IF2P_RAT
ID IF2P_RAT Reviewed; 1216 AA.
AC B2GUV7; A0JN31; P70488;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Eukaryotic translation initiation factor 5B;
DE Short=eIF-5B;
DE EC=3.6.5.3;
DE AltName: Full=Annexin V-binding protein ABP-7;
DE AltName: Full=Translation initiation factor IF-2;
GN Name=Eif5b; Synonyms=If2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo, Liver, and Lung;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 101-334, AND INTERACTION WITH ANXA5.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=8667030; DOI=10.1046/j.1471-4159.1996.67010089.x;
RA Ohsawa K., Imai Y., Ito D., Kohsaka S.;
RT "Molecular cloning and characterization of annexin V-binding proteins with
RT highly hydrophilic peptide structure.";
RL J. Neurochem. 67:89-97(1996).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544; SER-553 AND SER-556, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Plays a role in translation initiation. Translational GTPase
CC that catalyzes the joining of the 40S and 60S subunits to form the 80S
CC initiation complex with the initiator methionine-tRNA in the P-site
CC base paired to the start codon. GTP binding and hydrolysis induces
CC conformational changes in the enzyme that renders it active for
CC productive interactions with the ribosome. The release of the enzyme
CC after formation of the initiation complex is a prerequisite to form
CC elongation-competent ribosomes. {ECO:0000250|UniProtKB:P39730}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.3;
CC Evidence={ECO:0000250|UniProtKB:P39730};
CC -!- COFACTOR:
CC Name=a monovalent cation; Xref=ChEBI:CHEBI:60242;
CC Evidence={ECO:0000250|UniProtKB:G0S8G9};
CC Note=Binds 1 monovalent cation per monomer in the active site.
CC Structural cofactor that stabilizes the GTP-bound 'on' state. May also
CC act as a transition state stabilizer of the hydrolysis reaction.
CC {ECO:0000250|UniProtKB:G0S8G9};
CC -!- SUBUNIT: Interacts with ANXA5 in a calcium and phospholipid-dependent
CC manner. {ECO:0000269|PubMed:8667030}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q05D44}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI26103.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAI67065.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; BC126102; AAI26103.1; ALT_SEQ; mRNA.
DR EMBL; BC166424; AAI66424.1; -; mRNA.
DR EMBL; BC167065; AAI67065.1; ALT_SEQ; mRNA.
DR EMBL; D64061; BAA10937.1; -; mRNA.
DR RefSeq; NP_001103611.1; NM_001110141.1.
DR AlphaFoldDB; B2GUV7; -.
DR SMR; B2GUV7; -.
DR BioGRID; 258950; 1.
DR IntAct; B2GUV7; 4.
DR STRING; 10116.ENSRNOP00000065578; -.
DR iPTMnet; B2GUV7; -.
DR PhosphoSitePlus; B2GUV7; -.
DR jPOST; B2GUV7; -.
DR PaxDb; B2GUV7; -.
DR PeptideAtlas; B2GUV7; -.
DR PRIDE; B2GUV7; -.
DR Ensembl; ENSRNOT00000114110; ENSRNOP00000079088; ENSRNOG00000023356.
DR GeneID; 308306; -.
DR KEGG; rno:308306; -.
DR CTD; 9669; -.
DR RGD; 735017; Eif5b.
DR eggNOG; KOG1144; Eukaryota.
DR GeneTree; ENSGT00940000162583; -.
DR HOGENOM; CLU_002656_0_1_1; -.
DR InParanoid; B2GUV7; -.
DR OrthoDB; 1124591at2759; -.
DR PhylomeDB; B2GUV7; -.
DR TreeFam; TF101535; -.
DR Reactome; R-RNO-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR PRO; PR:B2GUV7; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Genevisible; B2GUV7; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; ISO:RGD.
DR GO; GO:0006446; P:regulation of translational initiation; ISO:RGD.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR Gene3D; 3.40.50.10050; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR015760; TIF_IF2.
DR InterPro; IPR023115; TIF_IF2_dom3.
DR InterPro; IPR036925; TIF_IF2_dom3_sf.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR43381; PTHR43381; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52156; SSF52156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTP-binding; Hydrolase; Initiation factor; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..1216
FT /note="Eukaryotic translation initiation factor 5B"
FT /id="PRO_0000354073"
FT DOMAIN 625..842
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 1..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..641
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 659..663
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 698..701
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 752..755
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 820..822
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..506
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..564
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..604
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 634..641
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 107
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q05D44"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05D44"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 497
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 553
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 584
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 1164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT CONFLICT 393
FT /note="E -> K (in Ref. 1; AAI26103/AAI67065)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1216 AA; 137686 MW; 515ACABDF33C3D00 CRC64;
MGKKQKNKSE DSTKDDTDLG ALAAEIEGAG AAKEQEPQKG KGKKKKEKKK QDFDENDILR
ELEELSLEAQ GIGADRDAAT VKPTENNEEE SASKQDKKKK GQKGKKTSFD ENDSEELEDK
DSKSKKPARP NSEVLLSGSE DADDPNKLSK KGKKAQKSTK KRDGSEEDED NSKRSKERSR
VNSSGESGGE SDEFLQSRKG QKKNQKNKSV PTIDSGNEDD DSSFKIKTVA QKKAEKKERE
RKKREEEKAK LRKVKEKEEL EKGRKEQSKQ REPQKRPDEE VLVLRGTPDA GAASEEKGDI
AATLEDDNEG DKKKKDKKKK KTEKDDKEKE KKKGPSKSTV KAIQEALAKL REEEERQKRE
EEERIKRLEE LEAKRKEEER LEQEKRERKK QKEKERKERL KKEGKLLTKS QREARARAEV
TLRHLQAQGV EVPSKDSLPK KRPVYEDKKK KKTPQQLESK EALETVEVSA PVEVVDQGVP
EKEETPPSVD AEEDEETEDA GLDDWEAMAS DEEREKEGNM IHIEVEENPE EEEEEEEDED
EEDSEDEEDE GDSEGSDGDE EDYKLSDEKD LGKAGDTKPN KDASSDSEYD SDDDRTKEER
AYDKAKRRIE KRRLEHGKNV NTEKLRAPII CVLGHVDTGK TKILDKLRHT HVQDGEAGGI
TQQIGATNVP LEAINEQTKM IKNFDRENVR IPGMLIIDTP GHESFSNLRN RGSSLCDIAI
LVVDIMHGLE PQTIESINIL KSKKCPFIVA LNKIDRLYDW KKSPDSDVAV TLKKQKKNTK
DEFEERAKAI IVEFAQQGLN AALFYENKDP RTFVSLVPTS AHTGDGMGSL IYLLVELTQT
MLSKRLAHCE ELRAQVMEVK ALPGMGTTID VILINGRLKE GDTIIVPGVE GPIVTQIRGL
LLPPPMKELR VKNQYEKHKE VEAAQGVKIL GKDLEKTLAG LPLLVAYKDD EIPVLKDELI
HELKQTLNAI KLEEKGVYVQ ASTLGSLEAL LEFLKTSEVP YAGINIGPVH KKDVMKASVM
LEHDPQYAVI LAFDVRIERD AQEMADSLGV RIFSAEIIYH LFDAFTKYRQ DYKKQKQEEF
KHIAVFPCKM KILPQYIFNS RDPIVIGVTV EAGQVKQGTP MCVPSKNFVD IGIVTSIEIN
HKQVDVAKKG QEVCVKIEPI PGESPKMFGR HFEATDILVS KISRQSIDAL KDWFRDEMQK
SDWQLIVELK KVFEII
