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Protein ELYS (Embryonic large molecule derived from yolk sac) (Protein MEL-28) (Putative AT-hook-containing transcription factor 1)

 ELYS_MOUSE              Reviewed;        2243 AA.
Q8CJF7; B2RRC8; Q8BVJ5; Q8VD55;
25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
12-SEP-2018, entry version 128.
RecName: Full=Protein ELYS;
AltName: Full=Embryonic large molecule derived from yolk sac;
AltName: Full=Protein MEL-28;
AltName: Full=Putative AT-hook-containing transcription factor 1;
Name=Ahctf1; Synonyms=Elys;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY,
DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
STRAIN=C57BL/6J; TISSUE=Yolk sac;
PubMed=11952839; DOI=10.1046/j.1365-2443.2002.00529.x;
Kimura N., Takizawa M., Okita K., Natori O., Igarashi K., Ueno M.,
Nakashima K., Nobuhisa I., Taga T.;
"Identification of a novel transcription factor, ELYS, expressed
predominantly in mouse foetal haematopoietic tissues.";
Genes Cells 7:435-446(2002).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=C57BL/6J; TISSUE=Liver;
PubMed=12745078; DOI=10.1016/S0006-291X(03)00772-1;
Okita K., Takizawa M., Ueno M., Kimura N., Nobuhisa I., Taga T.;
"Genomic organization and characterization of the mouse ELYS gene.";
Biochem. Biophys. Res. Commun. 305:327-332(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2082-2243.
STRAIN=C57BL/6J; TISSUE=Fetal head;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=15507119; DOI=10.1111/j.1365-2443.2004.00791.x;
Okita K., Kiyonari H., Nobuhisa I., Kimura N., Aizawa S., Taga T.;
"Targeted disruption of the mouse ELYS gene results in embryonic death
at peri-implantation development.";
Genes Cells 9:1083-1091(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1080 AND SER-1218, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1381, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528; THR-1083; SER-1138;
SER-1214; SER-1218; SER-1381; SER-1541; SER-1928; SER-2188 AND
SER-2198, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2221, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[10]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-494, REPEATS, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF TYR-284 AND 272-PHE--ARG-280.
PubMed=23499022; DOI=10.1016/j.str.2013.02.006;
Bilokapic S., Schwartz T.U.;
"Structural and functional studies of the 252 kDa nucleoporin ELYS
reveal distinct roles for its three tethered domains.";
Structure 21:572-580(2013).
-!- FUNCTION: Required for the assembly of a functional nuclear pore
complex (NPC) on the surface of chromosomes as nuclei form at the
end of mitosis. May initiate NPC assembly by binding to chromatin
and recruiting the Nup107-160 subcomplex of the NPC. Also required
for the localization of the Nup107-160 subcomplex of the NPC to
the kinetochore during mitosis and for the completion of
cytokinesis (By similarity). Has also been proposed to function as
a transcription factor which may play a specific role in
hematopoietic tissues (PubMed:11952839). {ECO:0000250,
ECO:0000269|PubMed:11952839}.
-!- SUBUNIT: Associates with the Nup107-160 subcomplex of the NPC.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
{ECO:0000250}. Nucleus, nucleoplasm {ECO:0000269|PubMed:11952839}.
Nucleus, nuclear pore complex {ECO:0000269|PubMed:23499022}.
Nucleus matrix {ECO:0000269|PubMed:23499022}. Cytoplasm
{ECO:0000269|PubMed:11952839}. Note=Localizes to the nuclear pore
complex (NPC) throughout interphase. Localizes to the kinetochore
from prophase, and this appears to require the Nup107-160
subcomplex of the NPC. Localizes to the periphery of chromatin
from late anaphase (By similarity).
{ECO:0000250|UniProtKB:Q8WYP5}.
-!- TISSUE SPECIFICITY: Widely expressed with higher expression in
testis, lung and kidney. Expressed in T-cells, B-cells and
granulocytes in bone marrow. {ECO:0000269|PubMed:11952839}.
