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P01132 (EGF_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 167. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pro-epidermal growth factor

Short name=EGF

Cleaved into the following chain:

  1. Epidermal growth factor
Gene names
Name:Egf
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1217 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.7

Subcellular location

Membrane; Single-pass type I membrane protein.

Sequence similarities

Contains 9 EGF-like domains.

Contains 8 LDL-receptor class B repeats.

Sequence caution

The sequence CAA24115.1 differs from that shown. Reason: Frameshift at positions 1134 and 1168.

Ontologies

Keywords
   Cellular componentMembrane
   DomainEGF-like domain
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionGrowth factor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processERK1 and ERK2 cascade

Inferred from electronic annotation. Source: Ensembl

STAT protein import into nucleus

Inferred from direct assay PubMed 15156153. Source: UniProtKB

activation of MAPKK activity

Inferred from direct assay PubMed 16339969. Source: MGI

angiogenesis

Inferred from electronic annotation. Source: Ensembl

branching morphogenesis of an epithelial tube

Inferred from direct assay PubMed 15831470. Source: MGI

epidermal growth factor receptor signaling pathway

Inferred from direct assay PubMed 15695332PubMed 6315706. Source: MGI

mammary gland alveolus development

Inferred from genetic interaction PubMed 10331984. Source: MGI

negative regulation of cholesterol efflux

Inferred from direct assay PubMed 20037141. Source: BHF-UCL

negative regulation of secretion

Inferred from electronic annotation. Source: Ensembl

peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 14561752. Source: MGI

positive regulation of DNA binding

Inferred from direct assay PubMed 15156153. Source: UniProtKB

positive regulation of MAP kinase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of catenin import into nucleus

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from direct assay PubMed 14712229PubMed 15695332. Source: MGI

positive regulation of cerebellar granule cell precursor proliferation

Inferred from direct assay PubMed 10027293. Source: MGI

positive regulation of epidermal growth factor-activated receptor activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of hyaluronan biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of mitosis

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-threonine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process

Inferred from direct assay PubMed 20208556. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

regulation of calcium ion import

Inferred from electronic annotation. Source: Ensembl

regulation of peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 11940581. Source: MGI

regulation of protein localization to cell surface

Inferred from electronic annotation. Source: Ensembl

regulation of protein transport

Inferred from sequence orthology PubMed 19723622. Source: MGI

   Cellular_componentextracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 7641815PubMed 8240367. Source: MGI

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

lysosomal membrane

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay PubMed 17626015. Source: UniProtKB

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

epidermal growth factor receptor binding

Inferred from direct assay PubMed 6315706. Source: MGI

protein binding

Inferred from physical interaction PubMed 17626015. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Chain29 – 12171189Pro-epidermal growth factor
PRO_0000007542
Chain977 – 102953Epidermal growth factor Ref.5
PRO_0000007543

Regions

Topological domain29 – 10381010Extracellular Potential
Transmembrane1039 – 105820Helical; Potential
Topological domain1059 – 1217159Cytoplasmic Potential
Repeat93 – 13442LDL-receptor class B 1
Repeat135 – 17642LDL-receptor class B 2
Repeat177 – 21943LDL-receptor class B 3
Domain327 – 36135EGF-like 1; incomplete
Domain362 – 40241EGF-like 2; calcium-binding Potential
Domain403 – 44341EGF-like 3
Domain441 – 48343EGF-like 4
Repeat489 – 52941LDL-receptor class B 4
Repeat530 – 57243LDL-receptor class B 5
Repeat573 – 61543LDL-receptor class B 6
Repeat616 – 65944LDL-receptor class B 7
Repeat660 – 70243LDL-receptor class B 8
Domain747 – 78741EGF-like 5
Domain838 – 87639EGF-like 6
Domain877 – 91842EGF-like 7; calcium-binding Potential
Domain919 – 95941EGF-like 8; calcium-binding Potential
Domain978 – 101942EGF-like 9
Region1024 – 10296Not required for full biological activity

Amino acid modifications

Glycosylation1111N-linked (GlcNAc...) Potential
Glycosylation4101N-linked (GlcNAc...) Potential
Glycosylation8101N-linked (GlcNAc...) Potential
Glycosylation9441N-linked (GlcNAc...) Potential
Disulfide bond366 ↔ 377 By similarity
Disulfide bond373 ↔ 386 By similarity
Disulfide bond388 ↔ 401 By similarity
Disulfide bond407 ↔ 418 By similarity
Disulfide bond414 ↔ 427 By similarity
Disulfide bond429 ↔ 442 By similarity
Disulfide bond445 ↔ 457 By similarity
Disulfide bond453 ↔ 467 By similarity
Disulfide bond469 ↔ 482 By similarity
Disulfide bond751 ↔ 762 By similarity
Disulfide bond758 ↔ 771 By similarity
Disulfide bond773 ↔ 786 By similarity
Disulfide bond842 ↔ 853 By similarity
Disulfide bond847 ↔ 862 By similarity
Disulfide bond864 ↔ 875 By similarity
Disulfide bond881 ↔ 895 By similarity
Disulfide bond888 ↔ 904 By similarity
Disulfide bond906 ↔ 917 By similarity
Disulfide bond923 ↔ 936 By similarity
Disulfide bond930 ↔ 945 By similarity
Disulfide bond947 ↔ 958 By similarity
Disulfide bond982 ↔ 996 Ref.6
Disulfide bond990 ↔ 1007 Ref.6
Disulfide bond1009 ↔ 1018 Ref.6

