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IF2G_CHICK
ID   IF2G_CHICK              Reviewed;         472 AA.
AC   Q5ZMS3;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Eukaryotic translation initiation factor 2 subunit 3;
DE            EC=3.6.5.3;
DE   AltName: Full=Eukaryotic translation initiation factor 2 subunit gamma;
DE            Short=eIF-2-gamma;
GN   Name=EIF2S3; ORFNames=RCJMB04_1f8;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-38; 290-303; 398-416 AND 427-440, CLEAVAGE OF
RP   INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RA   Bienvenut W.V., Black E.J., Gillespie D.A.;
RL   Submitted (JAN-2007) to UniProtKB.
CC   -!- FUNCTION: As a subunit of eukaryotic initiation factor 2 (eIF-2),
CC       involved in the early steps of protein synthesis. In the presence of
CC       GTP, eIF-2 forms a ternary complex with initiator tRNA Met-tRNAi and
CC       then recruits the 40S ribosomal complex and initiation factors eIF-1,
CC       eIF-1A and eIF-3 to form the 43S pre-initiation complex (43S PIC), a
CC       step that determines the rate of protein translation. The 43S PIC binds
CC       to mRNA and scans downstream to the initiation codon, where it forms a
CC       48S initiation complex by codon-anticodon base pairing. This leads to
CC       the displacement of eIF-1 to allow GTPase-activating protein (GAP) eIF-
CC       5-mediated hydrolysis of eIF2-bound GTP. Hydrolysis of GTP and release
CC       of Pi, which makes GTP hydrolysis irreversible, causes the release of
CC       the eIF-2-GDP binary complex from the 40S subunit, an event that is
CC       essential for the subsequent joining of the 60S ribosomal subunit to
CC       form an elongation-competent 80S ribosome. In order for eIF-2 to
CC       recycle and catalyze another round of initiation, the GDP bound to eIF-
CC       2 must be exchanged with GTP by way of a reaction catalyzed by GDP-GTP
CC       exchange factor (GEF) eIF-2B. {ECO:0000250|UniProtKB:P32481}.
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:P32481};
CC   -!- SUBUNIT: The eukaryotic translation initiation factor 2 complex/eIF2 is
CC       a heterotrimer composed of an alpha, a beta and a gamma subunit.
CC       {ECO:0000250|UniProtKB:P41091}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EIF2G subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR   EMBL; AJ719311; CAG30970.1; -; mRNA.
DR   RefSeq; NP_001006260.1; NM_001006260.2.
DR   AlphaFoldDB; Q5ZMS3; -.
DR   SMR; Q5ZMS3; -.
DR   BioGRID; 679807; 1.
DR   STRING; 9031.ENSGALP00000026307; -.
DR   PaxDb; Q5ZMS3; -.
DR   GeneID; 418597; -.
DR   KEGG; gga:418597; -.
DR   CTD; 1968; -.
DR   VEuPathDB; HostDB:geneid_418597; -.
DR   eggNOG; KOG0466; Eukaryota.
DR   InParanoid; Q5ZMS3; -.
DR   OrthoDB; 903135at2759; -.
DR   PhylomeDB; Q5ZMS3; -.
DR   PRO; PR:Q5ZMS3; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005850; C:eukaryotic translation initiation factor 2 complex; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0001731; P:formation of translation preinitiation complex; IBA:GO_Central.
DR   GO; GO:0045903; P:positive regulation of translational fidelity; IBA:GO_Central.
DR   CDD; cd01888; eIF2_gamma; 1.
DR   CDD; cd03688; eIF2_gamma_II; 1.
DR   CDD; cd15490; eIF2_gamma_III; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR015256; eIF2g_C.
DR   InterPro; IPR044127; eIF2g_dom_2.
DR   InterPro; IPR044128; eIF2g_GTP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   Pfam; PF09173; eIF2_C; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF50465; SSF50465; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; GTP-binding; Hydrolase;
KW   Initiation factor; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.2"
FT   CHAIN           2..472
FT                   /note="Eukaryotic translation initiation factor 2 subunit
FT                   3"
FT                   /id="PRO_0000280446"
FT   DOMAIN          39..247
FT                   /note="tr-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          48..55
FT                   /note="G1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          76..80
FT                   /note="G2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          134..137
FT                   /note="G3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          190..193
FT                   /note="G4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          225..227
FT                   /note="G5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   BINDING         51..56
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P32481"
FT   BINDING         190..193
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P32481"
FT   BINDING         225..227
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P32481"
FT   MOD_RES         2
FT                   /note="N-acetylalanine; partial"
FT                   /evidence="ECO:0000269|Ref.2"
SQ   SEQUENCE   472 AA;  51076 MW;  40036ABDDF10597A CRC64;
     MAGDEAGVTL GQPHLSRQDL ATLDVTKLTP LSPEVISRQA TINIGTIGHV AHGKSTVVKA
     ISGVHTVRFK NELERNITIK LGYANAKIYK LDDPSCSRPE CYRSCGSSTP DEFPTDIPGT
     KGNFKLVRHV SFVDCPGHDI LMATMLNGAA VMDAALLLIA GNESCPQPQT SEHLAAIEIM
     KLKHILILQN KIDLVKESQA KEQYEQILAF VQGTVAEGAP IIPISAQLKY SIEVVCEYIV
     KKIPVPLRDF TSEPRLIVIR SFDVNKPGCE VDDLKGGVAG GSILKGVLKV GQEIEVRPGI
     VSKDSEGKLM CKPIFSKIVS LFAEHNDLQY AAPGGLIGVG TKIDPTLCRA DRMVGQVLGA
     VGALPEIFTE LEISYFLLRR LLGVRTEGDK KAAKVQKLSK NEVLMVNIGS LSTGGRVSAV
     KADLGKIVLT NPVCTEVGEK IALSRRVEKH WRLIGWGQIR RGVTIKPTVD DD
 
 
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