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Database: UniProt
Entry: ETS1_MOUSE
LinkDB: ETS1_MOUSE
Original site: 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   18-SEP-2019, entry version 195.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   of 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
RT   a transcriptional activator sequence within the long terminal repeat
RT   of the 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
RT   baculovirus 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
RT   project: 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
RT   myeloid 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
RP   AND SER-285, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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
RT   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.,
RA   Seidel J.J., Graves B.J., McIntosh L.P.;
RT   "Structure of the ets-1 pointed domain and mitogen-activated protein
RT   kinase 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
RT   helix-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
RP   HUMAN 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
CC       of cytokine and chemokine genes in a wide variety of different
CC       cellular contexts. May control the differentiation, survival and
CC       proliferation of lymphoid cells. May also regulate angiogenesis
CC       through regulation of expression of genes controlling endothelial
CC       cell migration and invasion (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds DNA as a homodimer; homodimerization is required
CC       for 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
CC       (By similarity). Interacts with MAF and MAFB. Interacts with PAX5;
CC       the interaction alters DNA-binding properties. {ECO:0000250,
CC       ECO:0000269|PubMed:10790365, ECO:0000269|PubMed:11779502,
CC       ECO:0000269|PubMed:9566892}.
CC   -!- INTERACTION:
CC       P45481:Crebbp; NbExp=3; IntAct=EBI-4289053, EBI-296306;
CC       P31314:TLX1 (xeno); NbExp=2; IntAct=EBI-4289053, EBI-2820655;
CC       O43711:TLX3 (xeno); NbExp=2; IntAct=EBI-4289053, EBI-3939165;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P14921}.
CC       Nucleus {ECO:0000250|UniProtKB:P14921}. Note=Delocalizes from
CC       nucleus to 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;
CC       which inhibits transcriptional activity.
CC       {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   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   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   eggNOG; ENOG410Z0ZF; LUCA.
DR   GeneTree; ENSGT00940000159519; -.
DR   HOGENOM; HOG000285953; -.
DR   InParanoid; P27577; -.
DR   KO; K02678; -.
DR   OrthoDB; 526256at2759; -.
DR   PhylomeDB; P27577; -.
DR   TreeFam; TF316214; -.
DR   Reactome; R-MMU-2559585; Oncogene Induced Senescence.
DR   ChiTaRS; Ets1; mouse.
DR   EvolutionaryTrace; P27577; -.
DR   PRO; PR:P27577; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   Bgee; ENSMUSG00000032035; Expressed in 353 organ(s), highest expression level in thymus.
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 factor complex; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
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 proximal promoter 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: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:0061614; P:pri-miRNA transcription by RNA polymerase II; ISO:MGI.
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   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; Complete proteome;
KW   Cytoplasm; DNA-binding; Immunity; Isopeptide bond; Nucleus;
KW   Phosphoprotein; Proto-oncogene; Reference proteome; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN         1    440       Protein C-ets-1.
FT                                /FTId=PRO_0000204070.
FT   DOMAIN       51    136       PNT. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00762}.
FT   DNA_BIND    335    415       ETS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00237}.
FT   REGION      130    243       Activation domain; required for
FT                                transcription activation. {ECO:0000250}.
FT   MOD_RES       8      8       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P14921}.
FT   MOD_RES      15     15       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P14921}.
FT   MOD_RES      38     38       Phosphothreonine; by MAPK.
FT                                {ECO:0000269|PubMed:9770451}.
FT   MOD_RES     223    223       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P14921}.
FT   MOD_RES     251    251       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     254    254       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     265    265       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P14921}.
FT   MOD_RES     267    267       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P14921}.
FT   MOD_RES     270    270       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P14921}.
FT   MOD_RES     282    282       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     285    285       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     305    305       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P14921}.
FT   CROSSLNK      8      8       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:P14921}.
FT   CROSSLNK     15     15       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO);
FT                                alternate.
FT   CROSSLNK     15     15       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:P14921}.
FT   CROSSLNK    138    138       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:P14921}.
FT   CROSSLNK    227    227       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT                                {ECO:0000269|PubMed:16862185}.
