ETS1_MOUSE
ID ETS1_MOUSE Reviewed; 440 AA.
AC P27577; Q61403;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Protein C-ets-1;
DE AltName: Full=p54;
GN Name=Ets1; Synonyms=Ets-1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Fibroblast;
RA Watson D.K., Seth A., Smyth F.E., Schweinfest C.W., Papas T.S.;
RT "The chicken, mouse and human ETS-1 proteins all have predicted masses of
RT 50 kDa, but have different electrophoretic mobilities.";
RL (In) Papas T.S. (eds.);
RL Oncogenesis, pp.221-232, Gulf Publishing Company, Houston (1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Thymus;
RX PubMed=2163347; DOI=10.1101/gad.4.4.667;
RA Gunther C.V., Nye J.A., Bryner R.S., Graves B.J.;
RT "Sequence-specific DNA binding of the proto-oncoprotein ets-1 defines a
RT transcriptional activator sequence within the long terminal repeat of the
RT Moloney murine sarcoma virus.";
RL Genes Dev. 4:667-679(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Thymus;
RX PubMed=2204020;
RA Chen J.H.;
RT "Cloning, sequencing, and expression of mouse c-ets-1 cDNA in baculovirus
RT expression system.";
RL Oncogene Res. 5:277-285(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH MAF.
RX PubMed=9566892; DOI=10.1128/mcb.18.5.2729;
RA Hedge S.P., Kumar A., Kurschner C., Shapiro L.H.;
RT "c-Maf interacts with c-Myb to regulate transcription of an early myeloid
RT gene during differentiation.";
RL Mol. Cell. Biol. 18:2729-2737(1998).
RN [6]
RP INTERACTION WITH MAFB.
RX PubMed=10790365; DOI=10.1093/emboj/19.9.1987;
RA Kelly L.M., Englmeier U., Lafon I., Sieweke M.H., Graf T.;
RT "MafB is an inducer of monocytic differentiation.";
RL EMBO J. 19:1987-1997(2000).
RN [7]
RP SUMOYLATION AT LYS-15 AND LYS-227, AND UBIQUITINATION.
RX PubMed=16862185; DOI=10.1038/sj.onc.1209789;
RA Ji Z., Degerny C., Vintonenko N., Deheuninck J., Foveau B., Leroy C.,
RA Coll J., Tulasne D., Baert J.-L., Fafeur V.;
RT "Regulation of the Ets-1 transcription factor by sumoylation and
RT ubiquitinylation.";
RL Oncogene 26:395-406(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251; SER-254; SER-282 AND
RP SER-285, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP STRUCTURE BY NMR OF 29-138, AND PHOSPHORYLATION AT THR-38.
RX PubMed=9770451; DOI=10.1073/pnas.95.21.12129;
RA Slupsky C.M., Gentile L.N., Donaldson L.W., Mackereth C.D., Seidel J.J.,
RA Graves B.J., McIntosh L.P.;
RT "Structure of the ets-1 pointed domain and mitogen-activated protein kinase
RT phosphorylation site.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:12129-12134(1998).
RN [10]
RP STRUCTURE BY NMR OF 332-415.
RX PubMed=8598195; DOI=10.1002/j.1460-2075.1996.tb00340.x;
RA Donaldson L.W., Petersen J.M., Graves B.J., McIntosh L.P.;
RT "Solution structure of the ETS domain from murine Ets-1: a winged helix-
RT turn-helix DNA binding motif.";
RL EMBO J. 15:125-134(1996).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 331-440 IN COMPLEX WITH HUMAN
RP PAX5 AND DNA.
RX PubMed=11779502; DOI=10.1016/s1097-2765(01)00410-5;
RA Garvie C.W., Hagman J., Wolberger C.;
RT "Structural studies of Ets-1/Pax5 complex formation on DNA.";
RL Mol. Cell 8:1267-1276(2001).
CC -!- FUNCTION: Transcription factor. Directly controls the expression of
CC cytokine and chemokine genes in a wide variety of different cellular
CC contexts. May control the differentiation, survival and proliferation
CC of lymphoid cells. May also regulate angiogenesis through regulation of
CC expression of genes controlling endothelial cell migration and invasion
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds DNA as a homodimer; homodimerization is required for
CC transcription activation. Interacts with DAXX (By similarity).
