EGR1_HUMAN
ID EGR1_HUMAN Reviewed; 543 AA.
AC P18146;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Early growth response protein 1 {ECO:0000303|PubMed:2377485};
DE Short=EGR-1 {ECO:0000303|PubMed:2377485};
DE AltName: Full=AT225;
DE AltName: Full=Nerve growth factor-induced protein A;
DE Short=NGFI-A;
DE AltName: Full=Transcription factor ETR103;
DE AltName: Full=Transcription factor Zif268;
DE AltName: Full=Zinc finger protein 225 {ECO:0000303|PubMed:2110381};
DE AltName: Full=Zinc finger protein Krox-24;
GN Name=EGR1; Synonyms=KROX24, ZNF225 {ECO:0000303|PubMed:2110381};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Foreskin;
RX PubMed=2377485; DOI=10.1093/nar/18.14.4283;
RA Suggs S.V., Katzowitz J.L., Tsai-Morris C.-H., Sukhatme V.P.;
RT "cDNA sequence of the human cellular early growth response gene Egr-1.";
RL Nucleic Acids Res. 18:4283-4283(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1569051; DOI=10.1093/oxfordjournals.jbchem.a123748;
RA Shimizu N., Ohta M., Fujiwara C., Sagara J., Mochizuki N., Oda T.,
RA Utiyama H.;
RT "A gene coding for a zinc finger protein is induced during 12-O-
RT tetradecanoylphorbol-13-acetate-stimulated HL-60 cell differentiation.";
RL J. Biochem. 111:272-277(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2110381; DOI=10.1126/science.2110381;
RA Wright J.J., Gunter K.C., Mitsuya H., Irving S.G., Kelly K., Siebenlist U.;
RT "Expression of a zinc finger gene in HTLV-I- and HTLV-II-transformed
RT cells.";
RL Science 248:588-591(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=PNS;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [6]
RP INTERACTION WITH SNAI1 AND SP1, AND FUNCTION.
RX PubMed=20121949; DOI=10.1111/j.1742-4658.2009.07553.x;
RA Hu C.T., Chang T.Y., Cheng C.C., Liu C.S., Wu J.R., Li M.C., Wu W.S.;
RT "Snail associates with EGR-1 and SP-1 to upregulate transcriptional
RT activation of p15INK4b.";
RL FEBS J. 277:1202-1218(2010).
RN [7]
RP SUBCELLULAR LOCATION, AND INDUCTION BY GROWTH FACTORS.
RX PubMed=20363028; DOI=10.1016/j.molimm.2010.03.003;
RA Cullen E.M., Brazil J.C., O'Connor C.M.;
RT "Mature human neutrophils constitutively express the transcription factor
RT EGR-1.";
RL Mol. Immunol. 47:1701-1709(2010).
RN [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-305, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [9] {ECO:0007744|PDB:4R2A, ECO:0007744|PDB:4R2C, ECO:0007744|PDB:4R2D}
RP X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 335-423 IN COMPLEX WITH ZINC AND
RP TARGET DNA, FUNCTION, DOMAIN, AND SITES OF INTERACTION WITH DNA.
RX PubMed=25258363; DOI=10.1101/gad.250746.114;
RA Hashimoto H., Olanrewaju Y.O., Zheng Y., Wilson G.G., Zhang X., Cheng X.;
RT "Wilms tumor protein recognizes 5-carboxylcytosine within a specific DNA
RT sequence.";
RL Genes Dev. 28:2304-2313(2014).
RN [10] {ECO:0007744|PDB:4X9J}
RP X-RAY CRYSTALLOGRAPHY (1.41 ANGSTROMS) OF 335-423 IN COMPLEX WITH ZINC AND
RP TARGET DNA, FUNCTION, DOMAIN, AND SITES OF INTERACTION WITH DNA.
RX PubMed=25999311; DOI=10.1016/j.febslet.2015.05.022;
RA Zandarashvili L., White M.A., Esadze A., Iwahara J.;
RT "Structural impact of complete CpG methylation within target DNA on
RT specific complex formation of the inducible transcription factor Egr-1.";
RL FEBS Lett. 589:1748-1753(2015).
