GenomeNet

Database: UniProt
Entry: Q924X1
LinkDB: Q924X1
Original site: Q924X1 
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   13-FEB-2019, entry version 122.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   epidermal 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
CC       the 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
CC       liver. {ECO:0000269|PubMed:11278323}.
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   UniGene; Mm.197319; -.
DR   ProteinModelPortal; Q924X1; -.
DR   SMR; Q924X1; -.
DR   STRING; 10090.ENSMUSP00000046987; -.
DR   iPTMnet; Q924X1; -.
DR   PhosphoSitePlus; Q924X1; -.
DR   PaxDb; Q924X1; -.
DR   PRIDE; Q924X1; -.
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   eggNOG; ENOG410IVWD; Eukaryota.
DR   eggNOG; ENOG410Y2CI; LUCA.
DR   GeneTree; ENSGT00510000048556; -.
DR   HOGENOM; HOG000041330; -.
DR   HOVERGEN; HBG079616; -.
DR   InParanoid; Q924X1; -.
DR   OMA; YCYVRKR; -.
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   PRO; PR:Q924X1; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   Bgee; ENSMUSG00000035020; Expressed in 31 organ(s), highest expression level in cornea.
DR   ExpressionAtlas; Q924X1; baseline and differential.
DR   Genevisible; Q924X1; MM.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:HGNC.
DR   GO; GO:0005154; F:epidermal growth factor receptor binding; IDA:HGNC.
DR   GO; GO:0008083; F:growth factor activity; IDA:HGNC.
DR   GO; GO:0000187; P:activation of MAPK activity; IDA:HGNC.
DR   GO; GO:0001525; P:angiogenesis; ISS:HGNC.
DR   GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IBA:GO_Central.
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.
DR   GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IDA:HGNC.
DR   GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:HGNC.
DR   GO; GO:0045840; P:positive regulation of mitotic nuclear division; IDA:HGNC.
DR   InterPro; IPR013032; EGF-like_CS.
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   Complete proteome; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Growth factor; Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   CHAIN        19    152       Epigen.
FT                                /FTId=PRO_0000045463.
FT   TOPO_DOM     19    109       Extracellular. {ECO:0000255}.
FT   TRANSMEM    110    130       Helical. {ECO:0000255}.
FT   TOPO_DOM    131    152       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       55     95       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   CARBOHYD     36     36       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     40     40       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     59     72       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     67     83       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     85     94       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   CONFLICT     17     17       K -> E (in Ref. 2; BAC25281).
FT                                {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
//
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