CC Interacts with UBE2I (By similarity). Interacts with SP100; the
CC interaction is direct and modulates ETS1 transcriptional activity (By
CC similarity). Interacts with MAF and MAFB. Interacts with PAX5; the
CC interaction alters DNA-binding properties. {ECO:0000250,
CC ECO:0000269|PubMed:10790365, ECO:0000269|PubMed:11779502,
CC ECO:0000269|PubMed:9566892}.
CC -!- INTERACTION:
CC P27577; P45481: Crebbp; NbExp=3; IntAct=EBI-4289053, EBI-296306;
CC P27577; P31314: TLX1; Xeno; NbExp=2; IntAct=EBI-4289053, EBI-2820655;
CC P27577; O43711: TLX3; Xeno; NbExp=2; IntAct=EBI-4289053, EBI-3939165;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P14921}. Nucleus
CC {ECO:0000250|UniProtKB:P14921}. Note=Delocalizes from nucleus to
CC cytoplasm when coexpressed with isoform Ets-1 p27.
CC {ECO:0000250|UniProtKB:P14921}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=At least 2 isoforms are produced.;
CC Name=1;
CC IsoId=P27577-1; Sequence=Displayed;
CC -!- PTM: Sumoylated on Lys-15 and Lys-227, preferentially with SUMO2; which
CC inhibits transcriptional activity. {ECO:0000269|PubMed:16862185}.
CC -!- PTM: Ubiquitinated; which induces proteasomal degradation.
CC {ECO:0000269|PubMed:16862185}.
CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
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DR EMBL; M58482; AAA63299.1; -; mRNA.
DR EMBL; X53953; CAA37904.1; -; mRNA.
DR EMBL; X55787; CAA39310.1; -; mRNA.
DR EMBL; BC010588; AAH10588.1; -; mRNA.
DR CCDS; CCDS22954.1; -. [P27577-1]
DR PIR; A30487; A35875.
DR PIR; I48291; I48291.
DR RefSeq; NP_035938.2; NM_011808.2. [P27577-1]
DR PDB; 1K78; X-ray; 2.25 A; B/F=331-440.
DR PDB; 1K79; X-ray; 2.40 A; A/D=331-440.
DR PDB; 1K7A; X-ray; 2.80 A; A/D=331-440.
DR PDB; 1MD0; X-ray; 2.00 A; A/B=300-440.
DR PDB; 1MDM; X-ray; 2.80 A; B=280-440.
DR PDB; 1R36; NMR; -; A=301-440.
DR PDB; 2JV3; NMR; -; A=29-138.
DR PDB; 2KMD; NMR; -; A=29-138.
DR PDB; 6DA1; X-ray; 2.00 A; A/B=301-440.
DR PDB; 6DAT; X-ray; 2.35 A; A/B/C/D=301-440.
DR PDBsum; 1K78; -.
DR PDBsum; 1K79; -.
DR PDBsum; 1K7A; -.
DR PDBsum; 1MD0; -.
DR PDBsum; 1MDM; -.
DR PDBsum; 1R36; -.
DR PDBsum; 2JV3; -.
DR PDBsum; 2KMD; -.
DR PDBsum; 6DA1; -.
DR PDBsum; 6DAT; -.
DR AlphaFoldDB; P27577; -.
DR BMRB; P27577; -.
DR SMR; P27577; -.
DR BioGRID; 204765; 4.
DR DIP; DIP-41848N; -.
DR IntAct; P27577; 5.
DR STRING; 10090.ENSMUSP00000034534; -.
DR iPTMnet; P27577; -.
DR PhosphoSitePlus; P27577; -.
DR EPD; P27577; -.
DR jPOST; P27577; -.
DR PaxDb; P27577; -.
DR PRIDE; P27577; -.
DR ProteomicsDB; 275486; -. [P27577-1]
DR Antibodypedia; 3750; 791 antibodies from 42 providers.
DR DNASU; 23871; -.
