GENTAUR Molecular Products.

 ELYS_MOUSE              Reviewed;        2243 AA.
 Q8CJF7; B2RRC8; Q8BVJ5; Q8VD55;
 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
 01-MAR-2003, sequence version 1.
 28-MAR-2018, entry version 127.
 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; -.
 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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