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Protein

Pro-epidermal growth factor

Gene

Egf

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. Magnesiotropic hormone that stimulates magnesium reabsorption in the renal distal convoluted tubule via engagement of EGFR and activation of the magnesium channel TRPM6 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Growth factor

Enzyme and pathway databases

ReactomeiR-MMU-114608. Platelet degranulation.
R-MMU-1227986. Signaling by ERBB2.
R-MMU-1236394. Signaling by ERBB4.
R-MMU-1250196. SHC1 events in ERBB2 signaling.
R-MMU-1257604. PIP3 activates AKT signaling.
R-MMU-177929. Signaling by EGFR.
R-MMU-179812. GRB2 events in EGFR signaling.
R-MMU-180292. GAB1 signalosome.
R-MMU-180336. SHC1 events in EGFR signaling.
R-MMU-182971. EGFR downregulation.
R-MMU-1963642. PI3K events in ERBB2 signaling.
R-MMU-212718. EGFR interacts with phospholipase C-gamma.
R-MMU-5673001. RAF/MAP kinase cascade.
R-MMU-6785631. ERBB2 Regulates Cell Motility.
R-MMU-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-MMU-8847993. ERBB2 Activates PTK6 Signaling.
R-MMU-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-MMU-8856828. Clathrin-mediated endocytosis.
R-MMU-8863795. Downregulation of ERBB2 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Pro-epidermal growth factor
Short name:
EGF
Cleaved into the following chain:
Gene namesi
Name:Egf
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:95290. Egf.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini29 – 1038ExtracellularSequence analysisAdd BLAST1010
Transmembranei1039 – 1058HelicalSequence analysisAdd BLAST20
Topological domaini1059 – 1217CytoplasmicSequence analysisAdd BLAST159

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • extracellular region Source: Reactome
  • extracellular space Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • lysosomal membrane Source: MGI
  • plasma membrane Source: UniProtKB
  • receptor complex Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Sequence analysisAdd BLAST28
ChainiPRO_000000754229 – 1217Pro-epidermal growth factorAdd BLAST1189
ChainiPRO_0000007543977 – 1029Epidermal growth factor1 PublicationAdd BLAST53

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi111N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi366 ↔ 377PROSITE-ProRule annotation
Disulfide bondi373 ↔ 386PROSITE-ProRule annotation
Disulfide bondi388 ↔ 401PROSITE-ProRule annotation
Disulfide bondi407 ↔ 418PROSITE-ProRule annotation
Glycosylationi410N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi414 ↔ 427PROSITE-ProRule annotation
Disulfide bondi429 ↔ 442PROSITE-ProRule annotation
Disulfide bondi445 ↔ 457PROSITE-ProRule annotation
Disulfide bondi453 ↔ 467PROSITE-ProRule annotation
Disulfide bondi469 ↔ 482PROSITE-ProRule annotation
Disulfide bondi751 ↔ 762PROSITE-ProRule annotation
Disulfide bondi758 ↔ 771PROSITE-ProRule annotation
Disulfide bondi773 ↔ 786PROSITE-ProRule annotation
Glycosylationi810N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi842 ↔ 853PROSITE-ProRule annotation
Disulfide bondi847 ↔ 862PROSITE-ProRule annotation
Disulfide bondi864 ↔ 875PROSITE-ProRule annotation
Disulfide bondi881 ↔ 895PROSITE-ProRule annotation
Disulfide bondi888 ↔ 904PROSITE-ProRule annotation
Disulfide bondi906 ↔ 917PROSITE-ProRule annotation
Disulfide bondi923 ↔ 936PROSITE-ProRule annotation
Disulfide bondi930 ↔ 945PROSITE-ProRule annotation
Glycosylationi944N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi947 ↔ 958PROSITE-ProRule annotation
Disulfide bondi982 ↔ 996PROSITE-ProRule annotation1 Publication
Disulfide bondi990 ↔ 1007PROSITE-ProRule annotation1 Publication
Disulfide bondi1009 ↔ 1018PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP01132.
PaxDbiP01132.
PeptideAtlasiP01132.
PRIDEiP01132.

PTM databases

PhosphoSitePlusiP01132.

Miscellaneous databases

PMAP-CutDBP01132.

Expressioni

Gene expression databases

BgeeiENSMUSG00000028017.
CleanExiMM_EGF.
ExpressionAtlasiP01132. baseline and differential.
GenevisibleiP01132. MM.

Interactioni

Subunit structurei

Interacts with EGFR and promotes EGFR dimerization. Interacts with RHBDF1; may retain EGF in the endoplasmic reticulum and regulates its degradation through the endoplasmic reticulum-associated degradation (ERAD). Interacts with RHBDF2.1 Publication

GO - Molecular functioni

Protein-protein interaction databases

DIPiDIP-5762N.
IntActiP01132. 5 interactors.
STRINGi10090.ENSMUSP00000029653.

Structurei

Secondary structure

11217
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi987 – 990Combined sources4
Beta strandi991 – 993Combined sources3
Beta strandi995 – 998Combined sources4
Turni1000 – 1002Combined sources3
Beta strandi1003 – 1008Combined sources6
Turni1015 – 1017Combined sources3
Beta strandi1023 – 1026Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A3PNMR-A980-1024[»]
1EGFNMR-A977-1029[»]
1EPGNMR-A977-1029[»]
1EPHNMR-A977-1029[»]
1EPINMR-A977-1029[»]
1EPJNMR-A977-1029[»]
1GK5NMR-A977-1018[»]
3EGFNMR-A977-1029[»]
ProteinModelPortaliP01132.
SMRiP01132.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01132.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati93 – 134LDL-receptor class B 1Add BLAST42
Repeati135 – 176LDL-receptor class B 2Add BLAST42
Repeati177 – 219LDL-receptor class B 3Add BLAST43
Domaini327 – 361EGF-like 1; incompletePROSITE-ProRule annotationAdd BLAST35
Domaini362 – 402EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini403 – 443EGF-like 3PROSITE-ProRule annotationAdd BLAST41
Domaini441 – 483EGF-like 4PROSITE-ProRule annotationAdd BLAST43
Repeati489 – 529LDL-receptor class B 4Add BLAST41
Repeati530 – 572LDL-receptor class B 5Add BLAST43
Repeati573 – 615LDL-receptor class B 6Add BLAST43
Repeati616 – 659LDL-receptor class B 7Add BLAST44
Repeati660 – 702LDL-receptor class B 8Add BLAST43
Domaini747 – 787EGF-like 5PROSITE-ProRule annotationAdd BLAST41
Domaini838 – 876EGF-like 6PROSITE-ProRule annotationAdd BLAST39
Domaini877 – 918EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini919 – 959EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini978 – 1019EGF-like 9PROSITE-ProRule annotationAdd BLAST42

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1024 – 1029Not required for full biological activity6

Sequence similaritiesi

Contains 9 EGF-like domains.PROSITE-ProRule annotation
Contains 8 LDL-receptor class B repeats.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IPSY. Eukaryota.
ENOG410ZVIM. LUCA.
GeneTreeiENSGT00760000118968.
HOGENOMiHOG000112345.
HOVERGENiHBG003858.
InParanoidiP01132.
KOiK04357.
OMAiKIYFAHT.
OrthoDBiEOG091G014V.
TreeFamiTF315253.

Family and domain databases

Gene3Di2.120.10.30. 2 hits.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR000033. LDLR_classB_rpt.
IPR016317. Pro-epidermal_GF.
[Graphical view]
PfamiPF00008. EGF. 1 hit.
PF07645. EGF_CA. 3 hits.
PF00058. Ldl_recept_b. 3 hits.
[Graphical view]
PIRSFiPIRSF001778. Pro-epidermal_growth_factor. 1 hit.
SMARTiSM00181. EGF. 9 hits.
SM00179. EGF_CA. 8 hits.
SM00135. LY. 9 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 2 hits.
PROSITEiPS00010. ASX_HYDROXYL. 3 hits.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 6 hits.
PS50026. EGF_3. 5 hits.
PS01187. EGF_CA. 3 hits.
PS51120. LDLRB. 8 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P01132-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPWGRRPTWL LLAFLLVFLK ISILSVTAWQ TGNCQPGPLE RSERSGTCAG
60 70 80 90 100
PAPFLVFSQG KSISRIDPDG TNHQQLVVDA GISADMDIHY KKERLYWVDV
110 120 130 140 150
ERQVLLRVFL NGTGLEKVCN VERKVSGLAI DWIDDEVLWV DQQNGVITVT
160 170 180 190 200
DMTGKNSRVL LSSLKHPSNI AVDPIERLMF WSSEVTGSLH RAHLKGVDVK
210 220 230 240 250
TLLETGGISV LTLDVLDKRL FWVQDSGEGS HAYIHSCDYE GGSVRLIRHQ
260 270 280 290 300
ARHSLSSMAF FGDRIFYSVL KSKAIWIANK HTGKDTVRIN LHPSFVTPGK
310 320 330 340 350
LMVVHPRAQP RTEDAAKDPD PELLKQRGRP CRFGLCERDP KSHSSACAEG
360 370 380 390 400
YTLSRDRKYC EDVNECATQN HGCTLGCENT PGSYHCTCPT GFVLLPDGKQ
410 420 430 440 450
CHELVSCPGN VSKCSHGCVL TSDGPRCICP AGSVLGRDGK TCTGCSSPDN
460 470 480 490 500
GGCSQICLPL RPGSWECDCF PGYDLQSDRK SCAASGPQPL LLFANSQDIR
510 520 530 540 550
HMHFDGTDYK VLLSRQMGMV FALDYDPVES KIYFAQTALK WIERANMDGS
560 570 580 590 600
QRERLITEGV DTLEGLALDW IGRRIYWTDS GKSVVGGSDL SGKHHRIIIQ
610 620 630 640 650
ERISRPRGIA VHPRARRLFW TDVGMSPRIE SASLQGSDRV LIASSNLLEP
660 670 680 690 700
SGITIDYLTD TLYWCDTKRS VIEMANLDGS KRRRLIQNDV GHPFSLAVFE
710 720 730 740 750
DHLWVSDWAI PSVIRVNKRT GQNRVRLQGS MLKPSSLVVV HPLAKPGADP
760 770 780 790 800
CLYRNGGCEH ICQESLGTAR CLCREGFVKA WDGKMCLPQD YPILSGENAD
810 820 830 840 850
LSKEVTSLSN STQAEVPDDD GTESSTLVAE IMVSGMNYED DCGPGGCGSH
860 870 880 890 900
ARCVSDGETA ECQCLKGFAR DGNLCSDIDE CVLARSDCPS TSSRCINTEG
910 920 930 940 950
GYVCRCSEGY EGDGISCFDI DECQRGAHNC GENAACTNTE GGYNCTCAGR
960 970 980 990 1000
PSSPGLSCPD STAPSLLGED GHHLDRNSYP GCPSSYDGYC LNGGVCMHIE
1010 1020 1030 1040 1050
SLDSYTCNCV IGYSGDRCQT RDLRWWELRH AGYGQKHDIM VVAVCMVALV
1060 1070 1080 1090 1100
LLLVLGMWGT YYYRTRKQLS NPPKNPCDEP SGSVSSSGPN SSSGAAVASC
1110 1120 1130 1140 1150
PQPWFVVLEK HQDPKNGSLP ADGTNGAVVD AGLSPSLQLG SVHLTSWRQK
1160 1170 1180 1190 1200
PHIDGMGTGQ SCWIPPSSDR GPQEIEGNSH LPSYRPVGPE KLHSLQSANG
1210
SCHERAPDLP RQTEPVQ
Length:1,217
Mass (Da):133,072
Last modified:July 27, 2011 - v2
Checksum:i28F35C928280D31B
GO

Sequence cautioni

The sequence CAA24115 differs from that shown. Reason: Frameshift at positions 1134 and 1168.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti790D → Y in CAA24115 (PubMed:6304537).Curated1
Sequence conflicti931G → A in AAA37539 (PubMed:6602382).Curated1
Sequence conflicti931G → A in CAA24115 (PubMed:6304537).Curated1
Sequence conflicti931G → A in AAH60741 (PubMed:15489334).Curated1
Sequence conflicti931G → A in AAH92277 (PubMed:15489334).Curated1
Sequence conflicti956L → R in AAA37539 (PubMed:6602382).Curated1
Sequence conflicti956L → R in CAA24115 (PubMed:6304537).Curated1
Sequence conflicti956L → R in AAH60741 (PubMed:15489334).Curated1
Sequence conflicti956L → R in AAH92277 (PubMed:15489334).Curated1
Sequence conflicti1048A → S in CAA24115 (PubMed:6304537).Curated1
Sequence conflicti1054V → L in AAA37539 (PubMed:6602382).Curated1
Sequence conflicti1054V → L in CAA24115 (PubMed:6304537).Curated1
Sequence conflicti1054V → L in AAH60741 (PubMed:15489334).Curated1
Sequence conflicti1054V → L in AAH92277 (PubMed:15489334).Curated1
Sequence conflicti1090N → D in AAA37539 (PubMed:6602382).Curated1
Sequence conflicti1090N → D in CAA24115 (PubMed:6304537).Curated1
Sequence conflicti1090N → D in AAH60741 (PubMed:15489334).Curated1
Sequence conflicti1090N → D in AAH92277 (PubMed:15489334).Curated1
Sequence conflicti1217Q → K in AAA37539 (PubMed:6602382).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00380 mRNA. Translation: AAA37539.1.
V00741 mRNA. Translation: CAA24115.1. Frameshift.
V00741 mRNA. Translation: CAA24116.1.
AC098732 Genomic DNA. No translation available.
BC060741 mRNA. Translation: AAH60741.1.
BC092277 mRNA. Translation: AAH92277.1.
CCDSiCCDS17833.1.
RefSeqiNP_034243.2. NM_010113.4.
UniGeneiMm.252481.