DR Ensembl; ENSMUST00000034534; ENSMUSP00000034534; ENSMUSG00000032035. [P27577-1]
DR GeneID; 23871; -.
DR KEGG; mmu:23871; -.
DR UCSC; uc009osb.1; mouse. [P27577-1]
DR CTD; 2113; -.
DR MGI; MGI:95455; Ets1.
DR VEuPathDB; HostDB:ENSMUSG00000032035; -.
DR eggNOG; KOG3806; Eukaryota.
DR GeneTree; ENSGT00940000159519; -.
DR InParanoid; P27577; -.
DR OMA; ADMECAD; -.
DR OrthoDB; 526256at2759; -.
DR PhylomeDB; P27577; -.
DR TreeFam; TF316214; -.
DR Reactome; R-MMU-2559585; Oncogene Induced Senescence.
DR BioGRID-ORCS; 23871; 1 hit in 77 CRISPR screens.
DR ChiTaRS; Ets1; mouse.
DR EvolutionaryTrace; P27577; -.
DR PRO; PR:P27577; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P27577; protein.
DR Bgee; ENSMUSG00000032035; Expressed in peripheral lymph node and 298 other tissues.
DR ExpressionAtlas; P27577; baseline and differential.
DR Genevisible; P27577; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0035035; F:histone acetyltransferase binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IMP:CAFA.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0001222; F:transcription corepressor binding; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0048870; P:cell motility; ISO:MGI.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0045786; P:negative regulation of cell cycle; ISO:MGI.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IMP:CACAO.
DR GO; GO:0030578; P:PML body organization; ISO:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISO:MGI.
DR GO; GO:1904996; P:positive regulation of leukocyte adhesion to vascular endothelial cell; ISO:MGI.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0045765; P:regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI.
DR GO; GO:0010715; P:regulation of extracellular matrix disassembly; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0046677; P:response to antibiotic; ISO:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISO:MGI.
DR CDD; cd08542; SAM_PNT-ETS-1; 1.
DR DisProt; DP00111; -.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR IDEAL; IID50005; -.
DR InterPro; IPR045688; Ets1_N_flank.
DR InterPro; IPR000418; Ets_dom.
DR InterPro; IPR046328; ETS_fam.
DR InterPro; IPR003118; Pointed_dom.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR041886; SAM_PNT-ETS-1.
DR InterPro; IPR016311; Transform_prot_C-ets.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11849; PTHR11849; 1.
DR Pfam; PF00178; Ets; 1.
DR Pfam; PF19525; Ets1_N_flank; 1.
DR Pfam; PF02198; SAM_PNT; 1.
DR PIRSF; PIRSF001698; Transforming_factor_C-ets; 1.
DR PRINTS; PR00454; ETSDOMAIN.
DR SMART; SM00413; ETS; 1.
DR SMART; SM00251; SAM_PNT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS00345; ETS_DOMAIN_1; 1.
DR PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR PROSITE; PS50061; ETS_DOMAIN_3; 1.
