IF1AX_HUMAN
ID IF1AX_HUMAN Reviewed; 144 AA.
AC P47813; B2R5U5; Q0VGC2; Q5JPS5; Q5JPS6;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Eukaryotic translation initiation factor 1A, X-chromosomal;
DE Short=eIF-1A X isoform;
DE AltName: Full=Eukaryotic translation initiation factor 4C;
DE Short=eIF-4C;
GN Name=EIF1AX; Synonyms=EIF1A, EIF4C;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8106356; DOI=10.1016/s0021-9258(17)41850-3;
RA Dever T.E., Wei C.-L., Benkowski L.A., Browning K., Merrick W.C.,
RA Hershey J.W.B.;
RT "Determination of the amino acid sequence of rabbit, human, and wheat germ
RT protein synthesis factor eIF-4C by cloning and chemical sequencing.";
RL J. Biol. Chem. 269:3212-3218(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hypothalamus, and Placenta;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP INTERACTION WITH HRSV NUCLEOPROTEIN (MICROBIAL INFECTION).
RX PubMed=25479059; DOI=10.1371/journal.pone.0114447;
RA Wei T., Li D., Marcial D., Khan M., Lin M.H., Snape N., Ghildyal R.,
RA Harrich D., Spann K.;
RT "The eukaryotic elongation factor 1A is critical for genome replication of
RT the paramyxovirus respiratory syncytial virus.";
RL PLoS ONE 9:e114447-e114447(2014).
RN [8]
RP STRUCTURE BY NMR.
RX PubMed=10678173; DOI=10.1016/s1097-2765(00)80407-4;
RA Battiste J.L., Pestova T.V., Hellen C.U., Wagner G.;
RT "The eIF1A solution structure reveals a large RNA-binding surface important
RT for scanning function.";
RL Mol. Cell 5:109-119(2000).
CC -!- FUNCTION: Seems to be required for maximal rate of protein
CC biosynthesis. Enhances ribosome dissociation into subunits and
CC stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal
CC subunits.
CC -!- SUBUNIT: (Microbial infection) Interacts with human respiratory
CC syncytial virus (HRSV) nucleoprotein; this interaction recruits EIF1AX
CC to the viral replication complex to facilitate viral genomic RNA
CC synthesis and virus production. {ECO:0000269|PubMed:25479059}.
CC -!- INTERACTION:
CC P47813; Q14152: EIF3A; NbExp=2; IntAct=EBI-1045377, EBI-366617;
CC P47813; Q99613: EIF3C; NbExp=2; IntAct=EBI-1045377, EBI-353741;
CC P47813; O94829: IPO13; NbExp=14; IntAct=EBI-1045377, EBI-747310;
CC P47813; O75679: RFPL3; NbExp=3; IntAct=EBI-1045377, EBI-10188956;
CC -!- SIMILARITY: Belongs to the eIF-1A family. {ECO:0000305}.
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DR EMBL; L18960; AAA19812.1; -; mRNA.
DR EMBL; AK312320; BAG35242.1; -; mRNA.
DR EMBL; BT007064; AAP35727.1; -; mRNA.
DR EMBL; AL732366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000793; AAH00793.1; -; mRNA.
DR EMBL; BC067851; AAH67851.1; -; mRNA.
DR CCDS; CCDS14196.1; -.
DR PIR; C53045; C53045.
DR RefSeq; NP_001403.1; NM_001412.3.
DR RefSeq; XP_016855198.1; XM_016999709.1.
DR PDB; 1D7Q; NMR; -; A=2-144.
DR PDB; 3ZJY; X-ray; 3.60 A; C=1-112.
DR PDB; 4KZY; X-ray; 7.01 A; n=1-144.
DR PDB; 4KZZ; X-ray; 7.03 A; n=1-144.
DR PDB; 6YBW; EM; 3.10 A; q=1-144.
DR PDB; 6ZMW; EM; 3.70 A; q=1-144.
DR PDB; 6ZP4; EM; 2.90 A; G=1-144.
DR PDB; 7A09; EM; 3.50 A; G=1-112.
DR PDBsum; 1D7Q; -.
DR PDBsum; 3ZJY; -.
DR PDBsum; 4KZY; -.
DR PDBsum; 4KZZ; -.
DR PDBsum; 6YBW; -.
DR PDBsum; 6ZMW; -.
DR PDBsum; 6ZP4; -.
DR PDBsum; 7A09; -.
DR AlphaFoldDB; P47813; -.
DR BMRB; P47813; -.
DR SMR; P47813; -.
DR BioGRID; 108284; 115.
DR CORUM; P47813; -.
DR DIP; DIP-40995N; -.
DR IntAct; P47813; 26.
DR MINT; P47813; -.