-!- DEVELOPMENTAL STAGE: Expressed throughout the embryo at E3.5 and
E6.5. Higher expression is detected at 10.5 dpc nad then
progressively decreases. Highly expressed in fetal hematopoietic
tissues including liver, spleen and thymus. Expressed in the
endothelium lining the dorsal aorta of 11.5 dpc embryos (at
protein level). {ECO:0000269|PubMed:11952839,
ECO:0000269|PubMed:15507119}.
-!- DOMAIN: The N-terminus forms a highly conserved seven-bladed beta
propeller decorated with long loops and mediates anchorage to the
Nup107-160 subcomplex of the nuclear pore, synergistically with
the central alpha domain. The disordered C-terminus is responsible
for the interactions with chromatin (PubMed:23499022).
{ECO:0000269|PubMed:23499022}.
-!- DISRUPTION PHENOTYPE: Embryonic lethality before E7.5. Impaired
proliferation of the inner cells of the blastocyst due at least in
part to increased apoptosis. {ECO:0000269|PubMed:15507119}.
-!- SIMILARITY: Belongs to the ELYS family. {ECO:0000305}.
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EMBL; AB059278; BAB78517.1; -; mRNA.
EMBL; AB081498; BAC22610.1; -; Genomic_DNA.
EMBL; BC138343; AAI38344.1; -; mRNA.
EMBL; BC138344; AAI38345.1; -; mRNA.
EMBL; AK078022; BAC37101.2; ALT_SEQ; mRNA.
CCDS; CCDS15564.1; -.
RefSeq; NP_080651.2; NM_026375.2.
UniGene; Mm.128165; -.
PDB; 4I0O; X-ray; 1.90 A; A=1-494.
PDBsum; 4I0O; -.
ProteinModelPortal; Q8CJF7; -.
SMR; Q8CJF7; -.
BioGrid; 230549; 4.
IntAct; Q8CJF7; 2.
MINT; Q8CJF7; -.
STRING; 10090.ENSMUSP00000027768; -.
iPTMnet; Q8CJF7; -.
PhosphoSitePlus; Q8CJF7; -.
EPD; Q8CJF7; -.
MaxQB; Q8CJF7; -.
PaxDb; Q8CJF7; -.
PeptideAtlas; Q8CJF7; -.
PRIDE; Q8CJF7; -.
Ensembl; ENSMUST00000027768; ENSMUSP00000027768; ENSMUSG00000026491.
GeneID; 226747; -.
KEGG; mmu:226747; -.
UCSC; uc011wxn.1; mouse.
CTD; 25909; -.
MGI; MGI:1915033; Ahctf1.
eggNOG; ENOG410IG0H; Eukaryota.
eggNOG; ENOG410XQV6; LUCA.
GeneTree; ENSGT00390000018900; -.
HOGENOM; HOG000293244; -.
InParanoid; Q8CJF7; -.
OMA; FTWQVNI; -.
OrthoDB; EOG091G006H; -.
PhylomeDB; Q8CJF7; -.
TreeFam; TF350425; -.
Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-MMU-2467813; Separation of Sister Chromatids.
Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
Reactome; R-MMU-68877; Mitotic Prometaphase.
PRO; PR:Q8CJF7; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000026491; Expressed in 291 organ(s), highest expression level in embryo.
CleanEx; MM_AHCTF1; -.
ExpressionAtlas; Q8CJF7; baseline and differential.
Genevisible; Q8CJF7; MM.
GO; GO:0000785; C:chromatin; IEA:Ensembl.
GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0016363; C:nuclear matrix; IDA:MGI.
GO; GO:0031965; C:nuclear membrane; ISO:MGI.
GO; GO:0031080; C:nuclear pore outer ring; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:MGI.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0030097; P:hemopoiesis; TAS:UniProtKB.
GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
GO; GO:0051292; P:nuclear pore complex assembly; ISS:UniProtKB.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0032465; P:regulation of cytokinesis; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR032040; ELYS-bb.
InterPro; IPR025151; ELYS_dom.
Pfam; PF13934; ELYS; 1.