DR PROSITE; PS51433; PNT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; DNA-binding;
KW Immunity; Isopeptide bond; Nucleus; Phosphoprotein; Proto-oncogene;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..440
FT /note="Protein C-ets-1"
FT /id="PRO_0000204070"
FT DOMAIN 51..136
FT /note="PNT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00762"
FT DNA_BIND 335..415
FT /note="ETS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT REGION 130..243
FT /note="Activation domain; required for transcription
FT activation"
FT /evidence="ECO:0000250"
FT MOD_RES 8
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P14921"
FT MOD_RES 15
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P14921"
FT MOD_RES 38
FT /note="Phosphothreonine; by MAPK"
FT /evidence="ECO:0000269|PubMed:9770451"
FT MOD_RES 223
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P14921"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 265
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14921"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14921"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14921"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 305
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P14921"
FT CROSSLNK 8
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P14921"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P14921"
FT CROSSLNK 138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P14921"
FT CROSSLNK 227
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:16862185"
FT CONFLICT 28
FT /note="D -> E (in Ref. 1; AAA63299 and 3; CAA39310)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="L -> S (in Ref. 3; CAA39310)"
FT /evidence="ECO:0000305"
FT CONFLICT 51..52
FT /note="AT -> SY (in Ref. 3; CAA39310)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="G -> P (in Ref. 1; AAA63299)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="L -> R (in Ref. 3; CAA39310)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="E -> D (in Ref. 3; CAA39310)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="Q -> H (in Ref. 3; CAA39310)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="L -> V (in Ref. 3; CAA39310)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="D -> V (in Ref. 3; CAA39310)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="Q -> R (in Ref. 3; CAA39310)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="D -> E (in Ref. 3; CAA39310)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="A -> R (in Ref. 3; CAA39310)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="D -> N (in Ref. 3; CAA39310)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="G -> C (in Ref. 3; CAA39310)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="K -> S (in Ref. 3; CAA39310)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="G -> A (in Ref. 3; CAA39310)"
FT /evidence="ECO:0000305"
FT CONFLICT 408..409
FT /note="KR -> NA (in Ref. 3; CAA39310)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="R -> A (in Ref. 3; CAA39310)"
FT /evidence="ECO:0000305"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:2JV3"
FT HELIX 43..52
FT /evidence="ECO:0007829|PDB:2JV3"
FT HELIX 54..62
FT /evidence="ECO:0007829|PDB:2JV3"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:2JV3"
FT HELIX 74..88
FT /evidence="ECO:0007829|PDB:2JV3"
FT TURN 95..98
FT /evidence="ECO:0007829|PDB:2JV3"
FT HELIX 102..107
FT /evidence="ECO:0007829|PDB:2JV3"
FT HELIX 109..116
FT /evidence="ECO:0007829|PDB:2JV3"
FT HELIX 119..134
FT /evidence="ECO:0007829|PDB:2JV3"
FT HELIX 304..312
FT /evidence="ECO:0007829|PDB:1MD0"
FT TURN 313..315
FT /evidence="ECO:0007829|PDB:1MD0"
FT STRAND 318..321
FT /evidence="ECO:0007829|PDB:1R36"
FT HELIX 323..330
FT /evidence="ECO:0007829|PDB:1MD0"
FT HELIX 337..345
FT /evidence="ECO:0007829|PDB:1MD0"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:1MD0"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:1MD0"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:1K78"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:1MD0"
FT HELIX 368..379
FT /evidence="ECO:0007829|PDB:1MD0"
FT HELIX 386..395
FT /evidence="ECO:0007829|PDB:1MD0"
FT TURN 396..400
FT /evidence="ECO:0007829|PDB:1MD0"
FT STRAND 401..404
FT /evidence="ECO:0007829|PDB:1MD0"
FT STRAND 408..414
FT /evidence="ECO:0007829|PDB:1MD0"
FT HELIX 418..422
FT /evidence="ECO:0007829|PDB:1MD0"
FT HELIX 426..432
FT /evidence="ECO:0007829|PDB:1MD0"
SQ SEQUENCE 440 AA; 50202 MW; 151164D83C41B143 CRC64;
MKAAVDLKPT LTIIKTEKVD LELFPSPDME CADVPLLTPS SKEMMSQALK ATFSGFTKEQ
QRLGIPKDPR QWTETHVRDW VMWAVNEFSL KGVDFQKFCM SGAALCALGK ECFLELAPDF
VGDILWEHLE ILQKEDVKPY QVNGANPTYP ESCYTSDYFI SYGIEHAQCV PPSEFSEPSF
ITESYQTLHP ISSEELLSLK YENDYPSVIL QDPLQTDTLQ TDYFAIKQEV LTPDNMCLGR
ASRGKLGGQD SFESVESYDS CDRLTQSWSS QSSFNSLQRV PSYDSFDYED YPAALPNHKP
KGTFKDYVRD RADLNKDKPV IPAAALAGYT GSGPIQLWQF LLELLTDKSC QSFISWTGDG
WEFKLSDPDE VARRWGKRKN KPKMNYEKLS RGLRYYYDKN IIHKTAGKRY VYRFVCDLQS
LLGYTPEELH AMLDVKPDAD
