IF2B_RABIT
ID IF2B_RABIT Reviewed; 333 AA.
AC P41035;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 129.
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; Synonyms=EIF2B;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2207148; DOI=10.1016/0167-4781(90)90173-y;
RA Merrick W.C., Dever T.E., Kinzy T.G., Conroy S.C., Cavallius J.,
RA Owens C.L.;
RT "Characterization of protein synthesis factors from rabbit reticulocytes.";
RL Biochim. Biophys. Acta 1050:235-240(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white;
RX PubMed=8218412; DOI=10.1016/0167-4781(93)90059-m;
RA Price N.T., Hall L., Proud C.G.;
RT "Cloning of cDNA for the beta-subunit of rabbit translation initiation
RT factor-2 using PCR.";
RL Biochim. Biophys. Acta 1216:170-172(1993).
RN [3]
RP PROTEIN SEQUENCE OF 25-39; 122-136 AND 195-218.
RC TISSUE=Reticulocyte;
RX PubMed=1911855; DOI=10.1016/0167-4838(91)90074-a;
RA Bommer U.-A., Kraft R., Kurzchalia T.V., Price N.T., Proud C.G.;
RT "Amino acid sequence analysis of the beta- and gamma-subunits of eukaryotic
RT initiation factor eIF-2. Identification of regions interacting with GTP.";
RL Biochim. Biophys. Acta 1079:308-315(1991).
RN [4]
RP CHARACTERIZATION.
RC TISSUE=Reticulocyte;
RX PubMed=3592677; DOI=10.1016/0003-9861(87)90401-2;
RA Schafer M.P., Fairwell T., Parker D.S., Knight M., Anderson W.F., Safer B.;
RT "The purification and characterization of subunits alpha, beta, and gamma
RT from the rabbit reticulocyte eukaryotic initiation factor 2.";
RL Arch. Biochem. Biophys. 255:337-346(1987).
RN [5]
RP PHOSPHORYLATION AT SER-2; SER-13; SER-67 AND SER-218.
RX PubMed=8024572; DOI=10.1006/bbrc.1994.1843;
RA Welsh G.I., Price N.T., Bladergroen B.A., Bloomberg G., Proud C.G.;
RT "Identification of novel phosphorylation sites in the beta-subunit of
RT translation initiation factor eIF-2.";
RL Biochem. Biophys. Res. Commun. 201:1279-1288(1994).
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.
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).
CC {ECO:0000250}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family. {ECO:0000305}.
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DR EMBL; X73836; CAA52058.1; -; mRNA.
DR PIR; JC2329; JC2329.
DR PIR; S13147; S13147.
DR PIR; S17871; S17871.
DR RefSeq; NP_001075867.1; NM_001082398.2.
DR AlphaFoldDB; P41035; -.
DR SMR; P41035; -.
DR STRING; 9986.ENSOCUP00000000420; -.
DR iPTMnet; P41035; -.
DR Ensembl; ENSOCUT00000000482; ENSOCUP00000000420; ENSOCUG00000000481.
DR GeneID; 100009285; -.
DR KEGG; ocu:100009285; -.
DR CTD; 8894; -.
DR eggNOG; KOG2768; Eukaryota.
DR GeneTree; ENSGT00390000001804; -.
DR HOGENOM; CLU_026663_0_1_1; -.
DR InParanoid; P41035; -.
DR OMA; CMREGNK; -.
DR OrthoDB; 1178655at2759; -.
DR Proteomes; UP000001811; Chromosome 4.
DR Bgee; ENSOCUG00000000481; Expressed in autopod skin and 15 other tissues.
DR GO; GO:0005850; C:eukaryotic translation initiation factor 2 complex; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; ISS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0002176; P:male germ cell proliferation; IEA:Ensembl.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
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 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Initiation factor; Isopeptide bond;
KW Metal-binding; Phosphoprotein; Protein biosynthesis; Reference proteome;
KW Ubl conjugation; 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_0000137408"
FT ZN_FING 281..305
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 1..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..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 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; by PKC; in vitro"
FT /evidence="ECO:0000269|PubMed:8024572"
FT MOD_RES 36
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20042"
FT MOD_RES 67
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:8024572"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20042"
FT MOD_RES 218
FT /note="Phosphoserine; by PKA; in vitro"
FT /evidence="ECO:0000269|PubMed:8024572"
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; 38326 MW; 3FFDBAB92DFC1465 CRC64;
MSGDEMIFDP TMSKKKKKKK KPFMLDEEGD AQTEETQPLE TKEVEPEPTE DKDVEADEED
SRKKDASDDL DDLNFFNQKK KKKKTKKIFD IDEAEEGVKD LKIENDVQEP AEPEDDLDIM
LGNKKKKKKN VKFPDEDEIL EKDEALEDED SKKDDGISFS NQTGPAWAGS ERDYTYEELL
NRVFNIMREK NPDMVAGEKR KFVMKPPQVV RVGTKKTSFV NFTDICKLLH RQPKHLLAFL
LAELGTSGSI DGNNQLVIKG RFQQKQIENV LRRYIKEYVT CHTCRSPDTI LQKDTRLYFL
QCETCHSRCS VASIKTGFQA VTGKRAQLRA KAN
