IEX1_MOUSE
ID IEX1_MOUSE Reviewed; 160 AA.
AC P46694; Q4FJY1; Q91VZ5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Radiation-inducible immediate-early gene IEX-1;
DE AltName: Full=Immediate early protein GLY96;
DE AltName: Full=Immediate early response 3 protein;
GN Name=Ier3; Synonyms=Gly96, Iex1;
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].
RC STRAIN=BALB/cJ;
RX PubMed=8437864;
RA Charles C.H., Yoon J.K., Simske J.S., Lau L.F.;
RT "Genomic structure, cDNA sequence, and expression of gly96, a growth
RT factor-inducible immediate-early gene encoding a short-lived glycosylated
RT protein.";
RL Oncogene 8:797-801(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=14644419; DOI=10.1016/s0014-5793(03)01239-0;
RA Lopez-Casas P.P., del Mazo J.;
RT "Regulation of flotillin-1 in the establishment of NIH-3T3 cell-cell
RT interactions.";
RL FEBS Lett. 555:223-228(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, and Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION.
RX PubMed=22565310; DOI=10.1172/jci60144;
RA Hamidi T., Algul H., Cano C.E., Sandi M.J., Molejon M.I., Riemann M.,
RA Calvo E.L., Lomberk G., Dagorn J.C., Weih F., Urrutia R., Schmid R.M.,
RA Iovanna J.L.;
RT "Nuclear protein 1 promotes pancreatic cancer development and protects
RT cells from stress by inhibiting apoptosis.";
RL J. Clin. Invest. 122:2092-2103(2012).
CC -!- FUNCTION: May play a role in the ERK signaling pathway by inhibiting
CC the dephosphorylation of ERK by phosphatase PP2A-PPP2R5C holoenzyme.
CC Acts also as an ERK downstream effector mediating survival (By
CC similarity). As a member of the NUPR1/RELB/IER3 survival pathway, may
CC allow the development of pancreatic intraepithelial neoplasias.
CC {ECO:0000250, ECO:0000269|PubMed:22565310}.
CC -!- SUBUNIT: Interacts with the PPP2R5C-PP2A holoenzyme and ERK kinases;
CC regulates ERK dephosphorylation. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the lung, testes and the
CC uterus.
CC -!- INDUCTION: By serum growth factors and TPA.
CC -!- PTM: Glycosylated.
CC -!- SIMILARITY: Belongs to the IER3 family. {ECO:0000305}.
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DR EMBL; X67644; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY168443; AAO39405.1; -; Genomic_DNA.
DR EMBL; AK051003; BAC34493.1; -; mRNA.
DR EMBL; AK170477; BAE41821.1; -; mRNA.
DR EMBL; CT010247; CAJ18455.1; -; mRNA.
DR EMBL; CT010271; CAJ18479.1; -; mRNA.
DR EMBL; GL456179; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006950; AAH06950.1; -; mRNA.
DR CCDS; CCDS28704.1; -.
DR PIR; S33363; S33363.
DR RefSeq; NP_598423.1; NM_133662.2.
DR AlphaFoldDB; P46694; -.
DR STRING; 10090.ENSMUSP00000003635; -.
DR GlyGen; P46694; 1 site.
DR iPTMnet; P46694; -.
DR PhosphoSitePlus; P46694; -.
DR jPOST; P46694; -.
DR PaxDb; P46694; -.
DR PeptideAtlas; P46694; -.
DR PRIDE; P46694; -.
DR ProteomicsDB; 273267; -.
DR ProteomicsDB; 308489; -.
DR Antibodypedia; 26624; 180 antibodies from 27 providers.
DR DNASU; 15937; -.
DR Ensembl; ENSMUST00000003635; ENSMUSP00000003635; ENSMUSG00000003541.
DR GeneID; 15937; -.
DR KEGG; mmu:15937; -.
DR UCSC; uc008cio.1; mouse.
DR CTD; 8870; -.
DR MGI; MGI:104814; Ier3.
DR VEuPathDB; HostDB:ENSMUSG00000003541; -.
DR eggNOG; ENOG502S3QE; Eukaryota.
DR GeneTree; ENSGT00390000003213; -.
DR HOGENOM; CLU_138897_0_0_1; -.
DR InParanoid; P46694; -.
DR OMA; VIFCQIL; -.
DR OrthoDB; 1582002at2759; -.
DR PhylomeDB; P46694; -.
DR TreeFam; TF338252; -.
DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR BioGRID-ORCS; 15937; 2 hits in 110 CRISPR screens.
DR ChiTaRS; Ier3; mouse.
DR PRO; PR:P46694; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P46694; protein.
DR Bgee; ENSMUSG00000003541; Expressed in right lung lobe and 243 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0006096; P:glycolytic process; IMP:MGI.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IDA:MGI.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IMP:MGI.
DR GO; GO:0045820; P:negative regulation of glycolytic process; IMP:MGI.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IMP:MGI.
DR GO; GO:1901029; P:negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IDA:MGI.
DR GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; IMP:MGI.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:MGI.
DR GO; GO:0006282; P:regulation of DNA repair; IMP:MGI.
DR GO; GO:0046822; P:regulation of nucleocytoplasmic transport; IMP:MGI.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IDA:MGI.
DR GO; GO:2001020; P:regulation of response to DNA damage stimulus; IMP:MGI.
DR GO; GO:0001562; P:response to protozoan; IMP:MGI.
DR InterPro; IPR024829; IEX-1.
DR PANTHER; PTHR16915; PTHR16915; 1.
DR PRINTS; PR02100; GENEIEX1.
PE 1: Evidence at protein level;
KW Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..160
FT /note="Radiation-inducible immediate-early gene IEX-1"
FT /id="PRO_0000084160"
FT TOPO_DOM 1..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..102
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..153
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 134
FT /note="E -> G (in Ref. 4; CAJ18479)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 160 AA; 17655 MW; 0666DF96E751FCF4 CRC64;
MCHSRNHLHT MTGLRAPSPA PSTGPELRRG SGPEIFTFDP LPERAVVSTA RLNTSRGHRK
RSRRVLYPRV VRRQLPTEEP NIAKRVLFLL FAIIFCQILM AEEGVSQPLA PEDATSAVTP
EPISAPITAP PVLEPLNLTS ESSDYALDLK AFLQQHPAAF
