Skip Header

Contribute Send feedback
Read comments (?) or add your own

P07522 (EGF_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
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
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length1133 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) By similarity. Interacts with RHBDF2 By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein.

Sequence similarities

Contains 9 EGF-like domains.

Contains 9 LDL-receptor class B repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 11331112Pro-epidermal growth factor
PRO_0000007546
Chain974 – 102653Epidermal growth factor
PRO_0000007547

Regions

Topological domain22 – 10351014Extracellular Potential
Transmembrane1036 – 105722Helical; Potential
Topological domain1058 – 113376Cytoplasmic Potential
Repeat87 – 12842LDL-receptor class B 1
Repeat129 – 17042LDL-receptor class B 2
Repeat171 – 21242LDL-receptor class B 3
Repeat213 – 25947LDL-receptor class B 4
Domain322 – 35635EGF-like 1; incomplete
Domain357 – 39741EGF-like 2; calcium-binding Potential
Domain398 – 43841EGF-like 3
Domain436 – 47843EGF-like 4
Repeat485 – 52541LDL-receptor class B 5
Repeat526 – 56843LDL-receptor class B 6
Repeat569 – 61143LDL-receptor class B 7
Repeat612 – 65544LDL-receptor class B 8
Repeat656 – 69843LDL-receptor class B 9
Domain743 – 78341EGF-like 5
Domain835 – 87339EGF-like 6
Domain874 – 91542EGF-like 7; calcium-binding Potential
Domain916 – 95641EGF-like 8; calcium-binding Potential
Domain975 – 101642EGF-like 9

Amino acid modifications

Glycosylation1051N-linked (GlcNAc...) Potential
Glycosylation1181N-linked (GlcNAc...) Potential
Glycosylation1491N-linked (GlcNAc...) Potential
Glycosylation4051N-linked (GlcNAc...) Potential
Glycosylation9301N-linked (GlcNAc...) Potential
Glycosylation9411N-linked (GlcNAc...) Potential
Disulfide bond361 ↔ 372 By similarity
Disulfide bond368 ↔ 381 By similarity
Disulfide bond383 ↔ 396 By similarity
Disulfide bond402 ↔ 413 By similarity
Disulfide bond409 ↔ 422 By similarity
Disulfide bond424 ↔ 437 By similarity
Disulfide bond440 ↔ 452 By similarity
Disulfide bond448 ↔ 462 By similarity
Disulfide bond464 ↔ 477 By similarity
Disulfide bond747 ↔ 758 By similarity
Disulfide bond754 ↔ 767 By similarity
Disulfide bond769 ↔ 782 By similarity
Disulfide bond839 ↔ 850 By similarity
Disulfide bond844 ↔ 859 By similarity
Disulfide bond861 ↔ 872 By similarity
Disulfide bond878 ↔ 892 By similarity
Disulfide bond885 ↔ 901 By similarity
Disulfide bond903 ↔ 914 By similarity
Disulfide bond920 ↔ 933 By similarity
Disulfide bond927 ↔ 942 By similarity
Disulfide bond944 ↔ 955 By similarity
Disulfide bond979 ↔ 993
Disulfide bond987 ↔ 1004
Disulfide bond1006 ↔ 1015

Natural variations

Natural variant9551C → V.

Experimental info

Sequence conflict1024 – 10252KL → NW in CAA31241. Ref.4
Sequence conflict1109 – 113325QPKNG…LSSSL → SGAGVSSGPQPWFVVLEEHQ in CAA31241. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P07522 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: C224A302E9578031

FASTA1,133124,126
        10         20         30         40         50         60 
MLFSLTFLSV FLKITVLSVT AQQTRNCQSG PLERSGTTTY AAAGPPRFLI FLQGNSIFRI 

        70         80         90        100        110        120 
NTDGTNHQQL VVDAGVSVVM DFHYKEERLY WVDLERQLLQ RVFFNGSGQE TVCKVDKNVS 

       130        140        150        160        170        180 
GLAINWIDGE ILRTDRWKGV ITVTDMNGNN SRVLLSSLKR PANILVDPTE RLIFWSSVVT 

       190        200        210        220        230        240 
GNLHRADLGG MDVKTLLEAP ERISVLILDI LDKRLFWAQD GREGSHGYIH SCDYNGGSIH 

       250        260        270        280        290        300 
HIRHQARHDL LTMAIFGDKI LYSALKEKAI WIADKHTGKN VVRVNLDPAS VPPRELRVVH 

       310        320        330        340        350        360 
LHAQPGTENR AQASDSERCK QRRGQCLYSL SERDPNSDSS ACAEGYTLSR DRKYCEDVNE 

       370        380        390        400        410        420 
CALQNHGCTL GCENIPGSYY CTCPTGFVLL PDGKRCHELV ACPGNRSECS HDCILTSDGP 

       430        440        450        460        470        480 
LCICPAGSVL GKDGKTCTGC SFSDNGGCSQ ICLPLSLASW ECDCFPGYDL QLDRKSCAAS 

