epidermal growth factor (EGF)/urogastrone

Function: - facilitates cell growth, proliferation, & differentiation via its receptor EGFR - EGF is released by proteolysis of a membrane-bound precursor - EGF stimulates the growth of various epidermal & epithelial tissues in vivo & in vitro & of some fibroblasts in cell culture - stimulates Mg⁺² reabsorption in the distal renal tubule via engagement of EGFR & activation of the Mg⁺² channel TRPM6 - interacts with EGFR & promotes EGFR dimerization - interacts with RHBDF2 (putative) - interacts with RHBDF1 - may retain EGF in the endoplasmic reticulum & regulates its degradation through the ER-associated degradation (ERAD) Structure: - O-glycosylated with core 1-like & core 2-like glycans - uncertain if Ser-954 or Thr-955 is O-glycosylated - pro-EGF contains 9 EGF-like domains - pro-EGF contains 9 LDL-receptor class B repeats - EGF is a 6045-Da protein with 53 amino acid residues - EGF has 3 intramolecular disulfide bonds Compartment: - membrane; single-pass type 1 membrane protein - cleaved from membrane & released into extracellular space Alternative splicing: named isoforms=2 Expression: - expressed in kidney, salivary gland, cerebrum & prostate - found in platelets, macrophages, urine, saliva, milk, & plasma Pathology: - defects in EGF are the cause of hypomagnesemia type 4

Related

epidermal growth factor receptor; receptor tyrosine-protein kinase ErbB-1 (EGFR, ERBB1, HER1) epidermal growth factor [EGF] gene heparin-binding EGF-like growth factor; heparin-binding protein; HB-EGF; HBEGF; diphtheria toxin receptor; DT-R (HBEGF, DTR, DTS, HEGFL) teratocarcinoma-derived growth factor 1; cripto-1 growth factor; CRGF; EGF-like cripto protein CR1 (TDGF1, CRIPTO)

General

cytokine gastrointestinal hormone

Properties

SIZE: MW = 6 kD MW = 134 kD entity length = 53 aa entity length = 1207 aa COMPARTMENT: extracellular compartment SECRETED-BY: macrophage MOTIF: signal sequence {1-22} N-glycosylation site {N38} LDL-receptor class B {86-127} MOTIF: N-glycosylation site {N104} N-glycosylation site {N117} LDL-receptor class B {128-169} MOTIF: N-glycosylation site {N148} LDL-receptor class B {170-211} LDL-receptor class B {212-258} EGF domain {314-355} MOTIF: cysteine residue {C318} MODIFICATION: cysteine residue {C330} N-glycosylation site {N324} cysteine residue {C325} MODIFICATION: cysteine residue {C339} cysteine residue {C330} MODIFICATION: cysteine residue {C318} cysteine residue {C339} MODIFICATION: cysteine residue {C325} cysteine residue {C341} MODIFICATION: cysteine residue {C354} cysteine residue {C354} MODIFICATION: cysteine residue {C341} EGF domain {356-396} MOTIF: cysteine residue {C360} MODIFICATION: cysteine residue {C371} cysteine residue {C367} MODIFICATION: cysteine residue {C380} cysteine residue {C371} MODIFICATION: cysteine residue {C360} cysteine residue {C380} MODIFICATION: cysteine residue {C367} cysteine residue {C382} MODIFICATION: cysteine residue {C395} cysteine residue {C395} MODIFICATION: cysteine residue {C382} EGF domain {397-437} MOTIF: cysteine residue {C401} MODIFICATION: cysteine residue {C412} N-glycosylation site {N404} cysteine residue {C408} MODIFICATION: cysteine residue {C421} cysteine residue {C412} MODIFICATION: cysteine residue {C401} cysteine residue {C421} MODIFICATION: cysteine residue {C408} cysteine residue {C423} MODIFICATION: cysteine residue {C436} EGF domain {435-477} MOTIF: cysteine residue {C436} MODIFICATION: cysteine residue {C423} cysteine residue {C439} MODIFICATION: cysteine residue {C451} cysteine residue {C447} MODIFICATION: cysteine residue {C461} cysteine residue {C451} MODIFICATION: cysteine residue {C439} cysteine residue {C461} MODIFICATION: cysteine residue {C447} cysteine residue {C463} MODIFICATION: cysteine residue {C476} cysteine residue {C476} MODIFICATION: cysteine residue {C463} LDL-receptor class B {483-523} LDL-receptor class B {524-566} LDL-receptor class B {567-609} MOTIF: N-glycosylation site {N596} LDL-receptor class B {610-653} LDL-receptor class B {654-696} EGF domain {741-781} MOTIF: cysteine residue {C745} MODIFICATION: cysteine residue {C756} cysteine residue {C752} MODIFICATION: cysteine residue {C765} cysteine residue {C756} MODIFICATION: cysteine residue {C745} cysteine residue {C765} MODIFICATION: cysteine residue {C752} cysteine residue {C767} MODIFICATION: cysteine residue {C780} cysteine residue {C780} MODIFICATION: cysteine residue {C767} O-glycosylated at one site {801-807} N-glycosylation site {N815} EGF domain {831-869} MOTIF: cysteine residue {C835} MODIFICATION: cysteine residue {C846} cysteine residue {C840} MODIFICATION: cysteine residue {C855} cysteine residue {C846} MODIFICATION: cysteine residue {C835} cysteine residue {C855} MODIFICATION: cysteine residue {C840} cysteine residue {C857} MODIFICATION: cysteine residue {C868} cysteine residue {C868} MODIFICATION: cysteine residue {C857} EGF domain {870-911} MOTIF: cysteine residue {C874} MODIFICATION: cysteine residue {C888} cysteine residue {C881} MODIFICATION: cysteine residue {C897} cysteine residue {C888} MODIFICATION: cysteine residue {C874} cysteine residue {C897} MODIFICATION: cysteine residue {C881} cysteine residue {C899} MODIFICATION: cysteine residue {C910} cysteine residue {C910} MODIFICATION: cysteine residue {C899} EGF domain {912-952} MOTIF: cysteine residue {C916} MODIFICATION: cysteine residue {C929} cysteine residue {C923} MODIFICATION: cysteine residue {C938} N-glycosylation site {N926} cysteine residue {C929} MODIFICATION: cysteine residue {C916} cysteine residue {C938} MODIFICATION: cysteine residue {C923} cysteine residue {C940} MODIFICATION: cysteine residue {C951} cysteine residue {C951} MODIFICATION: cysteine residue {C940} Ser glycosylation site {S954} Thr glycosylation site {T955} EGF domain {972-1013} MOTIF: cysteine residue {C976} MODIFICATION: cysteine residue {C990} cysteine residue {C984} MODIFICATION: cysteine residue {C1001} cysteine residue {C990} MODIFICATION: cysteine residue {C976} cysteine residue {C1001} MODIFICATION: cysteine residue {C984} cysteine residue {C1003} MODIFICATION: cysteine residue {C1012} cysteine residue {C1012} MODIFICATION: cysteine residue {C1003} transmembrane domain {1033-1053}

Database Correlations

OMIM correlations MORBIDMAP 131530 UniProt P01133 PFAM correlations Entrez Gene 1950 Kegg hsa:1950