IF2B_PONAB
ID IF2B_PONAB Reviewed; 333 AA.
AC Q5R4T9;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Eukaryotic translation initiation factor 2 subunit 2;
DE AltName: Full=Eukaryotic translation initiation factor 2 subunit beta;
DE Short=eIF-2-beta;
GN Name=EIF2S2;
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: eIF-2 functions in the early steps of protein synthesis by
CC forming a ternary complex with GTP and initiator tRNA. This complex
CC binds to a 40S ribosomal subunit, followed by mRNA binding to form a
CC 43S preinitiation complex. Junction of the 60S ribosomal subunit to
CC form the 80S initiation complex is preceded by hydrolysis of the GTP
CC bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for
CC eIF-2 to recycle and catalyze another round of initiation, the GDP
CC bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by
CC eIF-2B (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma chain.
CC Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR,
CC CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5 (By similarity). Interacts
CC with BZW2/5MP1 and EIF5 (By similarity). {ECO:0000250|UniProtKB:P20042,
CC ECO:0000250|UniProtKB:Q99L45}.
CC -!- SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family. {ECO:0000305}.
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DR EMBL; CR861152; CAH93227.1; -; mRNA.
DR RefSeq; NP_001127646.1; NM_001134174.1.
DR AlphaFoldDB; Q5R4T9; -.
DR SMR; Q5R4T9; -.
DR STRING; 9601.ENSPPYP00000012209; -.
DR GeneID; 100174727; -.
DR KEGG; pon:100174727; -.
DR CTD; 8894; -.
DR eggNOG; KOG2768; Eukaryota.
DR InParanoid; Q5R4T9; -.
DR OrthoDB; 1178655at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
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 PANTHER; PTHR23001; PTHR23001; 1.
DR Pfam; PF01873; eIF-5_eIF-2B; 1.
DR SMART; SM00653; eIF2B_5; 1.
DR SUPFAM; SSF100966; SSF100966; 1.
DR SUPFAM; SSF75689; SSF75689; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Initiation factor; Isopeptide bond; Metal-binding;
KW Phosphoprotein; Protein biosynthesis; Reference proteome; Ubl conjugation;
KW Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P20042"
FT CHAIN 2..333
FT /note="Eukaryotic translation initiation factor 2 subunit
FT 2"
FT /id="PRO_0000290340"
FT ZN_FING 281..305
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 1..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P20042"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20042"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41035"
FT MOD_RES 31
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20042"
FT MOD_RES 36
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20042"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41035"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20042"
FT MOD_RES 111
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20042"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20042"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41035"
FT MOD_RES 265
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P20042"
FT MOD_RES 293
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P20042"
FT CROSSLNK 102
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P20042"
SQ SEQUENCE 333 AA; 38360 MW; 499FD4B48AA602E6 CRC64;
MSGDEMIFDP TMSKKKKKKK KPFMLDEEGD TQTEETQPSE TKEVEPEPTE DKDLEADEED
TRKKDASDDL DDLNFFNQKK KKKKTKKIFD IDEAEEGVKD LKIESDVQEP TEPEDDLDIM
LGNKKKKKKN VKFPDEDEIL EKDEALEDED NKKDDGISFS NQTGPAWAGS ERDYTYEELL
NRVFNIMREK NPDMVAGEKR KFVMKPPQVV RVGTKKTSFV NFTDICKLLH RQPKHLLAFL
LAELGTSGSI DGNNQLVIKG RFQQKQIENV LRRYIKEYVT CHTCRSPDTI LQKDTRLYFL
QCETCHSRCS AASIKTGFQA VTGKRAQLRA KAN
