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Protein

Pro-epidermal growth factor

Gene

EGF

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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

Names & Taxonomyi

Protein namesi
Recommended name:
Pro-epidermal growth factor
Short name:
EGF
Cleaved into the following chain:
Gene namesi
Name:EGF
OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
Proteomesi
  • UP000002254 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 10331015ExtracellularSequence analysisAdd
BLAST
Transmembranei1034 – 105421HelicalSequence analysisAdd
BLAST
Topological domaini1055 – 1216162CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence analysisAdd
BLAST
Chaini19 – 12161198Pro-epidermal growth factorPRO_0000007536Add
BLAST
Chaini973 – 102452Epidermal growth factorBy similarityPRO_0000007537Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence analysis
Glycosylationi117 – 1171N-linked (GlcNAc...)Sequence analysis
Glycosylationi148 – 1481N-linked (GlcNAc...)Sequence analysis
Disulfide bondi320 ↔ 332PROSITE-ProRule annotation
Disulfide bondi327 ↔ 341PROSITE-ProRule annotation
Disulfide bondi343 ↔ 356PROSITE-ProRule annotation
Disulfide bondi362 ↔ 373PROSITE-ProRule annotation
Disulfide bondi369 ↔ 382PROSITE-ProRule annotation
Disulfide bondi384 ↔ 397PROSITE-ProRule annotation
Disulfide bondi403 ↔ 414PROSITE-ProRule annotation
Glycosylationi406 – 4061N-linked (GlcNAc...)Sequence analysis
Disulfide bondi410 ↔ 423PROSITE-ProRule annotation
Disulfide bondi425 ↔ 438PROSITE-ProRule annotation
Disulfide bondi441 ↔ 453PROSITE-ProRule annotation
Disulfide bondi449 ↔ 463PROSITE-ProRule annotation
Disulfide bondi465 ↔ 478PROSITE-ProRule annotation
Disulfide bondi747 ↔ 758PROSITE-ProRule annotation
Disulfide bondi754 ↔ 767PROSITE-ProRule annotation
Disulfide bondi769 ↔ 782PROSITE-ProRule annotation
Glycosylationi818 – 8181N-linked (GlcNAc...)Sequence analysis
Disulfide bondi838 ↔ 849PROSITE-ProRule annotation
Disulfide bondi843 ↔ 858PROSITE-ProRule annotation
Glycosylationi855 – 8551N-linked (GlcNAc...)Sequence analysis
Disulfide bondi860 ↔ 871PROSITE-ProRule annotation
Disulfide bondi877 ↔ 891PROSITE-ProRule annotation
Disulfide bondi884 ↔ 900PROSITE-ProRule annotation
Disulfide bondi902 ↔ 913PROSITE-ProRule annotation
Disulfide bondi919 ↔ 932PROSITE-ProRule annotation
Disulfide bondi926 ↔ 941PROSITE-ProRule annotation
Glycosylationi929 – 9291N-linked (GlcNAc...)Sequence analysis
Glycosylationi938 – 9381N-linked (GlcNAc...)Sequence analysis
Disulfide bondi943 ↔ 954PROSITE-ProRule annotation
Disulfide bondi978 ↔ 992PROSITE-ProRule annotation
Disulfide bondi986 ↔ 1003PROSITE-ProRule annotation
Disulfide bondi1005 ↔ 1014PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9BEA0.
PRIDEiQ9BEA0.

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) (By similarity). Interacts with RHBDF2 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000016954.

