ID EGF_MOUSE Reviewed; 1217 AA. AC P01132; E9QNX6; Q569W5; Q6P9J2; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 02-SEP-2026, entry version 243. DE RecName: Full=Pro-epidermal growth factor; DE Short=EGF; DE Contains: DE RecName: Full=Epidermal growth factor; DE Flags: Precursor; GN Name=Egf; 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]. RX PubMed=6602382; DOI=10.1126/science.6602382; RA Scott J., Urdea M., Quiroga M., Sanchez-Pescador R., Fong N.M., Selby M., RA Rutter W.J., Bell G.I.; RT "Structure of a mouse submaxillary messenger RNA encoding epidermal growth RT factor and seven related proteins."; RL Science 221:236-240(1983). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=6304537; DOI=10.1038/303722a0; RA Gray A., Dull T.J., Ullrich A.; RT "Nucleotide sequence of epidermal growth factor cDNA predicts a 128,000- RT molecular weight protein precursor."; RL Nature 303:722-725(1983). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Kidney, and Salivary 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 PROTEIN SEQUENCE OF 977-1029. RX PubMed=4636327; DOI=10.1016/s0021-9258(19)44569-9; RA Savage C.R. Jr., Inagami T., Cohen S.; RT "The primary structure of epidermal growth factor."; RL J. Biol. Chem. 247:7612-7621(1972). RN [6] RP DISULFIDE BONDS. RX PubMed=4750422; DOI=10.1016/s0021-9258(19)43242-0; RA Savage C.R. Jr., Hash J.H., Cohen S.; RT "Epidermal growth factor. Location of disulfide bonds."; RL J. Biol. Chem. 248:7669-7672(1973). RN [7] RP INTERACTION WITH RHBDF1 AND RHBDF2. RX PubMed=21439629; DOI=10.1016/j.cell.2011.02.047; RA Zettl M., Adrain C., Strisovsky K., Lastun V., Freeman M.; RT "Rhomboid family pseudoproteases use the ER quality control machinery to RT regulate intercellular signaling."; RL Cell 145:79-91(2011). RN [8] RP STRUCTURE BY NMR OF 977-1029. RX PubMed=1731873; DOI=10.1021/bi00116a033; RA Montelione G.T., Wuethrich K., Burgess A.W., Nice E.C., Wagner G., RA Gibson K.D., Scheraga H.A.; RT "Solution structure of murine epidermal growth factor determined by NMR RT spectroscopy and refined by energy minimization with restraints."; RL Biochemistry 31:236-249(1992). RN [9] RP STRUCTURE BY NMR OF 977-1029. RX PubMed=1445923; DOI=10.1021/bi00162a036; RA Kohda D., Inagaki F.; RT "Three-dimensional nuclear magnetic resonance structures of mouse epidermal RT growth factor in acidic and physiological pH solutions."; RL Biochemistry 31:11928-11939(1992). RN [10] RP STRUCTURE BY NMR OF 980-1024. RX PubMed=10082370; DOI=10.1002/pro.5560070808; RA Barnham K.J., Torres A.M., Alewood D., Alewood P.F., Domagala T., RA Nice E.C., Norton R.S.; RT "Role of the 6-20 disulfide bridge in the structure and activity of RT epidermal growth factor."; RL Protein Sci. 7:1738-1749(1998). CC -!- FUNCTION: EGF stimulates the growth of various epidermal and epithelial CC tissues in vivo and in vitro and of some fibroblasts in cell culture. CC Magnesiotropic hormone that stimulates magnesium reabsorption in the CC renal distal convoluted tubule via engagement of EGFR and activation of CC the magnesium channel TRPM6 (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts with EGFR and promotes EGFR dimerization. Interacts CC with RHBDF1; may retain EGF in the endoplasmic reticulum and regulates CC its degradation through the endoplasmic reticulum-associated CC degradation (ERAD). Interacts with RHBDF2. CC {ECO:0000269|PubMed:21439629}. CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. CC -!