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Reviewed, UniProtKB/Swiss-Prot P01132 (EGF_MOUSE)

Last modified June 16, 2009. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Pro-epidermal growth factor
      Short name=EGF
Cleaved into the following chain:
    1- Recommended name:
            Epidermal growth factor
Gene names
Name: Egf
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

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

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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.

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.

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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.4
PRO_0000007543

Regions

Topological domain29 – 10381010Extracellular Potential
Transmembrane1039 – 105820 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.5
Disulfide bond990 ↔ 1007 Ref.5
Disulfide bond1009 ↔ 1018 Ref.5

Experimental info

Sequence conflict7901D → Y in CAA24115. Ref.2
Sequence conflict10481A → S in CAA24115. Ref.2
Sequence conflict12171K → Q in CAA24115. Ref.2
Sequence conflict12171K → Q in AAH60741. Ref.3

Secondary structure

1 .......... 1217
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P01132-1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: A9C7F3D512F82873

FASTA1,217133,144
        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 AENAACTNTE GGYNCTCAGR PSSPGRSCPD 

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

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

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

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

      1210 
SCHERAPDLP RQTEPVK

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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: 6602382] [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: 6304537] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Salivary gland.
[4]"The primary structure of epidermal growth factor."
Savage C.R. Jr., Inagami T., Cohen S.
J. Biol. Chem. 247:7612-7621(1972) [PubMed: 4636327] [Abstract]
Cited for: PROTEIN SEQUENCE OF 977-1029.
[5]"Epidermal growth factor. Location of disulfide bonds."
Savage C.R. Jr., Hash J.H., Cohen S.
J. Biol. Chem. 248:7669-7672(1973) [PubMed: 4750422] [Abstract]
Cited for: DISULFIDE BONDS.
[6]"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: 1731873] [Abstract]
Cited for: STRUCTURE BY NMR OF 977-1029.
[7]"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: 1445923] [Abstract]
Cited for: STRUCTURE BY NMR OF 977-1029.
[8]"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: 10082370] [Abstract]
Cited for: STRUCTURE BY NMR OF 980-1024.
+Additional computationally mapped references.

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Cross-references

Sequence databases

J00380 mRNA. Translation: AAA37539.1.
V00741 mRNA. Translation: CAA24115.1. Frameshift.
V00741 mRNA. Translation: CAA24116.1.
BC060741 mRNA. Translation: AAH60741.1.
IPIIPI00132121.
PIREGMSMG. A94272.
UniGeneMm.366162

3D structure databases

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[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:5762N.
IntActP01132. 2 interactions.

Proteomic databases

PRIDEP01132.

Genome annotation databases

EnsemblENSMUSG00000028017. Mus musculus. [Contig view]

Organism-specific databases

MGIMGI:95290. Egf.

Phylogenomic databases

HOGENOMP01132.
HOVERGENP01132.

Gene expression databases

ArrayExpressP01132.
BgeeP01132.
CleanExMM_EGF.
GermOnlineENSMUSG00000028017. Mus musculus.

Family and domain databases

InterProIPR011042. 6-blade_b-propeller_TolB-like.
IPR006209. EGF.
IPR006210. EGF-like.
IPR013032. EGF-like_reg_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_CS.
IPR001336. EGF_1.
IPR000742. EGF_3.
IPR001881. EGF_Ca_bd.
IPR013091. EGF_Ca_bd_2.
IPR018097. EGF_Ca_bd_CS.
IPR000033. LDLR.
IPR016317. Pro-epidermal_GF.
[Graphical view]
Gene3DG3DSA:2.120.10.30. 6-blade_b-propeller_TolB-like. 2 hits.
PfamPF00008. EGF. 4 hits.
PF07645. EGF_CA. 3 hits.
PF00058. Ldl_recept_b. 7 hits.
[Graphical view]
PIRSFPIRSF001778. Pro-epidermal_growth_factor. 1 hit.
PRINTSPR00009. EGFTGF.
SMARTSM00181. EGF. 5 hits.
SM00179. EGF_CA. 2 hits.
SM00135. LY. 9 hits.
[Graphical view]
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 Resources

PMAP-CutDBP01132.
SOURCESearch...

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Entry information

Entry nameEGF_MOUSE
AccessionPrimary (citable) accession number: P01132
Secondary accession number(s): Q6P9J2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 16, 2009
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents