P07522 (EGF_RAT)
Reviewed,
UniProtKB/Swiss-Prot
Last modified
August 10, 2010.
Version 98.
History...
Names and origin
| Protein names | Recommended name: Pro-epidermal growth factor Short name=EGF Cleaved into the following chain:
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| Gene names |
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| Organism | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 1133 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence 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. |
| Subcellular location | |
| Sequence similarities | Contains 9 EGF-like domains. Contains 9 LDL-receptor class B repeats. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Membrane |
| Domain | EGF-like domain Repeat Signal Transmembrane Transmembrane helix |
| Molecular function | Growth factor |
| PTM | Disulfide bond Glycoprotein |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | epidermal growth factor receptor signaling pathway Inferred from direct assay. Source: RGD regulation of protein secretionInferred from mutant phenotype. Source: RGD |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW soluble fractionInferred from direct assay. Source: RGD |
| Molecular function | calcium ion binding Inferred from electronic annotation. Source: InterPro epidermal growth factor receptor bindingInferred from direct assay. Source: RGD growth factor activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 21 | 21 | Potential | ||||||||
| Chain | 22 – 1133 | 1112 | Pro-epidermal growth factor | PRO_0000007546 | |||||||
| Chain | 974 – 1026 | 53 | Epidermal growth factor | PRO_0000007547 | |||||||
Regions | |||||||||||
| Topological domain | 22 – 1035 | 1014 | Extracellular Potential | ||||||||
| Transmembrane | 1036 – 1057 | 22 | Helical; Potential | ||||||||
| Topological domain | 1058 – 1133 | 76 | Cytoplasmic Potential | ||||||||
| Repeat | 87 – 128 | 42 | LDL-receptor class B 1 | ||||||||
| Repeat | 129 – 170 | 42 | LDL-receptor class B 2 | ||||||||
| Repeat | 171 – 212 | 42 | LDL-receptor class B 3 | ||||||||
| Repeat | 213 – 259 | 47 | LDL-receptor class B 4 | ||||||||
| Domain | 322 – 356 | 35 | EGF-like 1; incomplete | ||||||||
| Domain | 357 – 397 | 41 | EGF-like 2; calcium-binding Potential | ||||||||
| Domain | 398 – 438 | 41 | EGF-like 3 | ||||||||
| Domain | 436 – 478 | 43 | EGF-like 4 | ||||||||
| Repeat | 485 – 525 | 41 | LDL-receptor class B 5 | ||||||||
| Repeat | 526 – 568 | 43 | LDL-receptor class B 6 | ||||||||
| Repeat | 569 – 611 | 43 | LDL-receptor class B 7 | ||||||||
| Repeat | 612 – 655 | 44 | LDL-receptor class B 8 | ||||||||
| Repeat | 656 – 698 | 43 | LDL-receptor class B 9 | ||||||||
| Domain | 743 – 783 | 41 | EGF-like 5 | ||||||||
| Domain | 835 – 873 | 39 | EGF-like 6 | ||||||||
| Domain | 874 – 915 | 42 | EGF-like 7; calcium-binding Potential | ||||||||
| Domain | 916 – 956 | 41 | EGF-like 8; calcium-binding Potential | ||||||||
| Domain | 975 – 1016 | 42 | EGF-like 9 | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 105 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 118 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 149 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 405 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 930 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 941 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 361 ↔ 372 | By similarity | |||||||||
| Disulfide bond | 368 ↔ 381 | By similarity | |||||||||
| Disulfide bond | 383 ↔ 396 | By similarity | |||||||||
| Disulfide bond | 402 ↔ 413 | By similarity | |||||||||
| Disulfide bond | 409 ↔ 422 | By similarity | |||||||||
| Disulfide bond | 424 ↔ 437 | By similarity | |||||||||
| Disulfide bond | 440 ↔ 452 | By similarity | |||||||||
| Disulfide bond | 448 ↔ 462 | By similarity | |||||||||
| Disulfide bond | 464 ↔ 477 | By similarity | |||||||||
| Disulfide bond | 747 ↔ 758 | By similarity | |||||||||
| Disulfide bond | 754 ↔ 767 | By similarity | |||||||||
| Disulfide bond | 769 ↔ 782 | By similarity | |||||||||
| Disulfide bond | 839 ↔ 850 | By similarity | |||||||||
| Disulfide bond | 844 ↔ 859 | By similarity | |||||||||
| Disulfide bond | 861 ↔ 872 | By similarity | |||||||||
| Disulfide bond | 878 ↔ 892 | By similarity | |||||||||
| Disulfide bond | 885 ↔ 901 | By similarity | |||||||||
| Disulfide bond | 903 ↔ 914 | By similarity | |||||||||
| Disulfide bond | 920 ↔ 933 | By similarity | |||||||||
| Disulfide bond | 927 ↔ 942 | By similarity | |||||||||
| Disulfide bond | 944 ↔ 955 | By similarity | |||||||||
| Disulfide bond | 979 ↔ 993 | ||||||||||
| Disulfide bond | 987 ↔ 1004 | ||||||||||
| Disulfide bond | 1006 ↔ 1015 | ||||||||||
Natural variations | |||||||||||
| Natural variant | 955 | 1 | C → V | ||||||||
Experimental info | |||||||||||
| Sequence conflict | 1024 – 1025 | 2 | KL → NW in CAA31241. Ref.4 | ||||||||
| Sequence conflict | 1108 | 1 | Q → S Ref.4 | ||||||||
Sequences
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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 994-1108. 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. |
| IPI | IPI00231848. |
| PIR | EGRT. I52995. |
| RefSeq | NP_036974.1. |
| UniGene | Rn.6075. |
3D structure databases | |
| ProteinModelPortal | P07522. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P07522. |
Genome annotation databases | |
| Ensembl | ENSRNOT00000046113; ENSRNOP00000040920; ENSRNOG00000032707; Rattus norvegicus. [Genome view] |
| GeneID | 25313. |
| KEGG | rno:25313. |
Organism-specific databases | |
| CTD | 25313. |
| RGD | 2542. Egf. |
Phylogenomic databases | |
| eggNOG | roNOG08186. |
| HOVERGEN | HBG003858. |
| InParanoid | P07522. |
Gene expression databases | |
| Genevestigator | P07522. |
| GermOnline | ENSRNOG00000032707. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR011042. 6-blade_b-propeller_TolB-like. IPR006210. EGF-like. IPR013032. EGF-like_reg_CS. IPR000152. EGF-type_Asp/Asn_hydroxyl_site. IPR000742. EGF_3. IPR001881. EGF_Ca-bd. IPR013091. EGF_Ca-bd_2. IPR018097. EGF_Ca-bd_CS. IPR000033. LDL_rcpt_classB_YWTD_rpt. IPR016317. Pro-epidermal_GF. [Graphical view] |
| Gene3D | G3DSA:2.120.10.30. 6-blade_b-propeller_TolB-like. 2 hits. |
| Pfam | PF07645. EGF_CA. 3 hits. PF00058. Ldl_recept_b. 3 hits. [Graphical view] |
| PIRSF | PIRSF001778. Pro-epidermal_growth_factor. 1 hit. |
| SMART | SM00181. EGF. 5 hits. SM00179. EGF_CA. 2 hits. SM00135. LY. 8 hits. [Graphical view] |
| PROSITE | PS00010. 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] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 606131. |
Entry information
| Entry name | EGF_RAT | ||||||||
| Accession | Primary (citable) accession number: P07522 Secondary accession number(s): Q63183 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with