Genome annotation databases

EnsembliENSMUST00000029653; ENSMUSP00000029653; ENSMUSG00000028017.
GeneIDi13645.
KEGGimmu:13645.
UCSCiuc008rig.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00380 mRNA. Translation: AAA37539.1.
V00741 mRNA. Translation: CAA24115.1. Frameshift.
V00741 mRNA. Translation: CAA24116.1.
AC098732 Genomic DNA. No translation available.
BC060741 mRNA. Translation: AAH60741.1.
BC092277 mRNA. Translation: AAH92277.1.
CCDSiCCDS17833.1.
RefSeqiNP_034243.2. NM_010113.4.
UniGeneiMm.252481.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A3PNMR-A980-1024[»]
1EGFNMR-A977-1029[»]
1EPGNMR-A977-1029[»]
1EPHNMR-A977-1029[»]
1EPINMR-A977-1029[»]
1EPJNMR-A977-1029[»]
1GK5NMR-A977-1018[»]
3EGFNMR-A977-1029[»]
ProteinModelPortaliP01132.
SMRiP01132.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-5762N.
IntActiP01132. 5 interactors.
STRINGi10090.ENSMUSP00000029653.

PTM databases

PhosphoSitePlusiP01132.

Proteomic databases

MaxQBiP01132.
PaxDbiP01132.
PeptideAtlasiP01132.
PRIDEiP01132.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029653; ENSMUSP00000029653; ENSMUSG00000028017.
GeneIDi13645.
KEGGimmu:13645.
UCSCiuc008rig.2. mouse.

Organism-specific databases

CTDi1950.
MGIiMGI:95290. Egf.

Phylogenomic databases

eggNOGiENOG410IPSY. Eukaryota.
ENOG410ZVIM. LUCA.
GeneTreeiENSGT00760000118968.
HOGENOMiHOG000112345.
HOVERGENiHBG003858.
InParanoidiP01132.
KOiK04357.
OMAiKIYFAHT.
OrthoDBiEOG091G014V.
TreeFamiTF315253.

Enzyme and pathway databases

ReactomeiR-MMU-114608. Platelet degranulation.
R-MMU-1227986. Signaling by ERBB2.
R-MMU-1236394. Signaling by ERBB4.
R-MMU-1250196. SHC1 events in ERBB2 signaling.
R-MMU-1257604. PIP3 activates AKT signaling.
R-MMU-177929. Signaling by EGFR.
R-MMU-179812. GRB2 events in EGFR signaling.
R-MMU-180292. GAB1 signalosome.
R-MMU-180336. SHC1 events in EGFR signaling.
R-MMU-182971. EGFR downregulation.
R-MMU-1963642. PI3K events in ERBB2 signaling.
R-MMU-212718. EGFR interacts with phospholipase C-gamma.
R-MMU-5673001. RAF/MAP kinase cascade.
R-MMU-6785631. ERBB2 Regulates Cell Motility.
R-MMU-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-MMU-8847993. ERBB2 Activates PTK6 Signaling.
R-MMU-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-MMU-8856828. Clathrin-mediated endocytosis.
R-MMU-8863795. Downregulation of ERBB2 signaling.

Miscellaneous databases

ChiTaRSiEgf. mouse.
EvolutionaryTraceiP01132.
PMAP-CutDBP01132.
PROiP01132.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000028017.
CleanExiMM_EGF.
ExpressionAtlasiP01132. baseline and differential.
GenevisibleiP01132. MM.

Family and domain databases

Gene3Di2.120.10.30. 2 hits.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR000033. LDLR_classB_rpt.
IPR016317. Pro-epidermal_GF.
[Graphical view]
PfamiPF00008. EGF. 1 hit.
PF07645. EGF_CA. 3 hits.
PF00058. Ldl_recept_b. 3 hits.
[Graphical view]
PIRSFiPIRSF001778. Pro-epidermal_growth_factor. 1 hit.
SMARTiSM00181. EGF. 9 hits.
SM00179. EGF_CA. 8 hits.
SM00135. LY. 9 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 2 hits.
PROSITEiPS00010. ASX_HYDROXYL. 3 hits.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 6 hits.
PS50026. EGF_3. 5 hits.
PS01187. EGF_CA. 3 hits.
PS51120. LDLRB. 8 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEGF_MOUSE
AccessioniPrimary (citable) accession number: P01132
Secondary accession number(s): E9QNX6, Q569W5, Q6P9J2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 27, 2011
Last modified: November 30, 2016
This is version 189 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.