IEX1_PANTR
ID IEX1_PANTR Reviewed; 156 AA.
AC Q7YR42; Q1XI01;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=IEX1;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12799463; DOI=10.1073/pnas.1230533100;
RA Anzai T., Shiina T., Kimura N., Yanagiya K., Kohara S., Shigenari A.,
RA Yamagata T., Kulski J.K., Naruse T.K., Fujimori Y., Fukuzumi Y.,
RA Yamazaki M., Tashiro H., Iwamoto C., Umehara Y., Imanishi T., Meyer A.,
RA Ikeo K., Gojobori T., Bahram S., Inoko H.;
RT "Comparative sequencing of human and chimpanzee MHC class I regions unveils
RT insertions/deletions as the major path to genomic divergence.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7708-7713(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16702430; DOI=10.1534/genetics.106.057034;
RA Shiina T., Ota M., Shimizu S., Katsuyama Y., Hashimoto N., Takasu M.,
RA Anzai T., Kulski J.K., Kikkawa E., Naruse T., Kimura N., Yanagiya K.,
RA Watanabe A., Hosomichi K., Kohara S., Iwamoto C., Umehara Y., Meyer A.,
RA Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K., Gojobori T.,
RA Inoko H., Bahram S.;
RT "Rapid evolution of major histocompatibility complex class I genes in
RT primates generates new disease alleles in humans via hitchhiking
RT diversity.";
RL Genetics 173:1555-1570(2006).
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 provide pancreatic ductal adenocarcinoma with remarkable resistance to
CC cell stress, such as starvation or gemcitabine treatment (By
CC similarity). {ECO:0000250}.
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 -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- PTM: Phosphorylated at Thr-18, Thr-123 and Ser-126 by MAPK1/ERK2 and
CC probably MAPK3/ERK1. Upon phosphorylation by MAPK1/ERK2 and MAPK3/ERK1,
CC acquires the ability to inhibit cell death induced by various stimuli
CC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the IER3 family. {ECO:0000305}.
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DR EMBL; BA000041; BAC78173.1; -; Genomic_DNA.
DR EMBL; AB210163; BAE92767.1; -; Genomic_DNA.
DR EMBL; AB210164; BAE92769.1; -; Genomic_DNA.
DR RefSeq; NP_001038966.1; NM_001045501.1.
DR AlphaFoldDB; Q7YR42; -.
DR STRING; 9598.ENSPTRP00000030609; -.
DR PaxDb; Q7YR42; -.
DR GeneID; 462547; -.
DR KEGG; ptr:462547; -.
DR CTD; 8870; -.
DR eggNOG; ENOG502S3QE; Eukaryota.
DR HOGENOM; CLU_138897_0_0_1; -.
DR InParanoid; Q7YR42; -.
DR OrthoDB; 1582002at2759; -.
DR TreeFam; TF338252; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:InterPro.
DR GO; GO:2001020; P:regulation of response to DNA damage stimulus; IBA:GO_Central.
DR InterPro; IPR024829; IEX-1.
DR PANTHER; PTHR16915; PTHR16915; 1.
DR PRINTS; PR02100; GENEIEX1.
PE 3: Inferred from homology;
KW Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..156
FT /note="Radiation-inducible immediate-early gene IEX-1"
FT /id="PRO_0000084161"
FT TOPO_DOM 1..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..99
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..156
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphothreonine; by MAPK1"
FT /evidence="ECO:0000250|UniProtKB:P46695"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46695"
FT MOD_RES 123
FT /note="Phosphothreonine; by MAPK1"
FT /evidence="ECO:0000250|UniProtKB:P46695"
FT MOD_RES 126
FT /note="Phosphoserine; by MAPK1"
FT /evidence="ECO:0000250|UniProtKB:P46695"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 156 AA; 16930 MW; 83C067CDCAC09650 CRC64;
MCHSRSCHPT MTILQAPTPA PSTNPGPRRG SGPEIFTFDP LPEPAAAPAG RPSASRGHRK
RSRRVLYPRV VRRQLPVEEP NPAKRLLFLL LTIVFCQILM AEEGVPAPLP PEDAPNAASL
APTPVSPVLE PFNLTSEPSD YALDLSTFLQ QHPAAF
