ID   IF5_PONAB               Reviewed;         431 AA.
AC   Q5R4L0;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Eukaryotic translation initiation factor 5;
DE            Short=eIF-5;
GN   Name=EIF5;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the hydrolysis of GTP bound to the 40S ribosomal
CC       initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent
CC       joining of a 60S ribosomal subunit resulting in the release of eIF-2
CC       and the guanine nucleotide. The subsequent joining of a 60S ribosomal
CC       subunit results in the formation of a functional 80S initiation complex
CC       (80S.mRNA.Met-tRNA[F]) (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with FMR1; this interaction occurs in a RNA-
CC       dependent manner (By similarity). Interacts with EIF2S2 (By
CC       similarity). {ECO:0000250|UniProtKB:P55010}.
CC   -!- SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR861236; CAH93306.1; -; mRNA.
DR   RefSeq; NP_001126945.1; NM_001133473.1.
DR   RefSeq; XP_009247808.1; XM_009249533.1.
DR   AlphaFoldDB; Q5R4L0; -.
DR   BMRB; Q5R4L0; -.
DR   SMR; Q5R4L0; -.
DR   STRING; 9601.ENSPPYP00000024413; -.
DR   PRIDE; Q5R4L0; -.
DR   Ensembl; ENSPPYT00000007289; ENSPPYP00000007010; ENSPPYG00000006169.
DR   GeneID; 100173963; -.
DR   KEGG; pon:100173963; -.
DR   CTD; 1983; -.
DR   eggNOG; KOG2767; Eukaryota.
DR   GeneTree; ENSGT00390000016478; -.
DR   HOGENOM; CLU_026663_1_0_1; -.
DR   InParanoid; Q5R4L0; -.
DR   OMA; YRYKMEK; -.
DR   OrthoDB; 979826at2759; -.
DR   TreeFam; TF101533; -.
DR   Proteomes; UP000001595; Chromosome 14.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006446; P:regulation of translational initiation; IEA:Ensembl.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR045196; IF2/IF5.
DR   InterPro; IPR002735; Transl_init_fac_IF2/IF5_dom.
DR   InterPro; IPR016189; Transl_init_fac_IF2/IF5_N.
DR   InterPro; IPR016190; Transl_init_fac_IF2/IF5_Zn-bd.
DR   InterPro; IPR003307; W2_domain.
DR   PANTHER; PTHR23001; PTHR23001; 1.
DR   Pfam; PF01873; eIF-5_eIF-2B; 1.
DR   Pfam; PF02020; W2; 1.
DR   SMART; SM00653; eIF2B_5; 1.
DR   SMART; SM00515; eIF5C; 1.
DR   SUPFAM; SSF100966; SSF100966; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF75689; SSF75689; 1.
DR   PROSITE; PS51363; W2; 1.
PE   2: Evidence at transcript level;
KW   GTP-binding; Initiation factor; Isopeptide bond; Nucleotide-binding;
KW   Phosphoprotein; Protein biosynthesis; Reference proteome; Ubl conjugation.
FT   CHAIN           1..431
FT                   /note="Eukaryotic translation initiation factor 5"
FT                   /id="PRO_0000259422"
FT   DOMAIN          233..392
FT                   /note="W2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00695"
FT   REGION          143..216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..171
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..191
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         10
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P55010"
FT   MOD_RES         227
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P55010"
FT   MOD_RES         229
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P55010"
FT   MOD_RES         389
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P55010"
FT   MOD_RES         390
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P55010"
FT   MOD_RES         410
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P55010"
FT   MOD_RES         419
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P55010"
FT   CROSSLNK        413
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P55010"
FT   CROSSLNK        418
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P55010"
SQ   SEQUENCE   431 AA;  49212 MW;  9789C6C01D7638CC CRC64;
     MSVNVNRSVS DQFYRYKMPR LIAKVEGKGN GIKTVIVNMV DVAKALNRPP TYPTKYFGCE
     LGAQTQFDVK NDRYIVNGSH EANKLQDMLD GFIKKFVLCP ECENPETDLH VNPKKQTIGN
     SCKACGYRGM LDTHHKLCTF ILKNPPENSD SGTGKKEKEK KNRKGKDKEN GSVSSSETPP
     PPPPPNEISP PPHTMEEEED DDWGEDTTEE AQRRRMDEIS DHAKVLTLSD DLERTIEERV
     NILFDFVKKK KEEGVIDSSD KEIVAEAERL DVKAMGPLVL TEVLFNEKIR EQIKKYRRHF
     LRFCHNNKKA QRYLLHGLEC VVAMHQAQLI SKIPHILKEM YDADLLEEEV IISWSEKASK
     KYVSKELAKE IRVKAEPFIK WLKEAEEESS GGEEDDEDEN IEVVYSKTAS VPKVETVKSD
     NKDDDIDIDA I