- SEQUENCE CAUTION: CC Sequence=CAA24115.1; Type=Frameshift; Evidence={ECO:0000305}; 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; J00380; AAA37539.1; -; mRNA. DR EMBL; V00741; CAA24115.1; ALT_FRAME; mRNA. DR EMBL; V00741; CAA24116.1; -; mRNA. DR EMBL; AC098732; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC060741; AAH60741.1; -; mRNA. DR EMBL; BC092277; AAH92277.1; -; mRNA. DR CCDS; CCDS17833.1; -. DR RefSeq; NP_034243.2; NM_010113.4. DR PDB; 1A3P; NMR; -; A=980-1024. DR PDB; 1EGF; NMR; -; A=977-1029. DR PDB; 1EPG; NMR; -; A=977-1029. DR PDB; 1EPH; NMR; -; A=977-1029. DR PDB; 1EPI; NMR; -; A=977-1029. DR PDB; 1EPJ; NMR; -; A=977-1029. DR PDB; 1GK5; NMR; -; A=977-1018. DR PDB; 3EGF; NMR; -; A=977-1029. DR AlphaFoldDB; P01132; -. DR BMRB; P01132; -. DR MDposit; P01132; -. DR SMR; P01132; -. DR BioGRID; 199398; 5. DR DIP; DIP-5762N; -. DR FunCoup; P01132; 1146. DR IntAct; P01132; 5. DR MINT; P01132; -. DR STRING; 10090.ENSMUSP00000029653; -. DR GlyCosmos; P01132; 4 sites, No reported glycans. DR GlyGen; P01132; 6 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site). DR PhosphoSitePlus; P01132; -. DR PaxDb; 10090-ENSMUSP00000029653; -. DR PeptideAtlas; P01132; -. DR ProteomicsDB; 277802; -. DR Antibodypedia; 4510; 1417 antibodies from 45 providers. DR DNASU; 13645; -. DR Ensembl; ENSMUST00000029653.7; ENSMUSP00000029653.3; ENSMUSG00000028017.8. DR GeneID; 13645; -. DR KEGG; mmu:13645; -. DR UCSC; uc008rig.2; mouse. DR AGR; MGI:95290; -. DR CTD; 1950; -. DR MGI; MGI:95290; Egf. DR VEuPathDB; HostDB:ENSMUSG00000028017; -. DR eggNOG; KOG1215; Eukaryota. DR GeneTree; ENSGT00940000158366; -. DR HOGENOM; CLU_007857_0_0_1; -. DR InParanoid; P01132; -. DR OMA; YKEERIY; -. DR OrthoDB; 4062651at2759; -. DR PhylomeDB; P01132; -. DR Reactome; R-MMU-114608; Platelet degranulation. DR Reactome; R-MMU-1227986; Signaling by ERBB2. DR Reactome; R-MMU-1236394; Signaling by ERBB4. DR Reactome; R-MMU-1250196; SHC1 events in ERBB2 signaling. DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling. DR Reactome; R-MMU-177929; Signaling by EGFR. DR Reactome; R-MMU-179812; GRB2 events in EGFR signaling. DR Reactome; R-MMU-180292; GAB1 signalosome. DR Reactome; R-MMU-180336; SHC1 events in EGFR signaling. DR Reactome; R-MMU-182971; EGFR downregulation. DR Reactome; R-MMU-1963642; PI3K events in ERBB2 signaling. DR Reactome; R-MMU-212718; EGFR interacts with phospholipase C-gamma. DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade. DR Reactome; R-MMU-6785631; ERBB2 Regulates Cell Motility. DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling. DR Reactome; R-MMU-8847993; ERBB2 Activates PTK6 Signaling. DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis. DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis. DR Reactome; R-MMU-8863795; Downregulation of ERBB2 signaling. DR Reactome; R-MMU-9009391; Extra-nuclear estrogen signaling. DR Reactome; R-MMU-9013507; NOTCH3 Activation and Transmission of Signal to the Nucleus. DR BioGRID-ORCS; 13645; 1 hit in 79 CRISPR screens. DR EvolutionaryTrace; P01132; -. DR PRO; PR:P01132; -. DR Proteomes; UP000000589; Chromosome 3. DR RNAct; P01132; protein. DR Bgee; ENSMUSG00000028017; Expressed in submandibular gland and 136 other cell types or tissues. DR ExpressionAtlas; P01132; baseline and differential. DR GO; GO:0070062; C:extracellular exosome; ISO:GO_Central. DR GO; GO:0005576; C:extracellular region; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0005154; F:epidermal growth factor receptor binding; IDA:MGI. DR GO; GO:0008083; F:growth factor activity; ISO:MGI. DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:GO_Central. DR GO; GO:0048018; F:receptor ligand activity; IDA:MGI. DR GO; GO:0030297; F:transmembrane receptor protein tyrosine kinase activator activity; ISO:GO_Central. DR GO; GO:0001525; P:angiogenesis; ISO:GO_Central. DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IDA:MGI. DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IDA:MGI. DR