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Database: UniProt
Entry: P27577
LinkDB: P27577
Original site: P27577 
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   07-OCT-2020, entry version 201.
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}.
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   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   Antibodypedia; 3750; 723 antibodies.
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   eggNOG; KOG3806; Eukaryota.
DR   GeneTree; ENSGT00940000159519; -.
DR   InParanoid; P27577; -.
DR   KO; K02678; -.
DR   OrthoDB; 526256at2759; -.
DR   PhylomeDB; P27577; -.
DR   TreeFam; TF316214; -.
DR   Reactome; R-MMU-2559585; Oncogene Induced Senescence.
DR   BioGRID-ORCS; 23871; 1 hit in 20 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 thymus and 369 other tissues.
DR   ExpressionAtlas; P27577; baseline and differential.
DR   Genevisible; P27577; MM.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:InterPro.
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:0035035; F:histone acetyltransferase binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA 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:0060055; P:angiogenesis involved in wound healing; IEA:Ensembl.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0048870; P:cell motility; ISO:MGI.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
DR   GO; GO:0044849; P:estrous cycle; IEA:Ensembl.
DR   GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
DR   GO; GO:0021854; P:hypothalamus development; IEA:Ensembl.
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:0021983; P:pituitary gland development; IEA:Ensembl.
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:0051272; P:positive regulation of cellular component movement; 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 pri-miRNA transcription by RNA polymerase II; 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:0032355; P:response to estradiol; IEA:Ensembl.
DR   GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR   GO; GO:0070555; P:response to interleukin-1; IEA:Ensembl.
DR   GO; GO:0034616; P:response to laminar fluid shear stress; IEA:Ensembl.
DR   GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
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; IPR000418; Ets_dom.
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   Pfam; PF00178; Ets; 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:0000244|PubMed:21183079"
FT   MOD_RES         254
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|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:0000244|PubMed:21183079"
FT   MOD_RES         285
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|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:0000244|PDB:2JV3"
FT   HELIX           43..52
FT                   /evidence="ECO:0000244|PDB:2JV3"
FT   HELIX           54..62
FT                   /evidence="ECO:0000244|PDB:2JV3"
FT   STRAND          67..69
FT                   /evidence="ECO:0000244|PDB:2JV3"
FT   HELIX           74..88
FT                   /evidence="ECO:0000244|PDB:2JV3"
FT   TURN            95..98
FT                   /evidence="ECO:0000244|PDB:2JV3"
FT   HELIX           102..107
FT                   /evidence="ECO:0000244|PDB:2JV3"
FT   HELIX           109..116
FT                   /evidence="ECO:0000244|PDB:2JV3"
FT   HELIX           119..134
FT                   /evidence="ECO:0000244|PDB:2JV3"
FT   HELIX           304..312
FT                   /evidence="ECO:0000244|PDB:1MD0"
FT   TURN            313..315
FT                   /evidence="ECO:0000244|PDB:1MD0"
FT   STRAND          318..321
FT                   /evidence="ECO:0000244|PDB:1R36"
FT   HELIX           323..330
FT                   /evidence="ECO:0000244|PDB:1MD0"
FT   HELIX           337..345
FT                   /evidence="ECO:0000244|PDB:1MD0"
FT   HELIX           348..350
FT                   /evidence="ECO:0000244|PDB:1MD0"
FT   TURN            351..353
FT                   /evidence="ECO:0000244|PDB:1MD0"
FT   STRAND          354..356
FT                   /evidence="ECO:0000244|PDB:1K78"
FT   STRAND          362..364
FT                   /evidence="ECO:0000244|PDB:1MD0"
FT   HELIX           368..379
FT                   /evidence="ECO:0000244|PDB:1MD0"
FT   HELIX           386..395
FT                   /evidence="ECO:0000244|PDB:1MD0"
FT   TURN            396..400
FT                   /evidence="ECO:0000244|PDB:1MD0"
FT   STRAND          401..404
FT                   /evidence="ECO:0000244|PDB:1MD0"
FT   STRAND          408..414
FT                   /evidence="ECO:0000244|PDB:1MD0"
FT   HELIX           418..422
FT                   /evidence="ECO:0000244|PDB:1MD0"
FT   HELIX           426..432
FT                   /evidence="ECO:0000244|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
//
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