DR STRING; 9606.ENSP00000368927; -.
DR GlyGen; P47813; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P47813; -.
DR MetOSite; P47813; -.
DR PhosphoSitePlus; P47813; -.
DR SwissPalm; P47813; -.
DR BioMuta; EIF1AX; -.
DR DMDM; 1352425; -.
DR EPD; P47813; -.
DR jPOST; P47813; -.
DR MassIVE; P47813; -.
DR MaxQB; P47813; -.
DR PaxDb; P47813; -.
DR PeptideAtlas; P47813; -.
DR PRIDE; P47813; -.
DR ProteomicsDB; 55799; -.
DR TopDownProteomics; P47813; -.
DR Antibodypedia; 9819; 102 antibodies from 24 providers.
DR DNASU; 1964; -.
DR Ensembl; ENST00000379607.10; ENSP00000368927.5; ENSG00000173674.11.
DR GeneID; 1964; -.
DR KEGG; hsa:1964; -.
DR MANE-Select; ENST00000379607.10; ENSP00000368927.5; NM_001412.4; NP_001403.1.
DR UCSC; uc004czt.4; human.
DR CTD; 1964; -.
DR DisGeNET; 1964; -.
DR GeneCards; EIF1AX; -.
DR HGNC; HGNC:3250; EIF1AX.
DR HPA; ENSG00000173674; Low tissue specificity.
DR MalaCards; EIF1AX; -.
DR MIM; 300186; gene.
DR neXtProt; NX_P47813; -.
DR OpenTargets; ENSG00000173674; -.
DR Orphanet; 146; Differentiated thyroid carcinoma.
DR PharmGKB; PA27684; -.
DR VEuPathDB; HostDB:ENSG00000173674; -.
DR eggNOG; KOG3403; Eukaryota.
DR GeneTree; ENSGT00390000008256; -.
DR HOGENOM; CLU_109098_0_1_1; -.
DR InParanoid; P47813; -.
DR OMA; KMEDQEY; -.
DR OrthoDB; 1426335at2759; -.
DR PhylomeDB; P47813; -.
DR TreeFam; TF350394; -.
DR PathwayCommons; P47813; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-72649; Translation initiation complex formation.
DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR SignaLink; P47813; -.
DR BioGRID-ORCS; 1964; 398 hits in 651 CRISPR screens.
DR ChiTaRS; EIF1AX; human.
DR EvolutionaryTrace; P47813; -.
DR GeneWiki; EIF1AX; -.
DR Pharos; P47813; Tbio.
DR PRO; PR:P47813; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P47813; protein.
DR Bgee; ENSG00000173674; Expressed in endothelial cell and 206 other tissues.
DR ExpressionAtlas; P47813; baseline and differential.
DR Genevisible; P47813; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0008135; F:translation factor activity, RNA binding; TAS:ProtInc.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR CDD; cd05793; S1_IF1A; 1.
DR DisProt; DP00903; -.
DR Gene3D; 2.40.50.140; -; 1.
DR HAMAP; MF_00216; aIF_1A; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR006196; RNA-binding_domain_S1_IF1.
DR InterPro; IPR001253; TIF_eIF-1A.
DR InterPro; IPR018104; TIF_eIF-1A_CS.
DR PANTHER; PTHR21668; PTHR21668; 1.
DR Pfam; PF01176; eIF-1a; 1.
DR SMART; SM00652; eIF1a; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00523; eIF-1A; 1.
DR PROSITE; PS01262; IF1A; 1.
DR PROSITE; PS50832; S1_IF1_TYPE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Host-virus interaction; Initiation factor;
KW Protein biosynthesis; Reference proteome; RNA-binding.
FT CHAIN 1..144
FT /note="Eukaryotic translation initiation factor 1A, X-
FT chromosomal"
FT /id="PRO_0000145101"
FT DOMAIN 22..96
FT /note="S1-like"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..144
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:1D7Q"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:6YBW"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:6YBW"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:6YBW"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:6YBW"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:6YBW"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:6YBW"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:6YBW"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:6YBW"
FT HELIX 97..101
FT /evidence="ECO:0007829|PDB:6YBW"
FT TURN 102..106
FT /evidence="ECO:0007829|PDB:6YBW"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:1D7Q"
SQ SEQUENCE 144 AA; 16460 MW; 1C4209855B21BFD4 CRC64;
MPKNKGKGGK NRRRGKNENE SEKRELVFKE DGQEYAQVIK MLGNGRLEAM CFDGVKRLCH
IRGKLRKKVW INTSDIILVG LRDYQDNKAD VILKYNADEA RSLKAYGELP EHAKINETDT
FGPGDDDEIQ FDDIGDDDED IDDI
