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EIF1A_BOVIN
ID   EIF1A_BOVIN             Reviewed;         166 AA.
AC   Q58CY2; Q0VCL0; Q27HF3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Probable RNA-binding protein EIF1AD;
DE   AltName: Full=Eukaryotic translation initiation factor 1A domain-containing protein;
GN   Name=EIF1AD;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal pons;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-166.
RA   Heaton M.P., Clawson M.L., Snelling W.M., Keele J.W., Harhay G.P.,
RA   Wiedmann R.T., Bennett G.L., Smith T.P.L., Freking B.A., Van Tassell C.P.,
RA   Sonstegard T.S., Gasbarre L.C., Moore S.S., Murdoch B., McKay S.D.,
RA   Kalbfleisch T., Laegreid W.W.;
RT   "Estimating probability of parentage in U.S. beef and dairy cattle with
RT   single nucleotide polymorphisms.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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; BT021815; AAX46662.1; -; mRNA.
DR   EMBL; BC120113; AAI20114.1; -; mRNA.
DR   EMBL; DQ404153; ABD57202.1; -; Genomic_DNA.
DR   RefSeq; NP_001069861.1; NM_001076393.1.
DR   AlphaFoldDB; Q58CY2; -.
DR   SMR; Q58CY2; -.
DR   STRING; 9913.ENSBTAP00000026889; -.
DR   PaxDb; Q58CY2; -.
DR   PRIDE; Q58CY2; -.
DR   Ensembl; ENSBTAT00000026889; ENSBTAP00000026889; ENSBTAG00000020186.
DR   GeneID; 615726; -.
DR   KEGG; bta:615726; -.
DR   CTD; 84285; -.
DR   VEuPathDB; HostDB:ENSBTAG00000020186; -.
DR   VGNC; VGNC:28377; EIF1AD.
DR   eggNOG; KOG2925; Eukaryota.
DR   GeneTree; ENSGT00390000011180; -.
DR   HOGENOM; CLU_106477_2_1_1; -.
DR   InParanoid; Q58CY2; -.
DR   OMA; YLVSMPR; -.
DR   OrthoDB; 1431625at2759; -.
DR   TreeFam; TF314439; -.
DR   Proteomes; UP000009136; Chromosome 29.
DR   Bgee; ENSBTAG00000020186; Expressed in oocyte and 103 other tissues.
DR   ExpressionAtlas; Q58CY2; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0031090; C:organelle membrane; IEA:UniProt.
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   2: Evidence at transcript level;
KW   Nucleus; Phosphoprotein; Reference proteome; RNA-binding.
FT   CHAIN           1..166
FT                   /note="Probable RNA-binding protein EIF1AD"
FT                   /id="PRO_0000314150"
FT   DOMAIN          5..89
FT                   /note="S1-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00181"
FT   REGION          99..166
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   MOD_RES         33
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N9N8"
FT   MOD_RES         132
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3THJ3"
FT   MOD_RES         136
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5RKI6"
FT   MOD_RES         137
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3THJ3"
FT   MOD_RES         138
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5RKI6"
FT   MOD_RES         156
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N9N8"
FT   MOD_RES         160
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N9N8"
FT   CONFLICT        28
FT                   /note="V -> M (in Ref. 2; AAI20114)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        125
FT                   /note="L -> F (in Ref. 2; AAI20114)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   166 AA;  19143 MW;  0265B3786D5594AB CRC64;
     MSQATKRKHV VKEVLGEHMV PSDQQQIVRV LRTPGNNLHE VETAQGQRFL VSMPSKYRKN
     IWIKRGDFLI VDPIEEGEKV KAEISFVLCK DHVRSLQKDG HWPEAFSQVT EKDNNDRNRQ
     TQPELPAEPQ SSGEESSSED DSDLFVNTNR RQYHESEEES EEEEAA
 
 
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