ID   EIF1A_RAT               Reviewed;         167 AA.
AC   Q5RKI6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Probable RNA-binding protein EIF1AD;
DE   AltName: Full=Eukaryotic translation initiation factor 1A domain-containing protein;
GN   Name=Eif1ad;
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=Lung;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135 AND SER-137, AND
RP   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: Plays a role into cellular response to oxidative stress.
CC       Decreases cell proliferation (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with GAPDH and STAT1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the EIF1AD family. {ECO:0000305}.
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DR   EMBL; BC085818; AAH85818.1; -; mRNA.
DR   RefSeq; NP_001008306.1; NM_001008305.1.
DR   AlphaFoldDB; Q5RKI6; -.
DR   SMR; Q5RKI6; -.
DR   STRING; 10116.ENSRNOP00000027752; -.
DR   iPTMnet; Q5RKI6; -.
DR   PhosphoSitePlus; Q5RKI6; -.
DR   jPOST; Q5RKI6; -.
DR   PaxDb; Q5RKI6; -.
DR   Ensembl; ENSRNOT00000027753; ENSRNOP00000027752; ENSRNOG00000020463.
DR   GeneID; 293673; -.
DR   KEGG; rno:293673; -.
DR   CTD; 84285; -.
DR   RGD; 1304686; Eif1ad.
DR   eggNOG; KOG2925; Eukaryota.
DR   GeneTree; ENSGT00390000011180; -.
DR   HOGENOM; CLU_106477_2_1_1; -.
DR   InParanoid; Q5RKI6; -.
DR   OMA; YLVSMPR; -.
DR   OrthoDB; 1431625at2759; -.
DR   PhylomeDB; Q5RKI6; -.
DR   TreeFam; TF314439; -.
DR   PRO; PR:Q5RKI6; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000020463; Expressed in pancreas and 20 other tissues.
DR   Genevisible; Q5RKI6; RN.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:InterPro.
DR   Gene3D; 2.40.50.140; -; 1.
DR   InterPro; IPR039294; EIF1AD.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR006196; RNA-binding_domain_S1_IF1.
DR   InterPro; IPR001253; TIF_eIF-1A.
DR   PANTHER; PTHR21641; PTHR21641; 1.
DR   Pfam; PF01176; eIF-1a; 1.
DR   SMART; SM00652; eIF1a; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   PROSITE; PS50832; S1_IF1_TYPE; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Phosphoprotein; Reference proteome; RNA-binding.
FT   CHAIN           1..167
FT                   /note="Probable RNA-binding protein EIF1AD"
FT                   /id="PRO_0000314155"
FT   DOMAIN          5..89
FT                   /note="S1-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00181"
FT   REGION          104..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           6..12
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           56..65
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        110..124
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         33
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N9N8"
FT   MOD_RES         131
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3THJ3"
FT   MOD_RES         135
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         137
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         155
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N9N8"
FT   MOD_RES         159
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N9N8"
SQ   SEQUENCE   167 AA;  19076 MW;  855E53D9A5D4D8D1 CRC64;
     MSQASKRKHV VQEVLGEHMV PSDQQQIVKV LRTPGNNLHE VETAQGQRFL VSMPSKYRKN
     IWIKRGDFLI VDPIEEGEKV KAEISFVLCK NHVRSLQKEG HWPEAFSEVA EKQNNVNRES
     QPELPAEPQL SGEGSGSEDD SDLFVNTNHR QYHESEEESE EEEEEAA