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 27-MAR-2024, entry version 214. 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: BMAL1, PER2 and CC NR1D1 in the liver via the activation of PER1 (clock repressor) CC transcription. Regulates the rhythmic expression of core-clock gene CC BMAL1 in the suprachiasmatic nucleus (SCN) (By similarity). CC {ECO:0000250|UniProtKB:P08046, ECO:0000269|PubMed:20121949, CC ECO:0000269|PubMed:25258363, 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="https://atlasgeneticsoncology.org/gene/496/EGR1"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 54. DR CORUM; P18146; -. DR IntAct; P18146; 30. DR MINT; P18146; -. DR STRING; 9606.ENSP00000239938; -. DR ChEMBL; CHEMBL3616355; -. DR GlyConnect; 2852; 1 O-GlcNAc glycan (1 site). DR GlyCosmos; P18146; 5 sites, 2 glycans. DR GlyGen; P18146; 6 sites, 2 O-linked glycans (6 sites). DR iPTMnet; P18146; -. DR PhosphoSitePlus; P18146; -. DR BioMuta; EGR1; -. DR DMDM; 119242; -. DR EPD; P18146; -. DR MassIVE; P18146; -. DR PaxDb; 9606-ENSP00000239938; -. DR PeptideAtlas; P18146; -. DR ProteomicsDB; 53552; -. DR Antibodypedia; 14988; 616 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 AGR; HGNC:3238; -. 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; 2912670at2759; -. 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; 24 hits in 1177 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 210 other cell types or tissues. DR ExpressionAtlas; P18146; baseline and differential. 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:0045893; P:positive regulation of DNA-templated transcription; IDA: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:1901875; P:positive regulation of post-translational protein modification; IMP:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0043523; P:regulation of neuron apoptotic process; ISS:ARUK-UCL. 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: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 Gene3D; 3.30.160.60; Classic Zinc Finger; 3. DR InterPro; IPR021839; EGR1_C. DR InterPro; IPR021849; EGR_N. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR23235:SF42; EARLY GROWTH RESPONSE PROTEIN 1; 1. DR PANTHER; PTHR23235; KRUEPPEL-LIKE TRANSCRIPTION FACTOR; 1. 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; beta-beta-alpha zinc fingers; 2. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3. DR Genevisible; P18146; HS. 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 //