Structurei

3D structure databases

ProteinModelPortaliQ9BEA0.
SMRiQ9BEA0. Positions 975-1021.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati86 – 12742LDL-receptor class B 1Add
BLAST
Repeati128 – 16942LDL-receptor class B 2Add
BLAST
Repeati170 – 21344LDL-receptor class B 3Add
BLAST
Repeati214 – 26047LDL-receptor class B 4Add
BLAST
Domaini316 – 35742EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini358 – 39841EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini399 – 43941EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini437 – 47943EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Repeati485 – 52541LDL-receptor class B 5Add
BLAST
Repeati526 – 56843LDL-receptor class B 6Add
BLAST
Repeati569 – 61143LDL-receptor class B 7Add
BLAST
Repeati612 – 65544LDL-receptor class B 8Add
BLAST
Repeati656 – 69843LDL-receptor class B 9Add
BLAST
Domaini743 – 78341EGF-like 5PROSITE-ProRule annotationAdd
BLAST
Domaini834 – 87239EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini873 – 91442EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini915 – 95541EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini974 – 101542EGF-like 9PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

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

Phylogenomic databases

eggNOGiENOG410IPSY. Eukaryota.
ENOG410ZVIM. LUCA.
HOGENOMiHOG000112345.
HOVERGENiHBG003858.
InParanoidiQ9BEA0.
KOiK04357.

Family and domain databases

Gene3Di2.120.10.30. 2 hits.
2.40.155.10. 1 hit.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR026823. cEGF.
IPR032485. DUF5050.
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.
IPR023413. GFP-like.
IPR009030. Growth_fac_rcpt_.
IPR000033. LDLR_classB_rpt.
IPR016317. Pro-epidermal_GF.
[Graphical view]
PfamiPF12662. cEGF. 1 hit.
PF16472. DUF5050. 1 hit.
PF00008. EGF. 1 hit.
PF07645. EGF_CA. 2 hits.
PF00058. Ldl_recept_b. 4 hits.
[Graphical view]
PIRSFiPIRSF001778. Pro-epidermal_growth_factor. 1 hit.
SMARTiSM00181. EGF. 9 hits.
SM00179. EGF_CA. 6 hits.
SM00135. LY. 9 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 5 hits.
PROSITEiPS00010. ASX_HYDROXYL. 3 hits.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 7 hits.
PS50026. EGF_3. 6 hits.
PS01187. EGF_CA. 3 hits.
PS51120. LDLRB. 9 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9BEA0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLPLIILWP VVFKCSFASL SDPENWNCPE VSPSGKGSPA CVGPAPFLIF
60 70 80 90 100
SHGISIFRID LEGTNHEQLV ADAGVSVIMD FHYNKERIYW VDPERQLLQR
110 120 130 140 150
VFLNGTRQER VCNIEKNVSG MAINWINEEL IWSNQQEGII TVTDMKGNNS
160 170 180 190 200
RVLLRALNYP ANVAIDPIER FIFWSSEVAV AGSLHRADLN GVEEKILLQT
210 220 230 240 250
SERITAVSLD VLDKQLFWIQ YSRDGSNSHI YSCNYDGGSV HLSKHLTQHN
260 270 280 290 300
FFAMSLFGNQ IFYSTWKKKT IWIANKHSGK DMVRINLDSS FVPPGGIKVV
310 320 330 340 350
HPLLQPKAES GTWAPDQKLC KWKQGNCRGS TCGQDSKSYS CTCAEGYTLS
360 370 380 390 400
QDGKYCEDVN ECAFWNHGCT LGCENIPGSY YCTCPVGFIL LPDGKRCHQL
410 420 430 440 450
IACPSNTSKC SHDCVLTSDG PICFCPEGSV LEADGKTCSG CSSPDNGGCS
460 470 480 490 500
QLCLPLSPVS WECGCFPGYD LQLDKQSCAA SGPQPFLLFA NSQDIRHMHF
510 520 530 540 550
DGTDYGTLLS QQMGMVFALD HDPVENKIYF AHTALKWIER ANMDGSQRER
560 570 580 590 600
LIEEGVDVPE GLAIDWIDRK FYWTDSGKSL IEGSDLNGKH REIIIKEDIS
610 620 630 640 650
QPRGIAVHPM AKRLFWTDMG INPRIESSSL QGIGRLVIAS SDLVWPSGIT
660 670 680 690 700
IDYVTDKLYW CDTKLSVIEM ANLDGSKRQR LAQNDVGHPF AMAVFEDHVW
710 720 730 740 750
FSDWTMPSII RVDKRTGKNR VRLRGSMLKP SSLVVVHPLA KPGAQPCLYQ
760 770 780 790 800
NGGCEHICKE RFGTAQCLCR EGFVKAPDGK MCLALNGHQI PAVGSEADLS
810 820 830 840 850
NHVTPGDVLP RSEGFEDNIT ESQHMLVAEI MVSDADDCAP VGCSTWAECV
860 870 880 890 900
SEGENATCQC LKGFTGDGKL CFDIDECEMG ITICPPTSSK CVNTEGGYVC
910 920 930 940 950
QCSEGYRGDG IHCLDINECQ LGMHTCGENA TCTNMEGNYT CMCAGSLSEP
960 970 980 990 1000
GQICADSTPP SHPMEDSHYS VRNGYRECPS SYDGYCLYNG VCMYIEAVDR
1010 1020 1030 1040 1050
YACNCVFGYV GERCQHRDLK WELRHAGQGR QRQVAAVAVG VVVLVLLLLL
1060 1070 1080 1090 1100
GLGGAHCYRT KKLSSKNLKN PYEEPSREGS SSRPSDSEAR MASFPQPWFV
1110 1120 1130 1140 1150
VIKEHQNLRN GSQPMALKDG ESADVSQFSS PEPGSVKRTS WRNEHQLYKD
1160 1170 1180 1190 1200
TEQGCCTPPS SNRGTGSQSM EQSFSVPSYE AQPIALGVEK PQSLLSAKPL
1210
LQQRAPDPPH QMKLIQ
Length:1,216
Mass (Da):134,414
Last modified:June 1, 2001 - v1
Checksum:i72536D89D3310638
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB049597 mRNA. Translation: BAB40599.1.
RefSeqiNP_001003094.1. NM_001003094.1.
UniGeneiCfa.3524.