CC -!- FUNCTION: Transcriptional regulator (PubMed:20121949). Recognizes and
CC binds to the DNA sequence 5'-GCG(T/G)GGGCG-3'(EGR-site) in the promoter
CC region of target genes (By similarity). Binds double-stranded target
CC DNA, irrespective of the cytosine methylation status (PubMed:25258363,
CC PubMed:25999311). Regulates the transcription of numerous target genes,
CC and thereby plays an important role in regulating the response to
CC growth factors, DNA damage, and ischemia. Plays a role in the
CC regulation of cell survival, proliferation and cell death. Activates
CC expression of p53/TP53 and TGFB1, and thereby helps prevent tumor
CC formation. Required for normal progress through mitosis and normal
CC proliferation of hepatocytes after partial hepatectomy. Mediates
CC responses to ischemia and hypoxia; regulates the expression of proteins
CC such as IL1B and CXCL2 that are involved in inflammatory processes and
CC development of tissue damage after ischemia. Regulates biosynthesis of
CC luteinizing hormone (LHB) in the pituitary (By similarity). Regulates
CC the amplitude of the expression rhythms of clock genes: ARNTL/BMAL1,
CC PER2 and NR1D1 in the liver via the activation of PER1 (clock
CC repressor) transcription. Regulates the rhythmic expression of core-
CC clock gene ARNTL/BMAL1 in the suprachiasmatic nucleus (SCN) (By
CC similarity). {ECO:0000250|UniProtKB:P08046,
CC ECO:0000269|PubMed:20121949, ECO:0000269|PubMed:25258363,
CC ECO:0000269|PubMed:25999311}.
CC -!- SUBUNIT: Interacts with SNAI1 and SP1 upon 12-O-tetradecanoylphorbol-
CC 13-acetate (TPA) induction. {ECO:0000269|PubMed:20121949}.
CC -!- INTERACTION:
CC P18146; Q8N726: CDKN2A; NbExp=4; IntAct=EBI-2834611, EBI-625922;
CC P18146; P35222: CTNNB1; NbExp=7; IntAct=EBI-2834611, EBI-491549;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20363028}. Cytoplasm
CC {ECO:0000269|PubMed:20363028}.
CC -!- TISSUE SPECIFICITY: Detected in neutrophils (at protein level).
CC {ECO:0000269|PubMed:20363028}.
CC -!- INDUCTION: By growth factors. {ECO:0000269|PubMed:20363028}.
CC -!- DOMAIN: Binds to DNA motifs with the sequence 5'-GCG(T/G)GGGCG-3' via
CC its C2H2-type zinc fingers (PubMed:25258363, PubMed:25999311). The
CC first, most N-terminal zinc finger binds to the 3'-GCG motif, the
CC middle zinc finger interacts with the central TGG motif, and the C-
CC terminal zinc finger binds to the 5'-GCG motif. Binds double-stranded
CC target DNA, irrespective of the cytosine methylation status. Has
CC reduced affinity for target DNA where the cytosines have been oxidized
CC to 5-hydroxymethylcytosine. Does not bind target DNA where the
CC cytosines have been oxidized to 5-formylcytosine or 5-carboxylcytosine
CC (PubMed:25258363). {ECO:0000269|PubMed:25258363,
CC ECO:0000269|PubMed:25999311}.
CC -!- SIMILARITY: Belongs to the EGR C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/EGR1ID496ch5q31.html";
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DR EMBL; X52541; CAA36777.1; -; mRNA.
DR EMBL; M62829; AAA35815.1; -; mRNA.
DR EMBL; M80583; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC073983; AAH73983.1; -; mRNA.
DR CCDS; CCDS4206.1; -.
DR PIR; A41211; A41211.
DR RefSeq; NP_001955.1; NM_001964.2.
DR PDB; 4R2A; X-ray; 1.59 A; A=335-423.
DR PDB; 4R2C; X-ray; 1.89 A; A=335-423.
DR PDB; 4R2D; X-ray; 2.09 A; A=335-423.
DR PDB; 4X9J; X-ray; 1.41 A; A=335-423.
DR PDB; 5N14; NMR; -; A=395-408.
DR PDBsum; 4R2A; -.
DR PDBsum; 4R2C; -.
DR PDBsum; 4R2D; -.
DR PDBsum; 4X9J; -.
DR PDBsum; 5N14; -.
DR AlphaFoldDB; P18146; -.
DR BMRB; P18146; -.
DR SMR; P18146; -.
DR BioGRID; 108278; 46.
DR CORUM; P18146; -.
DR IntAct; P18146; 30.
DR MINT; P18146; -.
DR STRING; 9606.ENSP00000239938; -.
DR ChEMBL; CHEMBL3616355; -.
DR GlyConnect; 2852; 1 O-Linked glycan (1 site).
DR GlyGen; P18146; 5 sites, 2 O-linked glycans (5 sites).
DR iPTMnet; P18146; -.
DR PhosphoSitePlus; P18146; -.
DR BioMuta; EGR1; -.
DR DMDM; 119242; -.
DR EPD; P18146; -.
DR MassIVE; P18146; -.
DR PaxDb; P18146; -.
DR PeptideAtlas; P18146; -.