Experimental info

Sequence conflict7901D → Y in CAA24115. Ref.2
Sequence conflict9311G → A in AAA37539. Ref.1
Sequence conflict9311G → A in CAA24115. Ref.2
Sequence conflict9311G → A in AAH60741. Ref.4
Sequence conflict9311G → A in AAH92277. Ref.4
Sequence conflict9561L → R in AAA37539. Ref.1
Sequence conflict9561L → R in CAA24115. Ref.2
Sequence conflict9561L → R in AAH60741. Ref.4
Sequence conflict9561L → R in AAH92277. Ref.4
Sequence conflict10481A → S in CAA24115. Ref.2
Sequence conflict10541V → L in AAA37539. Ref.1
Sequence conflict10541V → L in CAA24115. Ref.2
Sequence conflict10541V → L in AAH60741. Ref.4
Sequence conflict10541V → L in AAH92277. Ref.4
Sequence conflict10901N → D in AAA37539. Ref.1
Sequence conflict10901N → D in CAA24115. Ref.2
Sequence conflict10901N → D in AAH60741. Ref.4
Sequence conflict10901N → D in AAH92277. Ref.4
Sequence conflict12171Q → K in AAA37539. Ref.1

Secondary structure

............. 1217
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P01132 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 28F35C928280D31B

FASTA1,217133,072
        10         20         30         40         50         60 
MPWGRRPTWL LLAFLLVFLK ISILSVTAWQ TGNCQPGPLE RSERSGTCAG PAPFLVFSQG 

        70         80         90        100        110        120 
KSISRIDPDG TNHQQLVVDA GISADMDIHY KKERLYWVDV ERQVLLRVFL NGTGLEKVCN 

       130        140        150        160        170        180 
VERKVSGLAI DWIDDEVLWV DQQNGVITVT DMTGKNSRVL LSSLKHPSNI AVDPIERLMF 

       190        200        210        220        230        240 
WSSEVTGSLH RAHLKGVDVK TLLETGGISV LTLDVLDKRL FWVQDSGEGS HAYIHSCDYE 

       250        260        270        280        290        300 
GGSVRLIRHQ ARHSLSSMAF FGDRIFYSVL KSKAIWIANK HTGKDTVRIN LHPSFVTPGK 

       310        320        330        340        350        360 
LMVVHPRAQP RTEDAAKDPD PELLKQRGRP CRFGLCERDP KSHSSACAEG YTLSRDRKYC 

       370        380        390        400        410        420 
EDVNECATQN HGCTLGCENT PGSYHCTCPT GFVLLPDGKQ CHELVSCPGN VSKCSHGCVL 

       430        440        450        460        470        480 
TSDGPRCICP AGSVLGRDGK TCTGCSSPDN GGCSQICLPL RPGSWECDCF PGYDLQSDRK 

       490        500        510        520        530        540 
SCAASGPQPL LLFANSQDIR HMHFDGTDYK VLLSRQMGMV FALDYDPVES KIYFAQTALK 

       550        560        570        580        590        600 
WIERANMDGS QRERLITEGV DTLEGLALDW IGRRIYWTDS GKSVVGGSDL SGKHHRIIIQ 

       610        620        630        640        650        660 
ERISRPRGIA VHPRARRLFW TDVGMSPRIE SASLQGSDRV LIASSNLLEP SGITIDYLTD 

       670        680        690        700        710        720 
TLYWCDTKRS VIEMANLDGS KRRRLIQNDV GHPFSLAVFE DHLWVSDWAI PSVIRVNKRT 

       730        740        750        760        770        780 
GQNRVRLQGS MLKPSSLVVV HPLAKPGADP CLYRNGGCEH ICQESLGTAR CLCREGFVKA 

       790        800        810        820        830        840 
WDGKMCLPQD YPILSGENAD LSKEVTSLSN STQAEVPDDD GTESSTLVAE IMVSGMNYED 

       850        860        870        880        890        900 
DCGPGGCGSH ARCVSDGETA ECQCLKGFAR DGNLCSDIDE CVLARSDCPS TSSRCINTEG 

       910        920        930        940        950        960 
GYVCRCSEGY EGDGISCFDI DECQRGAHNC GENAACTNTE GGYNCTCAGR PSSPGLSCPD 

       970        980        990       1000       1010       1020 
STAPSLLGED GHHLDRNSYP GCPSSYDGYC LNGGVCMHIE SLDSYTCNCV IGYSGDRCQT 