Pfam; PF16687; ELYS-bb; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Cell cycle; Cell division; Centromere;
Chromosome; Complete proteome; Cytoplasm; Developmental protein;
DNA-binding; Kinetochore; Mitosis; mRNA transport;
Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport;
Reference proteome; Transcription; Translocation; Transport.
CHAIN 1 2243 Protein ELYS.
/FTId=PRO_0000246320.
DNA_BIND 1955 1967 A.T hook. {ECO:0000250|UniProtKB:Q5U249}.
REGION 1 981 Necessary for cytoplasmic localization.
{ECO:0000269|PubMed:11952839}.
REGION 1 494 Seven-bladed beta propeller repeats.
{ECO:0000269|PubMed:23499022}.
REGION 591 1092 Important for nuclear localization.
{ECO:0000250|UniProtKB:Q8WYP5}.
REGION 1019 2243 Disordered.
{ECO:0000303|PubMed:23499022}.
REGION 1149 2243 Necessary for nuclear localization.
{ECO:0000269|PubMed:11952839}.
REGION 1447 1694 Mediates transcriptional activity.
{ECO:0000269|PubMed:11952839}.
REGION 1828 2243 Important for nuclear localization and
chromatin binding.
{ECO:0000250|UniProtKB:Q8WYP5}.
MOD_RES 528 528 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1080 1080 Phosphoserine.
{ECO:0000244|PubMed:17242355}.
MOD_RES 1083 1083 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1138 1138 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1142 1142 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WYP5}.
MOD_RES 1150 1150 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WYP5}.
MOD_RES 1155 1155 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WYP5}.
MOD_RES 1175 1175 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8WYP5}.
MOD_RES 1214 1214 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1218 1218 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 1222 1222 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WYP5}.
MOD_RES 1235 1235 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WYP5}.
MOD_RES 1381 1381 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 1517 1517 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8WYP5}.
MOD_RES 1533 1533 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WYP5}.
MOD_RES 1541 1541 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1725 1725 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WYP5}.
MOD_RES 1864 1864 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WYP5}.
MOD_RES 1870 1870 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WYP5}.
MOD_RES 1884 1884 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WYP5}.
MOD_RES 1928 1928 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1930 1930 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WYP5}.
MOD_RES 1980 1980 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WYP5}.
MOD_RES 2021 2021 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WYP5}.
MOD_RES 2099 2099 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WYP5}.
MOD_RES 2132 2132 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WYP5}.
MOD_RES 2188 2188 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2198 2198 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2202 2202 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WYP5}.
MOD_RES 2221 2221 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MUTAGEN 272 280 FQEPENDPR->GSGSGSGSG: Abolishes nuclear
pore localization; when associated with
S-284. {ECO:0000269|PubMed:23499022}.
MUTAGEN 284 284 Y->S: Abolishes nuclear pore
localization; when associated with 272-
GSGSGSGSG-280.
{ECO:0000269|PubMed:23499022}.
CONFLICT 1207 1207 F -> L (in Ref. 1; BAB78517).
{ECO:0000305}.
CONFLICT 1379 1379 A -> T (in Ref. 1; BAB78517).
{ECO:0000305}.
CONFLICT 1414 1414 A -> G (in Ref. 1; BAB78517).
{ECO:0000305}.
CONFLICT 1718 1718 H -> R (in Ref. 1; BAB78517).
{ECO:0000305}.
CONFLICT 2084 2084 T -> A (in Ref. 4; BAC37101).
{ECO:0000305}.
HELIX 17 24 {ECO:0000244|PDB:4I0O}.
STRAND 27 29 {ECO:0000244|PDB:4I0O}.
STRAND 35 38 {ECO:0000244|PDB:4I0O}.
STRAND 40 43 {ECO:0000244|PDB:4I0O}.
STRAND 45 50 {ECO:0000244|PDB:4I0O}.
STRAND 53 58 {ECO:0000244|PDB:4I0O}.
TURN 59 61 {ECO:0000244|PDB:4I0O}.
STRAND 64 69 {ECO:0000244|PDB:4I0O}.
STRAND 79 88 {ECO:0000244|PDB:4I0O}.
STRAND 91 99 {ECO:0000244|PDB:4I0O}.