GO; GO:0038134; P:ERBB2-EGFR signaling pathway; IDA:MGI. DR GO; GO:0070371; P:ERK1 and ERK2 cascade; ISO:GO_Central. DR GO; GO:0060749; P:mammary gland alveolus development; IGI:MGI. DR GO; GO:0090370; P:negative regulation of cholesterol efflux; IDA:BHF-UCL. DR GO; GO:0051048; P:negative regulation of secretion; ISO:GO_Central. DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI. DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:GO_Central. DR GO; GO:0030335; P:positive regulation of cell migration; ISO:GO_Central. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:MGI. DR GO; GO:0021940; P:positive regulation of cerebellar granule cell precursor proliferation; IDA:MGI. DR GO; GO:0043388; P:positive regulation of DNA binding; IDA:UniProtKB. DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; ISO:GO_Central. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:GO_Central. DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:GO_Central. DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:GO_Central. DR GO; GO:1905278; P:positive regulation of epithelial tube formation; ISO:GO_Central. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:GO_Central. DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:GO_Central. DR GO; GO:0010628; P:positive regulation of gene expression; ISO:GO_Central. DR GO; GO:1900127; P:positive regulation of hyaluronan biosynthetic process; ISO:GO_Central. DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:MGI. DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; ISO:GO_Central. DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; ISO:GO_Central. DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:MGI. DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISO:GO_Central. DR GO; GO:0042327; P:positive regulation of phosphorylation; ISO:GO_Central. DR GO; GO:1902966; P:positive regulation of protein localization to early endosome; ISO:GO_Central. DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IDA:MGI. DR GO; GO:0002092; P:positive regulation of receptor internalization; ISO:GO_Central. DR GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; IDA:BHF-UCL. DR GO; GO:0090279; P:regulation of calcium ion import; ISO:GO_Central. DR GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IDA:MGI. DR GO; GO:2000008; P:regulation of protein localization to cell surface; ISO:GO_Central. DR GO; GO:0051223; P:regulation of protein transport; ISO:MGI. DR GO; GO:0046425; P:regulation of receptor signaling pathway via JAK-STAT; IDA:UniProtKB. DR CDD; cd00054; EGF_CA; 3. DR FunFam; 2.10.25.10:FF:000038; Fibrillin 2; 1. DR FunFam; 2.10.25.10:FF:000010; Pro-epidermal growth factor; 1. DR FunFam; 2.10.25.10:FF:000219; Pro-epidermal growth factor; 1. DR FunFam; 2.10.25.10:FF:000254; Pro-epidermal growth factor; 1. DR FunFam; 2.10.25.10:FF:000362; Pro-epidermal growth factor; 1. DR FunFam; 2.10.25.10:FF:000896; Pro-epidermal growth factor; 1. DR FunFam; 2.120.10.30:FF:000028; Pro-epidermal growth factor; 1. DR FunFam; 2.120.10.30:FF:000036; Pro-epidermal growth factor; 1. DR Gene3D; 2.10.25.10; Laminin; 7. DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 2. DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like. DR InterPro; IPR000742; EGF. DR InterPro; IPR001881; EGF-like_Ca-bd_dom. DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site. DR InterPro; IPR018097; EGF_Ca-bd_CS. DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf. DR InterPro; IPR000033; LDLR_classB_rpt. DR InterPro; IPR049883; NOTCH1_EGF-like. DR InterPro; IPR016317; Pro-epidermal_GF. DR PANTHER; PTHR46513:SF5; PRO-EPIDERMAL