ID EIF1_CHICK Reviewed; 113 AA.
AC P51971;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2023, sequence version 2.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=Eukaryotic translation initiation factor 1;
DE Short=eIF1;
DE AltName: Full=Protein translation factor SUI1 homolog;
GN Name=EIF1; Synonyms=SUI1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7607213; DOI=10.1111/j.1432-1033.1995.tb20580.x;
RA Wu S.V., Dimaline R., Walsh J.H., Campbell B.J.;
RT "Molecular characterization and physiological regulation of a TATA-less
RT gene encoding chicken gastrin.";
RL Eur. J. Biochem. 230:439-446(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [3]
RP IDENTIFICATION.
RA Duret L.;
RL Unpublished observations (JUL-1996).
CC -!- FUNCTION: Component of the 43S pre-initiation complex (43S PIC), which
CC binds to the mRNA cap-proximal region, scans mRNA 5'-untranslated
CC region, and locates the initiation codon. Together with eIF1A (EIF1AX),
CC EIF1 facilitates scanning and is essential for start codon recognition
CC on the basis of AUG nucleotide context and location relative to the 5'-
CC cap. Participates to initiation codon selection by influencing the
CC conformation of the 40S ribosomal subunit and the positions of bound
CC mRNA and initiator tRNA; this is possible after its binding to the
CC interface surface of the platform of the 40S ribosomal subunit close to
CC the P-site. Together with eIF1A (EIF1AX), also regulates the opening
CC and closing of the mRNA binding channel, which ensures mRNA
CC recruitment, scanning and the fidelity of initiation codon selection.
CC Continuously monitors and protects against premature and partial base-
CC pairing of codons in the 5'-UTR with the anticodon of initiator tRNA.
CC Together with eIF1A (EIF1AX), acts for ribosomal scanning, promotion of
CC the assembly of 48S complex at the initiation codon (43S PIC becomes
CC 48S PIC after the start codon is reached), and dissociation of aberrant
CC complexes. Interacts with EIF4G1, which in a mutual exclusive
CC interaction associates either with EIF1 or with EIF4E on a common
CC binding site. EIF4G1-EIF1 complex promotes ribosome scanning (on both
CC short and long 5'UTR), leaky scanning (on short 5'UTR) which is the
CC bypass of the initial start codon, and discrimination against cap-
CC proximal AUG. Is probably maintained within the 43S PIC in open
CC conformation thanks to eIF1A-EIF5 interaction. Once the correct start
CC codon is reached, EIF1 is physically excluded from the decoding site,
CC shifting the PIC into the closed conformation and arresting it at the
CC start codon. {ECO:0000250|UniProtKB:P41567}.
CC -!- SUBUNIT: Component of the 43S pre-initiation complex (43S PIC), which
CC is composed of the 40S ribosomal subunit, EIF1, eIF1A (EIF1AX), eIF3
CC complex, EIF5 and eIF2-GTP-initiator tRNA complex (eIF2 ternary
CC complex). Interacts with EIF4G1; in specific 5'-UTR length and AUG
CC context. Interacts with EIF5; which in a mutual exclusive interaction
CC associates either with EIF1 or with EIF2S2 on a common binding site.
CC Interacts with RENT2. {ECO:0000250|UniProtKB:P41567}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P41567}.
CC -!- SIMILARITY: Belongs to the SUI1 family. {ECO:0000305}.
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DR EMBL; U25125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN05000735; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001161207.1; NM_001167735.1.
DR AlphaFoldDB; P51971; -.
DR BMRB; P51971; -.
DR SMR; P51971; -.
DR STRING; 9031.ENSGALP00000045582; -.
DR PaxDb; 9031-ENSGALP00000043024; -.
DR GeneID; 420037; -.
DR KEGG; gga:420037; -.
DR CTD; 10209; -.
DR VEuPathDB; HostDB:geneid_420037; -.
DR eggNOG; KOG1770; Eukaryota.
DR HOGENOM; CLU_082805_3_1_1; -.
DR InParanoid; P51971; -.
DR OMA; VENHIHI; -.
DR PhylomeDB; P51971; -.
DR Proteomes; UP000000539; Unassembled WGS sequence.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IBA:GO_Central.
DR GO; GO:0043024; F:ribosomal small subunit binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR CDD; cd11566; eIF1_SUI1; 1.
DR Gene3D; 3.30.780.10; SUI1-like domain; 1.
DR InterPro; IPR001950; SUI1.
DR InterPro; IPR036877; SUI1_dom_sf.
DR InterPro; IPR005874; SUI1_euk.
DR NCBIfam; TIGR01160; SUI1_MOF2; 1.
DR PANTHER; PTHR10388:SF10; EUKARYOTIC TRANSLATION INITIATION FACTOR 1; 1.
DR PANTHER; PTHR10388; EUKARYOTIC TRANSLATION INITIATION FACTOR SUI1; 1.
DR Pfam; PF01253; SUI1; 1.
DR PIRSF; PIRSF004499; SUI1_euk; 1.
DR SUPFAM; SSF55159; eIF1-like; 1.
DR PROSITE; PS50296; SUI1; 1.
PE 3: Inferred from homology;
KW Acetylation; Cytoplasm; Initiation factor; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P41567"
FT CHAIN 2..113
FT /note="Eukaryotic translation initiation factor 1"
FT /id="PRO_0000130557"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 41
FT /note="Binds 40S ribosomal subunit"
FT /evidence="ECO:0000250|UniProtKB:P41567"
FT SITE 65
FT /note="Binds 40S ribosomal subunit"
FT /evidence="ECO:0000250|UniProtKB:P41567"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P41567"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41567"
SQ SEQUENCE 113 AA; 12734 MW; 2CA2929B53FFE8C2 CRC64;
MSAIQNLQPF DPFADASKGD DLLPAGTEDY IHIRIQQRNG RKTLTTVQGI ADDYDKKKLV
KAFKKKFACN GTVIEHPEYG EVIQLQGDQR KNICQFLVEI GLAKDDQLKV HGF
//
