IF2B_BOVIN
ID IF2B_BOVIN Reviewed; 333 AA.
AC Q5E9D0; Q0IIJ6;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 82.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) 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; BT020990; AAX09007.1; -; mRNA.
DR EMBL; BC122609; AAI22610.1; -; mRNA.
DR RefSeq; NP_001015621.1; NM_001015621.1.
DR AlphaFoldDB; Q5E9D0; -.
DR SMR; Q5E9D0; -.
DR STRING; 9913.ENSBTAP00000007832; -.
DR PaxDb; Q5E9D0; -.
DR PeptideAtlas; Q5E9D0; -.
DR PRIDE; Q5E9D0; -.
DR GeneID; 520094; -.
DR KEGG; bta:520094; -.
DR CTD; 8894; -.
DR eggNOG; KOG2768; Eukaryota.
DR HOGENOM; CLU_026663_0_1_1; -.
DR InParanoid; Q5E9D0; -.
DR OrthoDB; 1178655at2759; -.
DR TreeFam; TF101503; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005850; C:eukaryotic translation initiation factor 2 complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; ISS:UniProtKB.
DR GO; GO:0031369; F:translation initiation factor binding; IBA:GO_Central.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IBA:GO_Central.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IBA:GO_Central.
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_0000247193"
FT ZN_FING 281..305
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..165
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 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 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 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"
FT CONFLICT 324
FT /note="R -> K (in Ref. 2; AAI22610)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 38286 MW; 96DD5CD2D50FC0B7 CRC64;
MSGDEMIFDP TMSKKKKKKK KPFMLDEEGD AQTEETQPSE TKEVEPEPTE DKDVEADEED
SRKKDASDDL DDLNFFNQKK KKKKSKKIFD IDEAEEGIKD LKIESDVQEP AEPEEDLDIM
LGNKKKKKKV VKFPDEDEVL EKDEALEDED SKKDDGISFS NQTGPAWAGS ERDYTYEELL
NRVFNIMREK NPDMVAGEKR KFVMKPPQVV RVGTKKTSFV NFTDICKLLH RQPKHLLAFL
LAELGTSGSI DGNNQLVIKG RFQQKQIENV LRRYIKEYVT CHTCRSPDTI LQKDTRLYFL
QCETCHSRCS VASIKTGFQA VTGRRAQLRA KAN
