GAFDQWWESK EEKAKPFQNA
AKQQAKEEDK EKTKLKEPGL LSLVDWAKSG GTTGIEAFAF GSGLRGALRL PSFKVKRKEP
SEISEASEEK RPRPSTPAEE DEDDPEQEKE AGEPGRPGTK PPKRDEERGK TQGKHRKSFA
LDSEGEEASQ ESSSEKDEED DEEDEEDEDR EEAVDTTKKE TEVSDGEDEE SDSSSKCSLY
ADSDGENDST SDSESSSSSS SSSSSSSSSS SSSSSSSSES SSEDEEEEER PAALPSASPP
PREVPVPTPA PVEVPVPERV AGSPVTPLPE QEASPARPAG PTEESPPSAP LRPPEPPAGP
PAPAPRPDER PSSPIPLLPP PKKRRKTVSF SAIEVVPAPE PPPATPPQAK FPGPASRKAP
RGVERTIRNL PLDHASLVKS WPEEVSRGGR SRAGGRGRLT EEEEAEPGTE VDLAVLADLA
LTPARRGLPA LPAVEDSEAT ETSDEAERPR PLLSHILLEH NYALAVKPTP PAPALRPPEP
VPAPAALFSS PADEVLEAPE VVVAEAEEPK PQQLQQQREE GEEEGEEEGE EEEEESSDSS
SSSDGEGALR RRSLRSHARR RRPPPPPPPP PPRAYEPRSE FEQMTILYDI WNSGLDSEDM
SYLRLTYERL LQQTSGADWL NDTHWVHHTI TNLTTPKRKR RPQDGPREHQ TGSARSEGYY
PISKKEKDKY LDVCPVSARQ LEGVDTQGTN RVLSERRSEQ RRLLSAIGTS AIMDSDLLKL
NQLKFRKKKL RFGRSRIHEW GLFAMEPIAA DEMVIEYVGQ NIRQMVADMR EKRYVQEGIG
SSYLFRVDHD TIIDATKCGN LARFINHCCT PNCYAKVITI ESQKKIVIYS KQPIGVDEEI
TYDYKFPLED NKIPCLCGTE SCRGSLN


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