EI24_RAT
ID EI24_RAT Reviewed; 340 AA.
AC Q4KM77;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Etoposide-induced protein 2.4 homolog;
GN Name=Ei24;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 [2]
RP FUNCTION.
RX PubMed=20550938; DOI=10.1016/j.cell.2010.04.034;
RA Tian Y., Li Z., Hu W., Ren H., Tian E., Zhao Y., Lu Q., Huang X., Yang P.,
RA Li X., Wang X., Kovacs A.L., Yu L., Zhang H.;
RT "C. elegans screen identifies autophagy genes specific to multicellular
RT organisms.";
RL Cell 141:1042-1055(2010).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-47; SER-326 AND
RP SER-330, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Acts as a negative growth regulator via p53-mediated
CC apoptosis pathway. Regulates formation of degradative autolysosomes
CC during autophagy. {ECO:0000269|PubMed:20550938}.
CC -!- SUBUNIT: Interacts with BCL2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Endoplasmic
CC reticulum membrane {ECO:0000250}; Multi-pass membrane protein
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the EI24 family. {ECO:0000305}.
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DR EMBL; BC098721; AAH98721.1; -; mRNA.
DR RefSeq; NP_001020831.1; NM_001025660.1.
DR RefSeq; XP_006242862.1; XM_006242800.3.
DR RefSeq; XP_006242863.1; XM_006242801.3.
DR AlphaFoldDB; Q4KM77; -.
DR STRING; 10116.ENSRNOP00000042710; -.
DR iPTMnet; Q4KM77; -.
DR PhosphoSitePlus; Q4KM77; -.
DR jPOST; Q4KM77; -.
DR PaxDb; Q4KM77; -.
DR PRIDE; Q4KM77; -.
DR GeneID; 300514; -.
DR KEGG; rno:300514; -.
DR UCSC; RGD:1309868; rat.
DR CTD; 9538; -.
DR RGD; 1309868; Ei24.
DR VEuPathDB; HostDB:ENSRNOG00000030391; -.
DR eggNOG; KOG3966; Eukaryota.
DR HOGENOM; CLU_031164_0_0_1; -.
DR InParanoid; Q4KM77; -.
DR OMA; QCCALNG; -.
DR OrthoDB; 889537at2759; -.
DR PhylomeDB; Q4KM77; -.
DR PRO; PR:Q4KM77; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000030391; Expressed in liver and 19 other tissues.
DR Genevisible; Q4KM77; RN.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0061676; F:importin-alpha family protein binding; ISO:RGD.
DR GO; GO:0006914; P:autophagy; ISO:RGD.
DR GO; GO:0071494; P:cellular response to UV-C; ISO:RGD.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; ISO:RGD.
DR GO; GO:0016236; P:macroautophagy; IBA:GO_Central.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:RGD.
DR GO; GO:0042308; P:negative regulation of protein import into nucleus; ISO:RGD.
DR GO; GO:0050885; P:neuromuscular process controlling balance; ISO:RGD.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:RGD.
DR InterPro; IPR009890; EI24.
DR PANTHER; PTHR21389; PTHR21389; 1.
PE 1: Evidence at protein level;
KW Acetylation; Apoptosis; Autophagy; Cytoplasm; Endoplasmic reticulum;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O14681"
FT CHAIN 2..340
FT /note="Etoposide-induced protein 2.4 homolog"
FT /id="PRO_0000331478"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 319..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O14681"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14681"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61070"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 340 AA; 38893 MW; 624D4BCFE2917C9C CRC64;
MADSVKTFLQ DLGRGIKDSI WGICTISKLD ARIQQKREEQ RRRRASSLLA QRRAQSVERK
QESEPRIVSR IFQCCAWNGG VFWFSLLLFY RVFIPVLQSV TARVIGDPSL HGDVWSWLEF
FLTSIFSALW VLPLFVLSKV VNAIWFQDIA DLAFEVSGRK PHPFPSVSKI IADMLFNLLL
QALFLIQGMF VSLFPIHLVG QLVSLLHMSL LYSLYCFEYR WFNKGIEMHQ RLSNIERNWP
YYFGFGLPLA FLTAMQSSYI ISGCLFSILF PLFIISANEA KTPGKAYLFQ LRLFSLVVFL
SNRLFHKTVY LQSALSSSSS AEKFPSPHPS PAKLKAAAGH