STRAND 101 110 {ECO:0000244|PDB:4I0O}.
TURN 111 114 {ECO:0000244|PDB:4I0O}.
STRAND 115 124 {ECO:0000244|PDB:4I0O}.
STRAND 126 134 {ECO:0000244|PDB:4I0O}.
HELIX 140 142 {ECO:0000244|PDB:4I0O}.
HELIX 147 150 {ECO:0000244|PDB:4I0O}.
STRAND 152 160 {ECO:0000244|PDB:4I0O}.
STRAND 165 169 {ECO:0000244|PDB:4I0O}.
HELIX 181 183 {ECO:0000244|PDB:4I0O}.
STRAND 187 192 {ECO:0000244|PDB:4I0O}.
HELIX 197 206 {ECO:0000244|PDB:4I0O}.
STRAND 210 214 {ECO:0000244|PDB:4I0O}.
STRAND 223 229 {ECO:0000244|PDB:4I0O}.
TURN 230 233 {ECO:0000244|PDB:4I0O}.
STRAND 234 239 {ECO:0000244|PDB:4I0O}.
STRAND 242 248 {ECO:0000244|PDB:4I0O}.
TURN 249 251 {ECO:0000244|PDB:4I0O}.
STRAND 254 259 {ECO:0000244|PDB:4I0O}.
STRAND 267 273 {ECO:0000244|PDB:4I0O}.
STRAND 282 290 {ECO:0000244|PDB:4I0O}.
TURN 292 295 {ECO:0000244|PDB:4I0O}.
STRAND 299 313 {ECO:0000244|PDB:4I0O}.
STRAND 319 336 {ECO:0000244|PDB:4I0O}.
STRAND 347 359 {ECO:0000244|PDB:4I0O}.
STRAND 377 389 {ECO:0000244|PDB:4I0O}.
STRAND 396 403 {ECO:0000244|PDB:4I0O}.
HELIX 404 409 {ECO:0000244|PDB:4I0O}.
HELIX 422 424 {ECO:0000244|PDB:4I0O}.
STRAND 428 432 {ECO:0000244|PDB:4I0O}.
HELIX 434 440 {ECO:0000244|PDB:4I0O}.
STRAND 445 450 {ECO:0000244|PDB:4I0O}.
HELIX 452 454 {ECO:0000244|PDB:4I0O}.
HELIX 467 470 {ECO:0000244|PDB:4I0O}.
HELIX 472 474 {ECO:0000244|PDB:4I0O}.
STRAND 476 483 {ECO:0000244|PDB:4I0O}.
STRAND 486 492 {ECO:0000244|PDB:4I0O}.
SEQUENCE 2243 AA; 247646 MW; EEEA09B70F2B5691 CRC64;
MQDLTAQVTS DLLHFPEVTI EALGEDEITL ESVLRGKFAA GKNGLACLAC GPQLEVVNSL
TGERLSAYRF SGVNEQPPVV LAVKEFSWHK RTGLLIGLEE ADGSVLCLYD LGISRVVKAV
VLPGRVTAIE PIINHGGASA STQHLHPSLR WLFGVAAVVT DVGQILLIDL CLDDLSCSQN
EVEASDLEVI TGIPAEVPHI RERVMREGRH LCFQLVSPLG VAISTLSYIN RTNQLAVGFS
DGYLALWNMK SMKREYYTQL EGGRVPVHAV AFQEPENDPR NCCYLWAVQS TQDSEGDVLS
LHLLQLAFGD RKCLASGQIL YEGLEYCEER YTLDLAGGTF PLRGQTSNTK LLGCQSIERF
PSHGDREESM REALSPDTSV SVFTWQVNIY GQGKPSVYLG LFDINRWYHA QMPDSLRSGE
SLHNCSYFAL WSLDSVVSRT SPHHILDILV HERSLNRGVP PSYPPPEQFF NPSTFNFDAT