DR PRIDE; P18146; -.
DR ProteomicsDB; 53552; -.
DR Antibodypedia; 14988; 561 antibodies from 42 providers.
DR DNASU; 1958; -.
DR Ensembl; ENST00000239938.5; ENSP00000239938.4; ENSG00000120738.8.
DR GeneID; 1958; -.
DR KEGG; hsa:1958; -.
DR MANE-Select; ENST00000239938.5; ENSP00000239938.4; NM_001964.3; NP_001955.1.
DR CTD; 1958; -.
DR DisGeNET; 1958; -.
DR GeneCards; EGR1; -.
DR HGNC; HGNC:3238; EGR1.
DR HPA; ENSG00000120738; Low tissue specificity.
DR MIM; 128990; gene.
DR neXtProt; NX_P18146; -.
DR OpenTargets; ENSG00000120738; -.
DR PharmGKB; PA27673; -.
DR VEuPathDB; HostDB:ENSG00000120738; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000160184; -.
DR HOGENOM; CLU_043235_2_0_1; -.
DR InParanoid; P18146; -.
DR OMA; NFQVPMI; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; P18146; -.
DR TreeFam; TF318980; -.
DR PathwayCommons; P18146; -.
DR Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-HSA-9031628; NGF-stimulated transcription.
DR Reactome; R-HSA-909733; Interferon alpha/beta signaling.
DR SignaLink; P18146; -.
DR SIGNOR; P18146; -.
DR BioGRID-ORCS; 1958; 22 hits in 1096 CRISPR screens.
DR ChiTaRS; EGR1; human.
DR GeneWiki; EGR1; -.
DR GenomeRNAi; 1958; -.
DR Pharos; P18146; Tbio.
DR PRO; PR:P18146; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P18146; protein.
DR Bgee; ENSG00000120738; Expressed in mucosa of stomach and 208 other tissues.
DR ExpressionAtlas; P18146; baseline and differential.
DR Genevisible; P18146; HS.
DR GO; GO:0000785; C:chromatin; IDA:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:ARUK-UCL.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0010385; F:double-stranded methylated DNA binding; IDA:UniProtKB.
DR GO; GO:0044729; F:hemi-methylated DNA-binding; IDA:UniProtKB.
DR GO; GO:0035035; F:histone acetyltransferase binding; IPI:BHF-UCL.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0030509; P:BMP signaling pathway; IEA:Ensembl.
DR GO; GO:0071480; P:cellular response to gamma radiation; IEA:Ensembl.
DR GO; GO:0071504; P:cellular response to heparin; ISS:UniProtKB.
DR GO; GO:0098759; P:cellular response to interleukin-8; IDA:UniProtKB.
DR GO; GO:0071506; P:cellular response to mycophenolic acid; ISS:UniProtKB.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0060086; P:circadian temperature homeostasis; ISS:UniProtKB.
DR GO; GO:0044849; P:estrous cycle; ISS:UniProtKB.
DR GO; GO:0072110; P:glomerular mesangial cell proliferation; ISS:UniProtKB.
DR GO; GO:0070498; P:interleukin-1-mediated signaling pathway; IMP:BHF-UCL.
DR GO; GO:0045475; P:locomotor rhythm; ISS:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0032722; P:positive regulation of chemokine production; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:0072303; P:positive regulation of glomerular metanephric mesangial cell proliferation; ISS:UniProtKB.
DR GO; GO:0046886; P:positive regulation of hormone biosynthetic process; ISS:UniProtKB.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISS:UniProtKB.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; IDA:ARUK-UCL.
DR GO; GO:1901216; P:positive regulation of neuron death; ISS:ARUK-UCL.
DR GO; GO:1902949; P:positive regulation of tau-protein kinase activity; ISS:ARUK-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:2000182; P:regulation of progesterone biosynthetic process; ISS:UniProtKB.
DR GO; GO:0033233; P:regulation of protein sumoylation; IDA:BHF-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; IEA:Ensembl.
DR GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
DR GO; GO:0032868; P:response to insulin; IEA:Ensembl.
DR GO; GO:0002931; P:response to ischemia; ISS:UniProtKB.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0030217; P:T cell differentiation; IEA:Ensembl.
DR InterPro; IPR021839; EGR1_C.
DR InterPro; IPR021849; EGR_N.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF11914; DUF3432; 2.