GROWTH FACTOR; 1. DR PANTHER; PTHR46513; VITELLOGENIN RECEPTOR-LIKE PROTEIN-RELATED-RELATED; 1. DR Pfam; PF00008; EGF; 1. DR Pfam; PF07645; EGF_CA; 2. DR Pfam; PF14670; FXa_inhibition; 2. DR Pfam; PF00058; Ldl_recept_b; 3. DR PIRSF; PIRSF001778; Pro-epidermal_growth_factor; 1. DR PRINTS; PR00009; EGFTGF. DR SMART; SM00181; EGF; 9. DR SMART; SM00179; EGF_CA; 8. DR SMART; SM00135; LY; 9. DR SUPFAM; SSF57196; EGF/Laminin; 4. DR SUPFAM; SSF57184; Growth factor receptor domain; 1. DR SUPFAM; SSF63825; YWTD domain; 2. DR PROSITE; PS00010; ASX_HYDROXYL; 3. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 6. DR PROSITE; PS50026; EGF_3; 5. DR PROSITE; PS01187; EGF_CA; 3. DR PROSITE; PS51120; LDLRB; 8. DR PDBsum; 1A3P; -. DR PDBsum; 1EGF; -. DR PDBsum; 1EPG; -. DR PDBsum; 1EPH; -. DR PDBsum; 1EPI; -. DR PDBsum; 1EPJ; -. DR PDBsum; 1GK5; -. DR PDBsum; 3EGF; -. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Disulfide bond; EGF-like domain; KW Glycoprotein; Growth factor; Membrane; Reference proteome; Repeat; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1..28 FT /evidence="ECO:0000255" FT CHAIN 29..1217 FT /note="Pro-epidermal growth factor" FT /id="PRO_0000007542" FT CHAIN 977..1029 FT /note="Epidermal growth factor" FT /evidence="ECO:0000269|PubMed:4636327" FT /id="PRO_0000007543" FT TOPO_DOM 29..1038 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1039..1058 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1059..1217 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REPEAT 93..134 FT /note="LDL-receptor class B 1" FT REPEAT 135..176 FT /note="LDL-receptor class B 2" FT REPEAT 177..219 FT /note="LDL-receptor class B 3" FT DOMAIN 327..361 FT /note="EGF-like 1; incomplete" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 362..402 FT /note="EGF-like 2; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 403..443 FT /note="EGF-like 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 441..483 FT /note="EGF-like 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT REPEAT 489..529 FT /note="LDL-receptor class B 4" FT REPEAT 530..572 FT /note="LDL-receptor class B 5" FT REPEAT 573..615 FT /note="LDL-receptor class B 6" FT REPEAT 616..659 FT /note="LDL-receptor class B 7" FT REPEAT 660..702 FT /note="LDL-receptor class B 8" FT DOMAIN 747..787 FT /note="EGF-like 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 838..876 FT /note="EGF-like 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 877..918 FT /note="EGF-like 7; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 919..959 FT /note="EGF-like 8; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 978..1019 FT /note="EGF-like 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT REGION 1024..1029 FT /note="Not required for full biological activity" FT REGION 1070..1096 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1164..1217 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1080..1096 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 111 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 410 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 810 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 944 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 366..377 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 373..386 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 388..401 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 407..418 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 414..427 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 429..442 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 445..457 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 453..467 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 