       490        500        510        520        530        540 
MGPQPFLLFA NSQDIRHMHF DGTDYKTLLS RQMGMVFALD YDPVESKIYF AQTALKWIER 

       550        560        570        580        590        600 
ANLDGSQRER RITEGVDTPE GLAVDWIGRR IYWTDSGKSV IEGSDLSGKH HQIIIKESIS 

       610        620        630        640        650        660 
RPRGIAVHPK ARRLFWTDTG MSPRIESSSL QGSDRTLIAS SNLLEPSGIA IDYLTDTLYW 

       670        680        690        700        710        720 
CDTKLSVIEM ADLDGSKRRR LTQNDVGHPF SLAVFEDHVW FSDWAIPSVI RVNKRTGQNR 

       730        740        750        760        770        780 
VRLRGSMLKP SSLVVVHPLA KPGADPCLHR NGGCEHICQE SLGTAQCLCR EGFVKAPDGK 

       790        800        810        820        830        840 
MCLTRKDDQI LAGDNADLSK EVASLDNSPK AYVPDDDRTE SSTLVAEIMV SGLNYEDDCG 

       850        860        870        880        890        900 
PGGCGSHAHC ISEGEAAVCQ CLKGFAGDGN LCSDIDECEL GSSDCPPTSS RCINTEGGYV 

       910        920        930        940        950        960 
CQCSEGYEGD GIYCLDVDEC QQGSHGCSEN ATCTNTEGGY NCTCAGCPSA PGLPCPDSTS 

       970        980        990       1000       1010       1020 
PSLLGKDGCH WVRNSNTGCP PSYDGYCLNG GVCMYVESVD RYVCNCVIGY IGERCQHRDL 

      1030       1040       1050       1060       1070       1080 
RWWKLRHADY GQRHDITVVS VCVVALALLL LLGMWGTYYY RTRKQLSESS KKPSEESSSN 

      1090       1100       1110       1120       1130 
VSSNGPDSSG AGVSSGPQPW FVVLEEHQQP KNGRLPAAGT NGAVVEAGLS SSL

« Hide

References

[1]"Cloning and sequencing of the rat preproepidermal growth factor cDNA: comparison with mouse and human sequences."
Price P.M., Saggi S.J., Safirstein R.
DNA Cell Biol. 11:481-487(1992) [PubMed: 1524680] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[2]Price P.M.
Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
Tissue: Kidney.
[3]"Rat epidermal growth factor: complete amino acid sequence. Homology with the corresponding murine and human proteins; isolation of a form truncated at both ends with full in vitro biological activity."
Simpson R.J., Smith J.A., Moritz R.L., O'Hare M.J., Rudland P.S., Morrison J.R., Lloyd C.J., Grego B., Burgess A.W., Nice E.C.
Eur. J. Biochem. 153:629-637(1985) [PubMed: 3000782] [Abstract]
Cited for: PROTEIN SEQUENCE OF 974-1021.
[4]"Cloning and sequence analysis of a cDNA for rat epidermal growth factor."
Dorow D.S., Simpson R.J.
Nucleic Acids Res. 16:9338-9338(1988) [PubMed: 3262867] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 994-1133.
Strain: Sprague-Dawley.
Tissue: Kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U04842 mRNA. Translation: AAB60436.1.
X12748 mRNA. Translation: CAA31241.1.
IPIIPI00231848.
PIREGRT. I52995.
RefSeqNP_036974.1. NM_012842.1.
UniGeneRn.6075.

3D structure databases

ProteinModelPortalP07522.
SMRP07522. Positions 974-1026.
ModBaseSearch...

Protein-protein interaction databases

STRINGP07522.

PTM databases

PhosphoSiteP07522.

Proteomic databases

PRIDEP07522.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID25313.
KEGGrno:25313.

Organism-specific databases

CTD1950.
RGD2542. Egf.

Phylogenomic databases

eggNOGroNOG08186.
HOVERGENHBG003858.
InParanoidP07522.
OrthoDBEOG480HVT.

Gene expression databases

GenevestigatorP07522.
GermOnlineENSRNOG00000032707. Rattus norvegicus.

Family and domain databases

InterProIPR011042. 6-blade_b-propeller_TolB-like.
IPR006210. EGF-like.
IPR001881. EGF-like_Ca-bd.
IPR013032. EGF-like_reg_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR000742. EGF_3.
IPR018097. EGF_Ca-bd_CS.
IPR000033. LDLR_classB_rpt.
IPR016317. Pro-epidermal_GF.
[Graphical view]
Gene3DG3DSA:2.120.10.30. 6-blade_b-propeller_TolB-like. 2 hits.
KOK04357.
PfamPF07645. EGF_CA. 3 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. 8 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. 9 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio606131.

Entry information

Entry nameEGF_RAT
AccessionPrimary (citable) accession number: P07522
Secondary accession number(s): Q63183
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: February 1, 1996
Last modified: November 16, 2011
This is version 108 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents