EPGN_MOUSE
ID EPGN_MOUSE Reviewed; 152 AA.
AC Q924X1; Q8CEX5;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Epigen;
DE AltName: Full=Epithelial mitogen;
DE Short=EPG;
DE Flags: Precursor;
GN Name=Epgn;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cByJ; TISSUE=Keratinocyte;
RX PubMed=11278323; DOI=10.1074/jbc.m006935200;
RA Strachan L., Murison J.G., Prestidge R.L., Sleeman M.A., Watson J.D.,
RA Kumble K.D.;
RT "Cloning and biological activity of epigen, a novel member of the epidermal
RT growth factor superfamily.";
RL J. Biol. Chem. 276:18265-18271(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-152.
RC STRAIN=C57BL/6J; TISSUE=Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
CC -!- FUNCTION: Promotes the growth of epithelial cells. May stimulate the
CC phosphorylation of EGFR and mitogen-activated protein kinases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in testis, heart and liver.
CC {ECO:0000269|PubMed:11278323}.
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DR EMBL; AJ291391; CAC39435.1; -; mRNA.
DR EMBL; AK010136; BAC25281.1; -; mRNA.
DR CCDS; CCDS19419.1; -.
DR RefSeq; NP_444317.1; NM_053087.2.
DR AlphaFoldDB; Q924X1; -.
DR SMR; Q924X1; -.
DR STRING; 10090.ENSMUSP00000046987; -.
DR GlyGen; Q924X1; 2 sites.
DR iPTMnet; Q924X1; -.
DR PhosphoSitePlus; Q924X1; -.
DR PaxDb; Q924X1; -.
DR PRIDE; Q924X1; -.
DR Antibodypedia; 24613; 176 antibodies from 27 providers.
DR DNASU; 71920; -.
DR Ensembl; ENSMUST00000041516; ENSMUSP00000046987; ENSMUSG00000035020.
DR GeneID; 71920; -.
DR KEGG; mmu:71920; -.
DR UCSC; uc008ybq.1; mouse.
DR CTD; 255324; -.
DR MGI; MGI:1919170; Epgn.
DR VEuPathDB; HostDB:ENSMUSG00000035020; -.
DR eggNOG; ENOG502S4QW; Eukaryota.
DR GeneTree; ENSGT00510000048556; -.
DR InParanoid; Q924X1; -.
DR OMA; DKPSCIC; -.
DR OrthoDB; 1425022at2759; -.
DR PhylomeDB; Q924X1; -.
DR TreeFam; TF335931; -.
DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
DR Reactome; R-MMU-177929; Signaling by EGFR.
DR Reactome; R-MMU-179812; GRB2 events in EGFR signaling.
DR Reactome; R-MMU-180292; GAB1 signalosome.
DR Reactome; R-MMU-180336; SHC1 events in EGFR signaling.
DR Reactome; R-MMU-182971; EGFR downregulation.
DR Reactome; R-MMU-212718; EGFR interacts with phospholipase C-gamma.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-MMU-9009391; Extra-nuclear estrogen signaling.
DR BioGRID-ORCS; 71920; 3 hits in 71 CRISPR screens.
DR PRO; PR:Q924X1; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q924X1; protein.
DR Bgee; ENSMUSG00000035020; Expressed in cornea and 18 other tissues.
DR ExpressionAtlas; Q924X1; baseline and differential.
DR Genevisible; Q924X1; MM.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:HGNC-UCL.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; IDA:HGNC-UCL.
DR GO; GO:0008083; F:growth factor activity; IDA:HGNC-UCL.
DR GO; GO:0048018; F:receptor ligand activity; IDA:MGI.
DR GO; GO:0030297; F:transmembrane receptor protein tyrosine kinase activator activity; IDA:MGI.
DR GO; GO:0001525; P:angiogenesis; ISS:HGNC-UCL.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IDA:MGI.
DR GO; GO:0000165; P:MAPK cascade; IDA:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0045741; P:positive regulation of epidermal growth factor-activated receptor activity; IDA:HGNC-UCL.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IDA:HGNC-UCL.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:HGNC-UCL.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; IDA:HGNC-UCL.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR015497; EGF_rcpt_ligand.
DR PANTHER; PTHR10740; PTHR10740; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; EGF-like domain; Glycoprotein; Growth factor; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..152
FT /note="Epigen"
FT /id="PRO_0000045463"
FT TOPO_DOM 19..109
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 55..95
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 59..72
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 67..83
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 85..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CONFLICT 17
FT /note="K -> E (in Ref. 2; BAC25281)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 152 AA; 16799 MW; 3302888CFFEA558E CRC64;
MALGVLIAVC LLFKAMKAAL SEEAEVIPPS TAQQSNWTFN NTEADYIEEP VALKFSHPCL
EDHNSYCING ACAFHHELKQ AICRCFTGYT GQRCEHLTLT SYAVDSYEKY IAIGIGVGLL
ISAFLAVFYC YIRKRCINLK SPYIICSGGS PL