469..482 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 751..762 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 758..771 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 773..786 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 842..853 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 847..862 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 864..875 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 881..895 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 888..904 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 906..917 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 923..936 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 930..945 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 947..958 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 982..996 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076, FT ECO:0000269|PubMed:4750422" FT DISULFID 990..1007 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076, FT ECO:0000269|PubMed:4750422" FT DISULFID 1009..1018 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076, FT ECO:0000269|PubMed:4750422" FT CONFLICT 790 FT /note="D -> Y (in Ref. 2; CAA24115)" FT /evidence="ECO:0000305" FT CONFLICT 931 FT /note="G -> A (in Ref. 1; AAA37539, 2; CAA24115 and 4; FT AAH60741/AAH92277)" FT /evidence="ECO:0000305" FT CONFLICT 956 FT /note="L -> R (in Ref. 1; AAA37539, 2; CAA24115 and 4; FT AAH60741/AAH92277)" FT /evidence="ECO:0000305" FT CONFLICT 1048 FT /note="A -> S (in Ref. 2; CAA24115)" FT /evidence="ECO:0000305" FT CONFLICT 1054 FT /note="V -> L (in Ref. 1; AAA37539, 2; CAA24115 and 4; FT AAH60741/AAH92277)" FT /evidence="ECO:0000305" FT CONFLICT 1090 FT /note="N -> D (in Ref. 1; AAA37539, 2; CAA24115 and 4; FT AAH60741/AAH92277)" FT /evidence="ECO:0000305" FT CONFLICT 1217 FT /note="Q -> K (in Ref. 1; AAA37539)" FT /evidence="ECO:0000305" FT STRAND 987..990 FT /evidence="ECO:0007829|PDB:1EPH" FT STRAND 991..993 FT /evidence="ECO:0007829|PDB:1A3P" FT STRAND 995..998 FT /evidence="ECO:0007829|PDB:1A3P" FT TURN 1000..1002 FT /evidence="ECO:0007829|PDB:1A3P" FT STRAND 1003..1008 FT /evidence="ECO:0007829|PDB:1A3P" FT TURN 1015..1018 FT /evidence="ECO:0007829|PDB:1A3P" FT STRAND 1023..1026 FT /evidence="ECO:0007829|PDB:1EPH" SQ SEQUENCE 1217 AA; 133072 MW; 28F35C928280D31B CRC64; MPWGRRPTWL LLAFLLVFLK ISILSVTAWQ TGNCQPGPLE RSERSGTCAG PAPFLVFSQG KSISRIDPDG TNHQQLVVDA GISADMDIHY KKERLYWVDV ERQVLLRVFL NGTGLEKVCN VERKVSGLAI DWIDDEVLWV DQQNGVITVT DMTGKNSRVL LSSLKHPSNI AVDPIERLMF WSSEVTGSLH RAHLKGVDVK TLLETGGISV LTLDVLDKRL FWVQDSGEGS HAYIHSCDYE GGSVRLIRHQ ARHSLSSMAF FGDRIFYSVL KSKAIWIANK HTGKDTVRIN LHPSFVTPGK LMVVHPRAQP RTEDAAKDPD PELLKQRGRP CRFGLCERDP KSHSSACAEG YTLSRDRKYC EDVNECATQN HGCTLGCENT PGSYHCTCPT GFVLLPDGKQ CHELVSCPGN VSKCSHGCVL TSDGPRCICP AGSVLGRDGK TCTGCSSPDN GGCSQICLPL RPGSWECDCF PGYDLQSDRK SCAASGPQPL LLFANSQDIR HMHFDGTDYK VLLSRQMGMV FALDYDPVES KIYFAQTALK WIERANMDGS QRERLITEGV DTLEGLALDW IGRRIYWTDS GKSVVGGSDL SGKHHRIIIQ ERISRPRGIA VHPRARRLFW TDVGMSPRIE SASLQGSDRV LIASSNLLEP SGITIDYLTD TLYWCDTKRS VIEMANLDGS KRRRLIQNDV GHPFSLAVFE DHLWVSDWAI PSVIRVNKRT GQNRVRLQGS MLKPSSLVVV HPLAKPGADP CLYRNGGCEH ICQESLGTAR CLCREGFVKA WDGKMCLPQD YPILSGENAD LSKEVTSLSN STQAEVPDDD GTESSTLVAE IMVSGMNYED DCGPGGCGSH ARCVSDGETA ECQCLKGFAR DGNLCSDIDE CVLARSDCPS TSSRCINTEG GYVCRCSEGY EGDGISCFDI DECQRGAHNC GENAACTNTE GGYNCTCAGR PSSPGLSCPD STAPSLLGED GHHLDRNSYP GCPSSYDGYC LNGGVCMHIE SLDSYTCNCV IGYSGDRCQT RDLRWWELRH AGYGQKHDIM VVAVCMVALV LLLVLGMWGT YYYRTRKQLS NPPKNPCDEP SGSVSSSGPN SSSGAAVASC PQPWFVVLEK HQDPKNGSLP ADGTNGAVVD AGLSPSLQLG SVHLTSWRQK PHIDGMGTGQ SCWIPPSSDR GPQEIEGNSH LPSYRPVGPE KLHSLQSANG SCHERAPDLP RQTEPVQ //