FT   CONFLICT     28     28       D -> E (in Ref. 1; AAA63299 and 3;
FT                                CAA39310). {ECO:0000305}.
FT   CONFLICT     37     37       L -> S (in Ref. 3; CAA39310).
FT                                {ECO:0000305}.
FT   CONFLICT     51     52       AT -> SY (in Ref. 3; CAA39310).
FT                                {ECO:0000305}.
FT   CONFLICT     55     55       G -> P (in Ref. 1; AAA63299).
FT                                {ECO:0000305}.
FT   CONFLICT     63     63       L -> R (in Ref. 3; CAA39310).
FT                                {ECO:0000305}.
FT   CONFLICT     74     74       E -> D (in Ref. 3; CAA39310).
FT                                {ECO:0000305}.
FT   CONFLICT     96     96       Q -> H (in Ref. 3; CAA39310).
FT                                {ECO:0000305}.
FT   CONFLICT    105    105       L -> V (in Ref. 3; CAA39310).
FT                                {ECO:0000305}.
FT   CONFLICT    157    157       D -> V (in Ref. 3; CAA39310).
FT                                {ECO:0000305}.
FT   CONFLICT    211    211       Q -> R (in Ref. 3; CAA39310).
FT                                {ECO:0000305}.
FT   CONFLICT    217    217       D -> E (in Ref. 3; CAA39310).
FT                                {ECO:0000305}.
FT   CONFLICT    225    225       A -> R (in Ref. 3; CAA39310).
FT                                {ECO:0000305}.
FT   CONFLICT    234    234       D -> N (in Ref. 3; CAA39310).
FT                                {ECO:0000305}.
FT   CONFLICT    360    360       G -> C (in Ref. 3; CAA39310).
FT                                {ECO:0000305}.
FT   CONFLICT    383    383       K -> S (in Ref. 3; CAA39310).
FT                                {ECO:0000305}.
FT   CONFLICT    392    392       G -> A (in Ref. 3; CAA39310).
FT                                {ECO:0000305}.
FT   CONFLICT    408    409       KR -> NA (in Ref. 3; CAA39310).
FT                                {ECO:0000305}.
FT   CONFLICT    413    413       R -> A (in Ref. 3; CAA39310).
FT                                {ECO:0000305}.
FT   TURN         39     42       {ECO:0000244|PDB:2JV3}.
FT   HELIX        43     52       {ECO:0000244|PDB:2JV3}.
FT   HELIX        54     62       {ECO:0000244|PDB:2JV3}.
FT   STRAND       67     69       {ECO:0000244|PDB:2JV3}.
FT   HELIX        74     88       {ECO:0000244|PDB:2JV3}.
FT   TURN         95     98       {ECO:0000244|PDB:2JV3}.
FT   HELIX       102    107       {ECO:0000244|PDB:2JV3}.
FT   HELIX       109    116       {ECO:0000244|PDB:2JV3}.
FT   HELIX       119    134       {ECO:0000244|PDB:2JV3}.
FT   HELIX       304    312       {ECO:0000244|PDB:1MD0}.
FT   TURN        313    315       {ECO:0000244|PDB:1MD0}.
FT   STRAND      318    321       {ECO:0000244|PDB:1R36}.
FT   HELIX       323    330       {ECO:0000244|PDB:1MD0}.
FT   HELIX       337    345       {ECO:0000244|PDB:1MD0}.
FT   HELIX       348    350       {ECO:0000244|PDB:1MD0}.
FT   TURN        351    353       {ECO:0000244|PDB:1MD0}.
FT   STRAND      354    356       {ECO:0000244|PDB:1K78}.
FT   STRAND      362    364       {ECO:0000244|PDB:1MD0}.
FT   HELIX       368    379       {ECO:0000244|PDB:1MD0}.
FT   HELIX       386    395       {ECO:0000244|PDB:1MD0}.
FT   TURN        396    400       {ECO:0000244|PDB:1MD0}.
FT   STRAND      401    404       {ECO:0000244|PDB:1MD0}.
FT   STRAND      408    414       {ECO:0000244|PDB:1MD0}.
FT   HELIX       418    422       {ECO:0000244|PDB:1MD0}.
FT   HELIX       426    432       {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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