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Database: UniProt
Entry: P01132
LinkDB: P01132
Original site: P01132 
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   07-APR-2021, entry version 219.
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;
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;
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   BMRB; P01132; -.
DR   SMR; P01132; -.
DR   BioGRID; 199398; 3.
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; 1408 antibodies.
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   eggNOG; KOG1215; Eukaryota.
DR   GeneTree; ENSGT00940000158366; -.
DR   HOGENOM; CLU_007857_0_0_1; -.
DR   InParanoid; P01132; -.
DR   OMA; CSHGCVL; -.
DR   OrthoDB; 1174178at2759; -.
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; 0 hits in 52 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 162 other tissues.
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:0000187; P:activation of MAPK activity; IDA:MGI.
DR   GO; GO:0000186; P:activation of MAPKK 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: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: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: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; ISO: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   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:0007744|PDB:1EPH"
FT   STRAND          991..993
FT                   /evidence="ECO:0007744|PDB:1A3P"
FT   STRAND          995..998
FT                   /evidence="ECO:0007744|PDB:1A3P"
FT   TURN            1000..1002
FT                   /evidence="ECO:0007744|PDB:1A3P"
FT   STRAND          1003..1008
FT                   /evidence="ECO:0007744|PDB:1A3P"
FT   TURN            1015..1017
FT                   /evidence="ECO:0007744|PDB:1A3P"
FT   STRAND          1023..1026
FT                   /evidence="ECO:0007744|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
//
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