CLLDSGVIHV TCAGFQKETL TFLKKSGPTL NEVIPDSYNR CLVAGLLSPR LIDIQPSSLS
QEEQLEAILS AAIQTSSLGL LTGYIRTWII EEQPNSAANL RFVLEWTWNK VVLTKEEFDR
LCVPLFDGSC RFIDPQTIQS IQQCHLLLSN LSTVLSCFAM EAQGITERGL VDLSNKHMVT
QLLCQYAHMV LWFCHSGLLP EGLDDALQLS RLRYNYPVIQ NYYTSRRQKS ERSPRGKWNH
DCLMIDGLVS QLGDEVEKLW KRDEGGTGRY PPASIHALLD IYLLDNITEA SKHAITIYLL
LDIMYSFPNK TDTPIESFPT AFAISWGQVK LVQGFWLLDH NDYENGLDLL FHPVTAKPAS
WQHSKIIEAF MSQGEHKQAL RYLQTMKPTV SSSNEVILHL TVLLFNRCMV EAWNLLRQNS
NRVNIEELLK HAYEVCQEMG LMEDLLKLPF TNTEQECLVK FLQSSTSVEN HEFLLVHHLQ
RANYISALKL NQILKNNLMS DRDPRLRERS VTRNSILDQY GKILPRVQRK LAVERAKPYH
LSTSSVFHEV SRPKPLSAFP KKAITGTVLT RSTFISNVLS KIGEVWASHE PRNGVSLFNS
PKTEQPSPVV HSFPHPELPE AFVGTPISNT SQRISRLLDL VVHPVPQPSQ CLEFIQQSPT
RSPLCLLSSS LPLSSQFKRP HQNTSRPSEL LLLETPLIVK KAKSLALSAT SSGFAEFTPP
SILRSGFRTT PLASPSLSPG RSLTPPFRVK ETRISFMEEG MNTHWTDRAT DDRNTKAFVS
TSFHKCGLPA ETEWMKTSDK NTYFPLDVPA KGPQKVVAES LATHSGRLEK LDVSKEDSTA
STRSDQTSLE YHDAPSPEDL EGAVFVSPKP ASSSTELTTN STLQTERDND KDAFKSEGAP
SPVKKQIGTG DAAVEAFSEL SRLDPVERAE ASFAVSSVCE GETSTSNSKT SVLDGIVPIE
SRTSILTADH KESVANTVAD VESSGSTSSK CPVTSERSLG QKLTLNLKED EIEAHVPKEN
VGLPEESPRI SAAPSDTHEI HLIGCENLEV QNSEEEAKNL SFDELYPLGA EKLEYNLSTI
EQQFCDLPDD KDSAECDAAE VDGELFVAQS NFTLILEGEE GEAEASDSAA PNMLPKATKE
KPVCHREPHN QERVTDLPSA VTADQESHKV ETLPYVPEPV KVAIAENLLD VIKDTRSKEA
TPVAAGEAGD EDGAVIVSKA AHSSRLTNST PKTVKEPHAE TVNTSQNDDM VSSRTLTRRQ
HALSLNVTSE QEPSAVATPK KRTRKIKETP ESSERTCSDL KVAPENQLTA QSPPAPRRGK
KKDVSQGTLP SSGAVEPEPE PQGTPGRLRL RTQPPEPAAE ETPSRTKVRL SSVRKGTPRR
LKKSVENGQS TEILDDLKGS EAASHDGTVT ELRNANLEDT QNMEYKQDEH SDQQLPLKRK
RVREREVSVS SVTEEPKLDS SQLPLQTGLD VPATPRKRGR PRKVVPLEAD GGTTGKEQTS
PQKKDVPVVR RSTRNTPARN VSTLEKSVLV PNKEAALVVT SKRRPTKKSA EESSKDPSAA
VSDLAGGAAH TESADRRDGL LAAAALTPSA QGTRTRSRRT MLLTDISEPK TEPLFPPPSV
KVPKKKSKAE NMEAAAQLKE LVSDLSSQFV VSPPALRTRQ KSISNTSKLL GELESDPKPL
EIIEQKPKRS RTVKTRASRN TGKGSSWSPP PVEIKLVSPL ASPVDEIKTG KPRKTAEIAG
KTLGRGRKKP SSFPKQILRR KML


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