IF5AL_HUMAN
ID IF5AL_HUMAN Reviewed; 154 AA.
AC Q6IS14;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Eukaryotic translation initiation factor 5A-1-like;
DE Short=eIF-5A-1-like;
DE Short=eIF-5A1-like;
DE AltName: Full=Eukaryotic initiation factor 5A isoform 1-like;
GN Name=EIF5AL1;
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 [LARGE SCALE MRNA].
RC TISSUE=Testis;
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).
CC -!- FUNCTION: mRNA-binding protein involved in translation elongation. Has
CC an important function at the level of mRNA turnover, probably acting
CC downstream of decapping. Critical for the efficient synthesis of
CC peptide bonds between consecutive proline residues. Can resolve
CC ribosomal stalling caused by consecutive prolines during translation
CC (By similarity). Involved in actin dynamics and cell cycle progression,
CC mRNA decay and probably in a pathway involved in stress response and
CC maintenance of cell wall integrity. Functions as a regulator of
CC apoptosis. Mediates effects of polyamines on neuronal process extension
CC and survival. May play an important role in brain development and
CC function, and in skeletal muscle stem cell differentiation (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:P63241}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear
CC pore complex {ECO:0000250}. Note=Hypusine modification promotes the
CC nuclear export and cytoplasmic localization and there was a dynamic
CC shift in the localization from predominantly cytoplasmic to primarily
CC nuclear under apoptotic inducing conditions. {ECO:0000250}.
CC -!- PTM: Lys-50 undergoes hypusination, a unique post-translational
CC modification that consists in the addition of a butylamino group from
CC spermidine to lysine side chain, leading to the formation of the
CC unusual amino acid hypusine. eIF-5As are the only known proteins to
CC undergo this modification, which is essential for their function.
CC {ECO:0000250|UniProtKB:P63241}.
CC -!- SIMILARITY: Belongs to the eIF-5A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH70048.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC070048; AAH70048.1; ALT_INIT; mRNA.
DR CCDS; CCDS53546.1; -.
DR RefSeq; NP_001093162.1; NM_001099692.1.
DR AlphaFoldDB; Q6IS14; -.
DR SMR; Q6IS14; -.
DR BioGRID; 126793; 15.
DR IntAct; Q6IS14; 6.
DR MINT; Q6IS14; -.
DR STRING; 9606.ENSP00000430706; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR iPTMnet; Q6IS14; -.
DR PhosphoSitePlus; Q6IS14; -.
DR SwissPalm; Q6IS14; -.
DR BioMuta; EIF5AL1; -.
DR DMDM; 190359775; -.
DR jPOST; Q6IS14; -.
DR MassIVE; Q6IS14; -.
DR MaxQB; Q6IS14; -.
DR PaxDb; Q6IS14; -.
DR PeptideAtlas; Q6IS14; -.
DR PRIDE; Q6IS14; -.
DR ProteomicsDB; 66490; -.
DR TopDownProteomics; Q6IS14; -.
DR Antibodypedia; 66911; 61 antibodies from 14 providers.
DR DNASU; 143244; -.
DR Ensembl; ENST00000520547.4; ENSP00000430706.2; ENSG00000253626.4.
DR GeneID; 143244; -.
DR KEGG; hsa:143244; -.
DR MANE-Select; ENST00000520547.4; ENSP00000430706.2; NM_001099692.2; NP_001093162.1.
DR UCSC; uc009xrx.4; human.
DR CTD; 143244; -.
DR DisGeNET; 143244; -.
DR GeneCards; EIF5AL1; -.
DR HGNC; HGNC:17419; EIF5AL1.
DR HPA; ENSG00000253626; Tissue enriched (testis).
DR neXtProt; NX_Q6IS14; -.
DR OpenTargets; ENSG00000253626; -.
DR PharmGKB; PA134920977; -.
DR VEuPathDB; HostDB:ENSG00000253626; -.
DR eggNOG; KOG3271; Eukaryota.
DR GeneTree; ENSGT00390000003738; -.
DR HOGENOM; CLU_102600_0_0_1; -.
DR InParanoid; Q6IS14; -.
DR OMA; HHFESSE; -.
DR OrthoDB; 1370513at2759; -.
DR PhylomeDB; Q6IS14; -.
DR TreeFam; TF101534; -.
DR PathwayCommons; Q6IS14; -.
DR SignaLink; Q6IS14; -.
DR BioGRID-ORCS; 143244; 287 hits in 1009 CRISPR screens.
DR ChiTaRS; EIF5AL1; human.
DR GeneWiki; EIF5AP1; -.
DR GenomeRNAi; 143244; -.
DR Pharos; Q6IS14; Tdark.
DR PRO; PR:Q6IS14; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q6IS14; protein.
DR Bgee; ENSG00000253626; Expressed in testis and 105 other tissues.
DR Genevisible; Q6IS14; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0045901; P:positive regulation of translational elongation; IBA:GO_Central.
DR GO; GO:0045905; P:positive regulation of translational termination; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR001884; IF5A-like.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR019769; Trans_elong_IF5A_hypusine_site.
DR InterPro; IPR020189; Transl_elong_IF5A_C.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR11673; PTHR11673; 1.
DR Pfam; PF01287; eIF-5a; 1.
DR PIRSF; PIRSF003025; eIF5A; 1.
DR SMART; SM01376; eIF-5a; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00037; eIF_5A; 1.
DR PROSITE; PS00302; IF5A_HYPUSINE; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Elongation factor; Endoplasmic reticulum; Hypusine; Membrane;
KW mRNA transport; Nuclear pore complex; Nucleus; Protein biosynthesis;
KW Protein transport; Reference proteome; RNA-binding; Translocation;
KW Transport.
FT CHAIN 1..154
FT /note="Eukaryotic translation initiation factor 5A-1-like"
FT /id="PRO_0000340263"
FT MOD_RES 50
FT /note="Hypusine"
FT /evidence="ECO:0000250|UniProtKB:P63241"
SQ SEQUENCE 154 AA; 16773 MW; 6A0F0426D24980C0 CRC64;
MADDLDFETG DAGASATFPM QCSALRKNGF VVLKGWPCKI VEMSASKTGK HGHAKVHLVG
IDIFTGKKYE DICPSTHNMD VPNIKRNDFQ LIGIQDGYLS LLQDSGEVPE DLRLPEGDLG
KEIEQKYDCG EEILITVLSA MTEEAAVAIK AMAK
