ID A0A2K5WBG5_MACFA Unreviewed; 1203 AA.
AC A0A2K5WBG5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Pro-epidermal growth factor {ECO:0000256|ARBA:ARBA00017466, ECO:0000256|PIRNR:PIRNR001778};
GN Name=EGF {ECO:0000313|Ensembl:ENSMFAP00000034454.2};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000034454.2, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000034454.2, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000034454.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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. {ECO:0000256|PIRNR:PIRNR001778}.
CC -!- SUBUNIT: Interacts with EGFR and promotes EGFR dimerization.
CC {ECO:0000256|PIRNR:PIRNR001778}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR AlphaFoldDB; A0A2K5WBG5; -.
DR Ensembl; ENSMFAT00000008684.2; ENSMFAP00000034454.2; ENSMFAG00000003730.2.
DR VEuPathDB; HostDB:ENSMFAG00000003730; -.
DR GeneTree; ENSGT00940000158366; -.
DR Proteomes; UP000233100; Chromosome 5.
DR Bgee; ENSMFAG00000003730; Expressed in adult mammalian kidney and 3 other cell types or tissues.
DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; IEA:Ensembl.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:Ensembl.
DR GO; GO:0030297; F:transmembrane receptor protein tyrosine kinase activator activity; IEA:Ensembl.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IEA:Ensembl.
DR GO; GO:0021930; P:cerebellar granule cell precursor proliferation; IEA:Ensembl.
DR GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0038134; P:ERBB2-EGFR signaling pathway; IEA:Ensembl.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0060749; P:mammary gland alveolus development; IEA:Ensembl.
DR GO; GO:0090370; P:negative regulation of cholesterol efflux; IEA:Ensembl.
DR GO; GO:0051048; P:negative regulation of secretion; IEA:Ensembl.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0021940; P:positive regulation of cerebellar granule cell precursor proliferation; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IEA:Ensembl.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:1905278; P:positive regulation of epithelial tube formation; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:1900127; P:positive regulation of hyaluronan biosynthetic process; IEA:Ensembl.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; IEA:Ensembl.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IEA:Ensembl.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR GO; GO:1902966; P:positive regulation of protein localization to early endosome; IEA:Ensembl.
DR GO; GO:0002092; P:positive regulation of receptor internalization; IEA:Ensembl.
DR GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:0090279; P:regulation of calcium ion import; IEA:Ensembl.
DR GO; GO:2000008; P:regulation of protein localization to cell surface; IEA:Ensembl.
DR GO; GO:0046425; P:regulation of receptor signaling pathway via JAK-STAT; IEA:Ensembl.
DR CDD; cd00054; EGF_CA; 2.
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; 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; IPR024731; EGF_dom.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR000033; LDLR_classB_rpt.
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; PF12947; EGF_3; 1.
DR Pfam; PF07645; EGF_CA; 3.
DR Pfam; PF14670; FXa_inhibition; 1.
DR Pfam; PF00058; Ldl_recept_b; 4.
DR PIRSF; PIRSF001778; Pro-epidermal_growth_factor; 1.
DR PRINTS; PR00009; EGFTGF.
DR SMART; SM00181; EGF; 9.
DR SMART; SM00179; EGF_CA; 4.
DR SMART; SM00135; LY; 9.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR SUPFAM; SSF63825; YWTD domain; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 3.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS51120; LDLRB; 4.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW Growth factor {ECO:0000256|ARBA:ARBA00023030,
KW ECO:0000256|PIRNR:PIRNR001778}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000233100};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1203
FT /note="Pro-epidermal growth factor"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030052057"
FT TRANSMEM 1033..1057
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 524..566
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 567..609
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 610..653
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 654..696
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 831..869
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 870..911
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 912..952
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 972..1013
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 1065..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1108..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1088
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 984..1001
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1003..1012
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1203 AA; 133166 MW; 64B0E9D8930A073C CRC64;
MLLPLIILLP VVLKFSCVSL SAPQHWSCPE GTPAGHGNST RVGPAPFLIF SHGNSIFRID
TEGTNYEPLV VDAGVSVIMD FHYKEKTIYW VDLERQLLQR VFLNGSRQER VCNIEKNVSG
MAINWINEEV IWSNQQEGII TVTDMKGNNS HVLLSALKYP ANIAVDPVER FIFWSSEVAG
SLYRADLDGV EVKSLLETSE KITAVSLDVL DKRLFWIQYS REGSNSLICS CDYDGGSVHV
SKHPTQHNLF AMSLFGDHVF YSTWKTRTIW IANKHTGKDM VRINLHPSFV PPGELKVVHP
LAQPKAEDDA REREQKLHKS RKGNCSSTVC GQDAQSHLCT CAEGYALSRD RKYCEDVNEC
AFWNHGCTLG CKNTPGSYYC TCPVGFVLLP DGKRCHQLVS CPSNVSECSH DCVLTSEGPL
CFCPEGSVLE RDGKTCSGCS SPDNGGCSQL CIPLSPVSWE CDCFPGYDLQ LDKKSCVASG
PQPFLLFANS QDIRHMHFDG TDYGTLLSQQ MGMVYALDHD PVENKIYFAH TALKWIERAN
MDGSQRERLI EEGVDVPEGL AVDWIGRRFY WTDRGKSLIG RSDLNGKHPK IIIKENISQP
QGIAVHPMAK RLFWTDTGIN PRIESSSLQG LGRLVIASSD LIWPNGITID FLTDKLYWCD
AKQSVIEMAN LDGSKRRTLT QNDVGHPFAI AVFEDYVWFS DWAMPSVIRV NKKTGKDRVR
LQGSMLKPSS LVVVHPLAKP GADPCLYQNG GCEHICKERL GTAWCLCREG FMKASDGKTC
LALDGHQLLA GGEVDLKNQV TPLDTLSKTR VSEDNITESQ HMLVAEITVS DQYDCAPVGC
STYARCVSEG KDVTCQCLKG FAGDGILCSD IDECEMGVPV CPPASSKCIN TEGGYVCQCS
EGYRGDGIHC LDIDECQLGV HSCGENANCT NTEGGYTCTC AGRLSEPGLI CPDSTPPPHL
REDGHHYSVR NSDSGCPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW
ELRHAGHGQQ QKVTVVAVCV VVLVVLLLLS LWGAHYYRTQ KLLTKNPKNP SEESSRDARS
HRPADREDGM SSCPQPWFVV TKEHQDLRNG SQPVAGEDGQ AADVGSVQPT SWRQKPQLCG
VGPEQGCWIP VSSDKGSCPQ PALISCCYWN FKNLCLQVSA PFDNTSDNNP TLYPWTKTHR
NMM
//