      1030       1040       1050       1060       1070       1080 
RDLRWWELRH AGYGQKHDIM VVAVCMVALV LLLVLGMWGT YYYRTRKQLS NPPKNPCDEP 

      1090       1100       1110       1120       1130       1140 
SGSVSSSGPN SSSGAAVASC PQPWFVVLEK HQDPKNGSLP ADGTNGAVVD AGLSPSLQLG 

      1150       1160       1170       1180       1190       1200 
SVHLTSWRQK PHIDGMGTGQ SCWIPPSSDR GPQEIEGNSH LPSYRPVGPE KLHSLQSANG 

      1210 
SCHERAPDLP RQTEPVQ 

« Hide

References

« Hide 'large scale' references
[1]"Structure of a mouse submaxillary messenger RNA encoding epidermal growth factor and seven related proteins."
Scott J., Urdea M., Quiroga M., Sanchez-Pescador R., Fong N.M., Selby M., Rutter W.J., Bell G.I.
Science 221:236-240(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Nucleotide sequence of epidermal growth factor cDNA predicts a 128,000-molecular weight protein precursor."
Gray A., Dull T.J., Ullrich A.
Nature 303:722-725(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Kidney and Salivary gland.
[5]"The primary structure of epidermal growth factor."
Savage C.R. Jr., Inagami T., Cohen S.
J. Biol. Chem. 247:7612-7621(1972) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 977-1029.
[6]"Epidermal growth factor. Location of disulfide bonds."
Savage C.R. Jr., Hash J.H., Cohen S.
J. Biol. Chem. 248:7669-7672(1973) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS.
[7]"Rhomboid family pseudoproteases use the ER quality control machinery to regulate intercellular signaling."
Zettl M., Adrain C., Strisovsky K., Lastun V., Freeman M.
Cell 145:79-91(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RHBDF1 AND RHBDF2.
[8]"Solution structure of murine epidermal growth factor determined by NMR spectroscopy and refined by energy minimization with restraints."
Montelione G.T., Wuethrich K., Burgess A.W., Nice E.C., Wagner G., Gibson K.D., Scheraga H.A.
Biochemistry 31:236-249(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 977-1029.
[9]"Three-dimensional nuclear magnetic resonance structures of mouse epidermal growth factor in acidic and physiological pH solutions."
Kohda D., Inagaki F.
Biochemistry 31:11928-11939(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 977-1029.
[10]"Role of the 6-20 disulfide bridge in the structure and activity of epidermal growth factor."
Barnham K.J., Torres A.M., Alewood D., Alewood P.F., Domagala T., Nice E.C., Norton R.S.
Protein Sci. 7:1738-1749(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 980-1024.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS17833.1.
RefSeqNP_034243.2. NM_010113.3.
UniGeneMm.252481.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP01132.
SMRP01132. Positions 977-1029.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-5762N.
IntActP01132. 5 interactions.

PTM databases

PhosphoSiteP01132.

Proteomic databases

MaxQBP01132.
PaxDbP01132.
PRIDEP01132.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029653; ENSMUSP00000029653; ENSMUSG00000028017.
GeneID13645.
KEGGmmu:13645.
UCSCuc008rig.2. mouse.

Organism-specific databases

CTD1950.
MGIMGI:95290. Egf.

Phylogenomic databases

eggNOGNOG325841.
GeneTreeENSGT00750000117524.
HOGENOMHOG000112345.
HOVERGENHBG003858.
InParanoidQ569W5.
KOK04357.
OMAKIYFAHT.
OrthoDBEOG7Q2N4J.
TreeFamTF315253.

Enzyme and pathway databases

ReactomeREACT_188257. Signal Transduction.
REACT_189085. Disease.

Gene expression databases

BgeeP01132.
CleanExMM_EGF.
GenevestigatorP01132.

Family and domain databases

Gene3D2.120.10.30. 2 hits.
InterProIPR011042. 6-blade_b-propeller_TolB-like.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
IPR000033. LDLR_classB_rpt.
IPR016317. Pro-epidermal_GF.
[Graphical view]
PfamPF00008. EGF. 1 hit.
PF07645. EGF_CA. 2 hits.
PF00058. Ldl_recept_b. 3 hits.
[Graphical view]
PIRSFPIRSF001778. Pro-epidermal_growth_factor. 1 hit.
SMARTSM00181. EGF. 5 hits.
SM00179. EGF_CA. 2 hits.
SM00135. LY. 9 hits.
[Graphical view]
SUPFAMSSF57184. SSF57184. 2 hits.
PROSITEPS00010. 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]
ProtoNetSearch...

Other

ChiTaRSEGF. mouse.
EvolutionaryTraceP01132.
NextBio284358.
PMAP-CutDBP01132.
PROP01132.
SOURCESearch...

Entry information

Entry nameEGF_MOUSE
AccessionPrimary (citable) accession number: P01132
Secondary accession number(s): E9QNX6, Q569W5, Q6P9J2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 167 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot