EIF2A_MOUSE
ID EIF2A_MOUSE Reviewed; 581 AA.
AC Q8BJW6; Q05C11; Q640P8;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Eukaryotic translation initiation factor 2A;
DE Short=eIF-2A;
DE Contains:
DE RecName: Full=Eukaryotic translation initiation factor 2A, N-terminally processed;
GN Name=Eif2a; Synonyms=D3Ertd194e;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Muellerian duct;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
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).
CC -!- FUNCTION: Functions in the early steps of protein synthesis of a small
CC number of specific mRNAs. Acts by directing the binding of methionyl-
CC tRNAi to 40S ribosomal subunits. In contrast to the eIF-2 complex, it
CC binds methionyl-tRNAi to 40S subunits in a codon-dependent manner,
CC whereas the eIF-2 complex binds methionyl-tRNAi to 40S subunits in a
CC GTP-dependent manner. {ECO:0000250|UniProtKB:Q9BY44}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BJW6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BJW6-2; Sequence=VSP_024977, VSP_024978;
CC -!- SIMILARITY: Belongs to the WD repeat EIF2A family. {ECO:0000305}.
CC -!- CAUTION: This gene should not be confused with EIF2S1, frequently
CC called eIF2-alpha in the literature, and with which it shares the alias
CC EIF2A. EIF2S1 is the alpha subunit of the eIF2 translation initiation
CC complex. Although both of these proteins function in binding initiator
CC tRNA to the 40S ribosomal subunit, the EIF2A protein does so in a
CC codon-dependent manner, whereas eIF2 complex requires GTP.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC37320.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK078519; BAC37320.1; ALT_INIT; mRNA.
DR EMBL; BC030447; AAH30447.1; -; mRNA.
DR EMBL; BC082557; AAH82557.1; -; mRNA.
DR CCDS; CCDS17367.1; -. [Q8BJW6-1]
DR RefSeq; NP_001005509.1; NM_001005509.2. [Q8BJW6-1]
DR AlphaFoldDB; Q8BJW6; -.
DR SMR; Q8BJW6; -.
DR BioGRID; 230831; 19.
DR IntAct; Q8BJW6; 1.
DR STRING; 10090.ENSMUSP00000029387; -.
DR iPTMnet; Q8BJW6; -.
DR PhosphoSitePlus; Q8BJW6; -.
DR SwissPalm; Q8BJW6; -.
DR EPD; Q8BJW6; -.
DR jPOST; Q8BJW6; -.
DR MaxQB; Q8BJW6; -.
DR PaxDb; Q8BJW6; -.
DR PeptideAtlas; Q8BJW6; -.
DR PRIDE; Q8BJW6; -.
DR ProteomicsDB; 275518; -. [Q8BJW6-1]
DR ProteomicsDB; 275519; -. [Q8BJW6-2]
DR Antibodypedia; 33590; 348 antibodies from 35 providers.
DR Ensembl; ENSMUST00000029387; ENSMUSP00000029387; ENSMUSG00000027810. [Q8BJW6-1]
DR GeneID; 229317; -.
DR KEGG; mmu:229317; -.
DR UCSC; uc008phu.2; mouse. [Q8BJW6-1]
DR UCSC; uc008phv.2; mouse. [Q8BJW6-2]
DR CTD; 83939; -.
DR MGI; MGI:1098684; Eif2a.
DR VEuPathDB; HostDB:ENSMUSG00000027810; -.
DR eggNOG; KOG2315; Eukaryota.
DR GeneTree; ENSGT00730000111053; -.
DR HOGENOM; CLU_013809_1_0_1; -.
DR InParanoid; Q8BJW6; -.
DR OMA; LITWQRP; -.
DR OrthoDB; 464990at2759; -.
DR PhylomeDB; Q8BJW6; -.
DR TreeFam; TF105866; -.
DR BioGRID-ORCS; 229317; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Eif2a; mouse.
DR PRO; PR:Q8BJW6; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8BJW6; protein.
DR Bgee; ENSMUSG00000027810; Expressed in undifferentiated genital tubercle and 249 other tissues.
DR ExpressionAtlas; Q8BJW6; baseline and differential.
DR Genevisible; Q8BJW6; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0005850; C:eukaryotic translation initiation factor 2 complex; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; ISS:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; TAS:MGI.
DR GO; GO:0009967; P:positive regulation of signal transduction; IDA:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0006417; P:regulation of translation; ISS:UniProtKB.
DR GO; GO:1990928; P:response to amino acid starvation; ISO:MGI.
DR GO; GO:0042255; P:ribosome assembly; ISS:UniProtKB.
DR GO; GO:0032933; P:SREBP signaling pathway; IDA:MGI.
DR GO; GO:0006412; P:translation; IDA:MGI.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR011387; TIF2A.
DR InterPro; IPR013979; TIF_beta_prop-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13227; PTHR13227; 1.
DR Pfam; PF08662; eIF2A; 1.
DR PIRSF; PIRSF017222; eIF2A; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Initiation factor;
KW Phosphoprotein; Protein biosynthesis; Reference proteome; Repeat;
KW Translation regulation; WD repeat.
FT CHAIN 1..581
FT /note="Eukaryotic translation initiation factor 2A"
FT /id="PRO_0000424467"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9BY44"
FT CHAIN 2..581
FT /note="Eukaryotic translation initiation factor 2A, N-
FT terminally processed"
FT /id="PRO_0000286077"
FT REPEAT 23..63
FT /note="WD 1"
FT REPEAT 125..163
FT /note="WD 2"
FT REPEAT 356..401
FT /note="WD 3"
FT REGION 432..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 527..578
FT /evidence="ECO:0000255"
FT COMPBIAS 457..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9BY44"
FT MOD_RES 2
FT /note="N-acetylalanine; in Eukaryotic translation
FT initiation factor 2A, N-terminally processed"
FT /evidence="ECO:0000250|UniProtKB:Q9BY44"
FT MOD_RES 5
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BY44"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BY44"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BY44"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BY44"
FT VAR_SEQ 1..94
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024977"
FT VAR_SEQ 95..97
FT /note="PYT -> MEK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024978"
SQ SEQUENCE 581 AA; 64403 MW; D485C05ACE5D0908 CRC64;
MAPSTPLLTV RGSEGLYMVN GPPHFTESTV LPRESGRNCK VYTFSKDGTL FAWSNGEKVN
IINVANKGLL HSFDLPKAVC LEFSPNNTVL ATWQPYTTSK DGTAGTPNLQ LYDMKTGACL
KSFIQKKMQN WCPSWSDDEI ICARNVNNEV HFFENNNFNT IANKLHLQKV NDFNLSPGTQ
PYKVAVYVPG SKGAPSFVRL YQYPNFAGPQ AALANKSFFK ADKVTMLWNK KATAVLVIAS
TEVDKTGASY YGEQTLHYIA TNGESAVVQL PKNGPIYDVV WNSSSTEFCA VYGFMPAKAT
VFNLKCDPVF DFGTGPRNAA FYSPHGHILV LAGFGNLRGQ MEVWDVKNYK LISKPVASDS
TYFAWCPDGE HILTATCAPR LRVNNGYKIW HYTGSLLHKY DVPSNGELWQ VSWQPFLDGI
FPAKTIKYQA VPSEVPSEEP KVATAYRPPA LRNKPVTNSK LHEEEPPQNM KPHPGSDKPL
SKTALKNQRK HEAKKAAKQE ARSDAAPTPV PQSAPRNTVT QSASGDPEVD KKIKNLKKKL
KAIEQLKEQA AAGKQLEKNQ LEKIQKETAL LQELEDLELG V