DR Pfam; PF11928; DUF3446; 1.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Biological rhythms; Cytoplasm; DNA-binding;
KW Isopeptide bond; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..543
FT /note="Early growth response protein 1"
FT /id="PRO_0000047109"
FT ZN_FING 338..362
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042,
FT ECO:0000269|PubMed:25258363, ECO:0000269|PubMed:25999311,
FT ECO:0007744|PDB:4R2A, ECO:0007744|PDB:4R2C,
FT ECO:0007744|PDB:4R2D, ECO:0007744|PDB:4X9J"
FT ZN_FING 368..390
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042,
FT ECO:0000269|PubMed:25258363, ECO:0000269|PubMed:25999311,
FT ECO:0007744|PDB:4R2A, ECO:0007744|PDB:4R2C,
FT ECO:0007744|PDB:4R2D, ECO:0007744|PDB:4X9J"
FT ZN_FING 396..418
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042,
FT ECO:0000269|PubMed:25258363, ECO:0000269|PubMed:25999311,
FT ECO:0007744|PDB:4R2A, ECO:0007744|PDB:4R2C,
FT ECO:0007744|PDB:4R2D, ECO:0007744|PDB:4X9J"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 336
FT /note="Interaction with DNA"
FT /evidence="ECO:0000269|PubMed:25258363,
FT ECO:0007744|PDB:4R2A"
FT SITE 347
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P08046"
FT SITE 351
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P08046"
FT SITE 357
FT /note="Interaction with DNA"
FT /evidence="ECO:0000269|PubMed:25258363,
FT ECO:0007744|PDB:4R2A"
FT SITE 375
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P08046"
FT SITE 379
FT /note="Interaction with DNA"
FT /evidence="ECO:0000269|PubMed:25258363,
FT ECO:0007744|PDB:4R2A"
FT SITE 403
FT /note="Interaction with DNA"
FT /evidence="ECO:0000269|PubMed:25999311,
FT ECO:0007744|PDB:4X9J"
FT SITE 407
FT /note="Interaction with DNA"
FT /evidence="ECO:0000269|PubMed:25258363,
FT ECO:0007744|PDB:4R2A"
FT SITE 413
FT /note="Interaction with DNA"
FT /evidence="ECO:0000269|PubMed:25258363,
FT ECO:0000269|PubMed:25999311, ECO:0007744|PDB:4R2A,
FT ECO:0007744|PDB:4X9J"
FT CROSSLNK 305
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 28
FT /note="T -> I (in dbSNP:rs13181973)"
FT /id="VAR_052712"
FT VARIANT 144
FT /note="N -> K (in dbSNP:rs28365166)"
FT /id="VAR_029330"
FT VARIANT 145
FT /note="S -> R (in dbSNP:rs28365164)"
FT /id="VAR_029331"
FT VARIANT 219
FT /note="E -> D (in dbSNP:rs28365165)"
FT /id="VAR_029332"
FT STRAND 348..351
FT /evidence="ECO:0007829|PDB:4X9J"
FT HELIX 352..363
FT /evidence="ECO:0007829|PDB:4X9J"
FT TURN 371..373
FT /evidence="ECO:0007829|PDB:4X9J"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:4X9J"
FT HELIX 380..391
FT /evidence="ECO:0007829|PDB:4X9J"
FT TURN 399..401
FT /evidence="ECO:0007829|PDB:4X9J"
FT STRAND 404..407
FT /evidence="ECO:0007829|PDB:4X9J"
FT HELIX 408..415
FT /evidence="ECO:0007829|PDB:4X9J"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:4X9J"
SQ SEQUENCE 543 AA; 57507 MW; 768CE670D9743E4E CRC64;
MAAAKAEMQL MSPLQISDPF GSFPHSPTMD NYPKLEEMML LSNGAPQFLG AAGAPEGSGS
NSSSSSSGGG GGGGGGSNSS SSSSTFNPQA DTGEQPYEHL TAESFPDISL NNEKVLVETS
YPSQTTRLPP ITYTGRFSLE PAPNSGNTLW PEPLFSLVSG LVSMTNPPAS SSSAPSPAAS
SASASQSPPL SCAVPSNDSS PIYSAAPTFP TPNTDIFPEP QSQAFPGSAG TALQYPPPAY
PAAKGGFQVP MIPDYLFPQQ QGDLGLGTPD QKPFQGLESR TQQPSLTPLS TIKAFATQSG
SQDLKALNTS YQSQLIKPSR MRKYPNRPSK TPPHERPYAC PVESCDRRFS RSDELTRHIR
IHTGQKPFQC RICMRNFSRS DHLTTHIRTH TGEKPFACDI CGRKFARSDE RKRHTKIHLR
QKDKKADKSV VASSATSSLS SYPSPVATSY PSPVTTSYPS PATTSYPSPV PTSFSSPGSS
TYPSPVHSGF PSPSVATTYS SVPPAFPAQV SSFPSSAVTN SFSASTGLSD MTATFSPRTI
EIC