Genome annotation databases

GeneIDi403657.
KEGGicfa:403657.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB049597 mRNA. Translation: BAB40599.1.
RefSeqiNP_001003094.1. NM_001003094.1.
UniGeneiCfa.3524.

3D structure databases

ProteinModelPortaliQ9BEA0.
SMRiQ9BEA0. Positions 975-1021.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000016954.

Proteomic databases

PaxDbiQ9BEA0.
PRIDEiQ9BEA0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi403657.
KEGGicfa:403657.

Organism-specific databases

CTDi1950.

Phylogenomic databases

eggNOGiENOG410IPSY. Eukaryota.
ENOG410ZVIM. LUCA.
HOGENOMiHOG000112345.
HOVERGENiHBG003858.
InParanoidiQ9BEA0.
KOiK04357.

Family and domain databases

Gene3Di2.120.10.30. 2 hits.
2.40.155.10. 1 hit.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR026823. cEGF.
IPR032485. DUF5050.
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.
IPR023413. GFP-like.
IPR009030. Growth_fac_rcpt_.
IPR000033. LDLR_classB_rpt.
IPR016317. Pro-epidermal_GF.
[Graphical view]
PfamiPF12662. cEGF. 1 hit.
PF16472. DUF5050. 1 hit.
PF00008. EGF. 1 hit.
PF07645. EGF_CA. 2 hits.
PF00058. Ldl_recept_b. 4 hits.
[Graphical view]
PIRSFiPIRSF001778. Pro-epidermal_growth_factor. 1 hit.
SMARTiSM00181. EGF. 9 hits.
SM00179. EGF_CA. 6 hits.
SM00135. LY. 9 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 5 hits.
PROSITEiPS00010. ASX_HYDROXYL. 3 hits.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 7 hits.
PS50026. EGF_3. 6 hits.
PS01187. EGF_CA. 3 hits.
PS51120. LDLRB. 9 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Canis familiaris epidermal growth factor (EGF) cDNA."
    Ohashi K., Takahashi N., Sugimoto C., Onuma M.
    Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiEGF_CANLF
AccessioniPrimary (citable) accession number: Q9BEA0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.