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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)DescriptionActionsGraphical viewLength
Topological domaini19 – 1033ExtracellularSequence analysisAdd BLAST1015
Transmembranei1034 – 1054HelicalSequence analysisAdd BLAST21
Topological domaini1055 – 1216CytoplasmicSequence analysisAdd BLAST162

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000000753619 – 1216Pro-epidermal growth factorAdd BLAST1198
ChainiPRO_0000007537973 – 1024Epidermal growth factorBy similarityAdd BLAST52

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi104N-linked (GlcNAc...)Sequence analysis1
Glycosylationi117N-linked (GlcNAc...)Sequence analysis1
Glycosylationi148N-linked (GlcNAc...)Sequence analysis1
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
Glycosylationi406N-linked (GlcNAc...)Sequence analysis1
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
Glycosylationi818N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi838 ↔ 849PROSITE-ProRule annotation
Disulfide bondi843 ↔ 858PROSITE-ProRule annotation
Glycosylationi855N-linked (GlcNAc...)Sequence analysis1
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
Glycosylationi929N-linked (GlcNAc...)Sequence analysis1
Glycosylationi938N-linked (GlcNAc...)Sequence analysis1
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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati86 – 127LDL-receptor class B 1Add BLAST42
Repeati128 – 169LDL-receptor class B 2Add BLAST42
Repeati170 – 213LDL-receptor class B 3Add BLAST44
Repeati214 – 260LDL-receptor class B 4Add BLAST47
Domaini316 – 357EGF-like 1PROSITE-ProRule annotationAdd BLAST42
Domaini358 – 398EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini399 – 439EGF-like 3PROSITE-ProRule annotationAdd BLAST41
Domaini437 – 479EGF-like 4PROSITE-ProRule annotationAdd BLAST43
Repeati485 – 525LDL-receptor class B 5Add BLAST41
Repeati526 – 568LDL-receptor class B 6Add BLAST43
Repeati569 – 611LDL-receptor class B 7Add BLAST43
Repeati612 – 655LDL-receptor class B 8Add BLAST44
Repeati656 – 698LDL-receptor class B 9Add BLAST43
Domaini743 – 783EGF-like 5PROSITE-ProRule annotationAdd BLAST41
Domaini834 – 872EGF-like 6PROSITE-ProRule annotationAdd BLAST39
Domaini873 – 914EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini915 – 955EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini974 – 1015EGF-like 9PROSITE-ProRule annotationAdd BLAST42

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.
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...

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: October 5, 2016
This is version 102 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.