EGF_MOUSE
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 03-AUG-2022, entry version 224.
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};
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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 PDBsum; 1A3P; -.
DR PDBsum; 1EGF; -.
DR PDBsum; 1EPG; -.
DR PDBsum; 1EPH; -.
DR PDBsum; 1EPI; -.
DR PDBsum; 1EPJ; -.
DR PDBsum; 1GK5; -.
DR PDBsum; 3EGF; -.
DR AlphaFoldDB; P01132; -.
DR BMRB; P01132; -.
DR SMR; P01132; -.
DR BioGRID; 199398; 4.
DR DIP; DIP-5762N; -.
DR IntAct; P01132; 5.
DR MINT; P01132; -.
DR STRING; 10090.ENSMUSP00000029653; -.
DR GlyGen; P01132; 4 sites.
DR iPTMnet; P01132; -.
DR PhosphoSitePlus; P01132; -.
DR MaxQB; P01132; -.
DR PaxDb; P01132; -.
DR PeptideAtlas; P01132; -.
DR PRIDE; P01132; -.
DR ProteomicsDB; 277802; -.
DR Antibodypedia; 4510; 1422 antibodies from 44 providers.
DR DNASU; 13645; -.
DR Ensembl; ENSMUST00000029653; ENSMUSP00000029653; ENSMUSG00000028017.
DR GeneID; 13645; -.
DR KEGG; mmu:13645; -.
DR UCSC; uc008rig.2; mouse.
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; CHELVSC; -.
DR OrthoDB; 1174178at2759; -.
DR PhylomeDB; P01132; -.
DR TreeFam; TF315253; -.
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 74 CRISPR screens.
DR ChiTaRS; Egf; mouse.
DR EvolutionaryTrace; P01132; -.
DR PRO; PR:P01132; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P01132; protein.
DR Bgee; ENSMUSG00000028017; Expressed in submandibular gland and 132 other tissues.
DR ExpressionAtlas; P01132; baseline and differential.
DR Genevisible; P01132; MM.
DR GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:MGI.
DR GO; GO:0048018; F:receptor ligand activity; IDA:MGI.
DR GO; GO:0030297; F:transmembrane receptor protein tyrosine kinase activator activity; IDA:MGI.
DR GO; GO:0001525; P:angiogenesis; ISO:MGI.
DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IDA:MGI.
DR GO; GO:0008283; P:cell population proliferation; IGI:MGI.
DR GO; GO:0021930; P:cerebellar granule cell precursor proliferation; IDA:MGI.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IDA:MGI.
DR GO; GO:0038029; P:epidermal growth factor receptor signaling pathway via MAPK cascade; ISS:UniProtKB.
DR GO; GO:0050673; P:epithelial cell proliferation; IGI:MGI.
DR GO; GO:0038134; P:ERBB2-EGFR signaling pathway; IDA:MGI.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; ISO:MGI.
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:MGI.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; 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; 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:MGI.
DR GO; GO:0045740; P:positive regulation of DNA replication; ISS:UniProtKB.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:MGI.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:MGI.
DR GO; GO:0045741; P:positive regulation of epidermal growth factor-activated receptor activity; ISO:MGI.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IGI:MGI.
DR GO; GO:1905278; P:positive regulation of epithelial tube formation; ISO:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:1900127; P:positive regulation of hyaluronan biosynthetic process; ISO:MGI.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:MGI.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; ISO:MGI.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; ISO:MGI.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:MGI.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:MGI.
DR GO; GO:0042327; P:positive regulation of phosphorylation; ISO:MGI.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
DR GO; GO:1902966; P:positive regulation of protein localization to early endosome; ISO:MGI.
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:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
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:MGI.
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:MGI.
DR GO; GO:0050708; P:regulation of protein secretion; ISO:MGI.
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 Gene3D; 2.120.10.30; -; 2.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_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; IPR016317; Pro-epidermal_GF.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF07645; EGF_CA; 3.
DR Pfam; PF00058; Ldl_recept_b; 3.
DR PIRSF; PIRSF001778; Pro-epidermal_growth_factor; 1.
DR SMART; SM00181; EGF; 9.
DR SMART; SM00179; EGF_CA; 8.
DR SMART; SM00135; LY; 9.
DR SUPFAM; SSF57184; SSF57184; 1.
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.
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 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..1017
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
