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Protein

Proepiregulin

Gene

Ereg

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Ligand of the EGF receptor/EGFR and ERBB4. Stimulates EGFR and ERBB4 tyrosine phosphorylation (PubMed:9990076). Contributes to inflammation, wound healing, tissue repair, and oocyte maturation by regulating angiogenesis and vascular remodeling and by stimulating cell proliferation (PubMed:24631357).1 Publication1 Publication

GO - Molecular functioni

  • epidermal growth factor receptor binding Source: UniProtKB
  • growth factor activity Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Growth factor, Mitogen

Keywords - Biological processi

Angiogenesis, Differentiation

Enzyme and pathway databases

ReactomeiR-RNO-1227986. Signaling by ERBB2.
R-RNO-1236394. Signaling by ERBB4.
R-RNO-1250196. SHC1 events in ERBB2 signaling.
R-RNO-1250342. PI3K events in ERBB4 signaling.
R-RNO-1250347. SHC1 events in ERBB4 signaling.
R-RNO-1257604. PIP3 activates AKT signaling.
R-RNO-1963640. GRB2 events in ERBB2 signaling.
R-RNO-1963642. PI3K events in ERBB2 signaling.
R-RNO-5673001. RAF/MAP kinase cascade.

Names & Taxonomyi

Protein namesi
Recommended name:
Proepiregulin
Cleaved into the following chain:
Epiregulin
Short name:
EPR
Gene namesi
Name:Ereg
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 14

Organism-specific databases

RGDi620299. Ereg.

Subcellular locationi

Epiregulin :
  • Secretedextracellular space By similarity
Proepiregulin :
  • Cell membrane By similarity; Single-pass type I membrane protein By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei113 – 13321HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222 PotentialSequence analysisAdd
BLAST
Chaini23 – 162140ProepiregulinPRO_5000054710Add
BLAST
Propeptidei23 – 55331 PublicationPRO_0000433960Add
BLAST
Chaini56 – 10146EpiregulinPRO_5000054711Add
BLAST
Propeptidei102 – 16261Removed in mature formBy similarityPRO_0000433961Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi40 – 401N-linked (GlcNAc...)Sequence analysis
Disulfide bondi61 ↔ 74PROSITE-ProRule annotation
Disulfide bondi69 ↔ 85PROSITE-ProRule annotation
Disulfide bondi87 ↔ 96PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9Z0L5.

Expressioni

Inductioni

By angiotensin II, endothelin-1 and alpha-thrombin. Strongly induced in ovarian granulosa cells by FSH stimulation.2 Publications

Gene expression databases

GenevisibleiQ9Z0L5. RN.

Interactioni

Subunit structurei

Interacts with EGFR and ERBB4.By similarity

GO - Molecular functioni

  • epidermal growth factor receptor binding Source: UniProtKB
  • growth factor activity Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000003716.

Structurei

3D structure databases

ProteinModelPortaliQ9Z0L5.
SMRiQ9Z0L5. Positions 56-101.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini57 – 9741EGF-likePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 EGF-like domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IXV0. Eukaryota.
ENOG410YNFA. LUCA.
GeneTreeiENSGT00510000048748.
HOGENOMiHOG000059635.
HOVERGENiHBG005601.
KOiK09784.
OMAiESEDNCT.
OrthoDBiEOG7JT6XP.
PhylomeDBiQ9Z0L5.
TreeFamiTF336145.

Family and domain databases

InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR015497. EGF_rcpt_ligand.
[Graphical view]
PANTHERiPTHR10740. PTHR10740. 1 hit.
PROSITEiPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9Z0L5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METFPAAWVL ALLCLGSHLL QAVISTTVIP SCIPEESEDN CTALVQMEDD
60 70 80 90 100
PRVAQVLITK CSSDMDGYCL HGHCIYLVDM SEKYCRCEVG YTGLRCEHFF
110 120 130 140 150
LTVHQPLSRE YVALTVILVF LFLIVTAGSM YYFCRWYRNR KSKKSREEYE
160
RVTSGGPGLP QV
Length:162
Mass (Da):18,404
Last modified:May 1, 1999 - v1
Checksum:iEA660DE2B34990C4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF074952 mRNA. Translation: AAD10631.1.
AB078739 Genomic DNA. Translation: BAC44880.1.
AABR07072382 Genomic DNA. No translation available.
AC108576 Genomic DNA. No translation available.
CH474060 Genomic DNA. Translation: EDL88580.1.
RefSeqiNP_067721.1. NM_021689.1.
UniGeneiRn.42897.

Genome annotation databases

EnsembliENSRNOT00000003716; ENSRNOP00000003716; ENSRNOG00000002771.
GeneIDi59325.
KEGGirno:59325.
UCSCiRGD:620299. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF074952 mRNA. Translation: AAD10631.1.
AB078739 Genomic DNA. Translation: BAC44880.1.
AABR07072382 Genomic DNA. No translation available.
AC108576 Genomic DNA. No translation available.
CH474060 Genomic DNA. Translation: EDL88580.1.
RefSeqiNP_067721.1. NM_021689.1.
UniGeneiRn.42897.

3D structure databases

ProteinModelPortaliQ9Z0L5.
SMRiQ9Z0L5. Positions 56-101.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000003716.

Proteomic databases

PaxDbiQ9Z0L5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000003716; ENSRNOP00000003716; ENSRNOG00000002771.
GeneIDi59325.
KEGGirno:59325.
UCSCiRGD:620299. rat.

Organism-specific databases

CTDi2069.
RGDi620299. Ereg.

Phylogenomic databases

eggNOGiENOG410IXV0. Eukaryota.
ENOG410YNFA. LUCA.
GeneTreeiENSGT00510000048748.
HOGENOMiHOG000059635.
HOVERGENiHBG005601.
KOiK09784.
OMAiESEDNCT.
OrthoDBiEOG7JT6XP.
PhylomeDBiQ9Z0L5.
TreeFamiTF336145.

Enzyme and pathway databases

ReactomeiR-RNO-1227986. Signaling by ERBB2.
R-RNO-1236394. Signaling by ERBB4.
R-RNO-1250196. SHC1 events in ERBB2 signaling.
R-RNO-1250342. PI3K events in ERBB4 signaling.
R-RNO-1250347. SHC1 events in ERBB4 signaling.
R-RNO-1257604. PIP3 activates AKT signaling.
R-RNO-1963640. GRB2 events in ERBB2 signaling.
R-RNO-1963642. PI3K events in ERBB2 signaling.
R-RNO-5673001. RAF/MAP kinase cascade.

Miscellaneous databases

NextBioi611917.

Gene expression databases

GenevisibleiQ9Z0L5. RN.

Family and domain databases

InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR015497. EGF_rcpt_ligand.
[Graphical view]
PANTHERiPTHR10740. PTHR10740. 1 hit.
PROSITEiPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Epiregulin is a potent vascular smooth muscle cell-derived mitogen induced by angiotensin II, endothelin-1, and thrombin."
    Taylor D.S., Cheng X., Pawlowski J.E., Wallace A.R., Ferrer P., Molloy C.J.
    Proc. Natl. Acad. Sci. U.S.A. 96:1633-1638(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 56-75, FUNCTION, INDUCTION.
    Tissue: Aortic smooth muscle.
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
    Tissue: Liver.
  3. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Epiregulin: roles in normal physiology and cancer."
    Riese D.J. II, Cullum R.L.
    Semin. Cell Dev. Biol. 28:49-56(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiEREG_RAT
AccessioniPrimary (citable) accession number: Q9Z0L5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 14, 2015
Last sequence update: May 1, 1999
Last modified: May 11, 2016
This is version 125 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, Direct protein sequencing, 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.