IF2GL_HUMAN
ID IF2GL_HUMAN Reviewed; 472 AA.
AC Q2VIR3; F8W810; Q5I0X0; Q6KF84;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Eukaryotic translation initiation factor 2 subunit 3B {ECO:0000305};
DE EC=3.6.5.3;
DE AltName: Full=Eukaryotic translation initiation factor 2 subunit gamma A;
DE Short=eIF-2-gamma A {ECO:0000303|PubMed:9736774};
DE Short=eIF-2gA;
GN Name=EIF2S3B {ECO:0000312|HGNC:HGNC:43863};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND EVOLUTIONARY ANALYSIS.
RX PubMed=16201836; DOI=10.1371/journal.pbio.0030357;
RA Marques A.C., Dupanloup I., Vinckenbosch N., Reymond A., Kaessmann H.;
RT "Emergence of young human genes after a burst of retroposition in
RT primates.";
RL PLoS Biol. 3:E357-E357(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-471 (ISOFORM 2).
RC TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 61-309, AND TISSUE SPECIFICITY.
RX PubMed=9736774; DOI=10.1093/hmg/7.11.1725;
RA Ehrmann I.E., Ellis P.S., Mazeyrat S., Duthie S., Brockdorff N.,
RA Mattei M.-G., Gavin M.A., Affara N.A., Brown G.M., Simpson E.,
RA Mitchell M.J., Scott D.M.;
RT "Characterization of genes encoding translation initiation factor eIF-
RT 2gamma in mouse and human: sex chromosome localization, escape from X-
RT inactivation and evolution.";
RL Hum. Mol. Genet. 7:1725-1737(1998).
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 (By similarity). Along with its paralog on
CC chromosome Y, may contribute to spermatogenesis up to the round
CC spermatid stage (By similarity). {ECO:0000250|UniProtKB:P32481,
CC ECO:0000250|UniProtKB:Q9Z0N1}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q2VIR3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2VIR3-2; Sequence=VSP_034711;
CC -!- TISSUE SPECIFICITY: Specifically expressed in testis at the mRNA level.
CC {ECO:0000269|PubMed:9736774}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABB92405.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA07331.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; DQ120619; ABB92405.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC068775; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC087847; AAH87847.1; -; mRNA.
DR EMBL; AJ006932; CAA07331.1; ALT_FRAME; Genomic_DNA.
DR CCDS; CCDS86282.1; -. [Q2VIR3-2]
DR AlphaFoldDB; Q2VIR3; -.
DR SMR; Q2VIR3; -.
DR IntAct; Q2VIR3; 11.
DR MINT; Q2VIR3; -.
DR STRING; 9606.ENSP00000445077; -.
DR iPTMnet; Q2VIR3; -.
DR MetOSite; Q2VIR3; -.
DR PhosphoSitePlus; Q2VIR3; -.
DR SwissPalm; Q2VIR3; -.
DR BioMuta; EIF2S3L; -.
DR BioMuta; ENSG00000180574; -.
DR DMDM; 205830883; -.
DR EPD; Q2VIR3; -.
DR jPOST; Q2VIR3; -.
DR MassIVE; Q2VIR3; -.
DR MaxQB; Q2VIR3; -.
DR PaxDb; Q2VIR3; -.
DR PeptideAtlas; Q2VIR3; -.
DR PRIDE; Q2VIR3; -.
DR Antibodypedia; 71457; 15 antibodies from 4 providers.
DR Ensembl; ENST00000322446.3; ENSP00000323063.3; ENSG00000180574.4. [Q2VIR3-2]
DR Ensembl; ENST00000538173.2; ENSP00000445077.1; ENSG00000180574.4. [Q2VIR3-1]
DR MANE-Select; ENST00000538173.2; ENSP00000445077.1; NM_001357734.3; NP_001344663.1.
DR UCSC; uc058lel.1; human. [Q2VIR3-1]
DR GeneCards; EIF2S3B; -.
DR HGNC; HGNC:43863; EIF2S3B.
DR HPA; ENSG00000180574; Low tissue specificity.
DR neXtProt; NX_Q2VIR3; -.
DR OpenTargets; ENSG00000180574; -.
DR VEuPathDB; HostDB:ENSG00000180574; -.
DR eggNOG; KOG0466; Eukaryota.
DR GeneTree; ENSGT00550000074801; -.
DR HOGENOM; CLU_027154_0_1_1; -.
DR InParanoid; Q2VIR3; -.
DR PhylomeDB; Q2VIR3; -.
DR TreeFam; TF101513; -.
DR PathwayCommons; Q2VIR3; -.
DR SignaLink; Q2VIR3; -.
DR Pharos; Q2VIR3; Tdark.
DR PRO; PR:Q2VIR3; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q2VIR3; protein.
DR Bgee; ENSG00000180574; Expressed in stromal cell of endometrium and 79 other tissues.
DR Genevisible; Q2VIR3; HS.
DR GO; GO:0005850; C:eukaryotic translation initiation factor 2 complex; 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: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 2: Evidence at transcript level;
KW Acetylation; Alternative splicing; GTP-binding; Hydrolase;
KW Initiation factor; Nucleotide-binding; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P41091"
FT CHAIN 2..472
FT /note="Eukaryotic translation initiation factor 2 subunit
FT 3B"
FT /id="PRO_0000343941"
FT DOMAIN 39..248
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"
FT /evidence="ECO:0000250|UniProtKB:P41091"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0N1"
FT VAR_SEQ 437..472
FT /note="VGEKIALSRRVEKHWRLIGWGQIRRGVTIKPTVDDD -> IHLIHLDLIKEL
FT EWGPVLTNETQRKSAANF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034711"
FT CONFLICT 243
FT /note="I -> F (in Ref. 1; ABB92405)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="V -> G (in Ref. 4; CAA07331)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="A -> T (in Ref. 4; CAA07331)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="Q -> H (in Ref. 4; CAA07331)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="I -> L (in Ref. 4; CAA07331)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="S -> P (in Ref. 1; ABB92405 and 3; AAH87847)"
FT /evidence="ECO:0000305"
FT CONFLICT Q2VIR3-2:453
FT /note="V -> L (in Ref. 3; AAH87847)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 472 AA; 51229 MW; 6ECFD47900903ED9 CRC64;
MAGGEAGVTL GQPHLSRQDL TTLDVTKLTP LSHEVISRQA TINIGTIGHV AHGKSTVVKA
ISGVHTVRFK NELERNITIK LGYANAKIYQ LDDPSCPRPE CYRSCGSSMP DEFPTDIPGT
KGNFRLVRHV SFVDCPGHDI LMATMLNGAA VMDAALLLIA GNESCPQPQT SEHLAAIEIM
KLKHILILQN KIDLVKERQA KEQYEQILAF VQGTVAEGAP IIPISAQLKY NIEVVCEYIV
KKIPVPPRDF TSEPRLIVIR SFDVNKPGCE VDDLKGGVAG GSILKGVLKV GQETEVRPGI
VSKDSEGKLM CKSIFSKIVS LFAEHNDLQY AAPGGLIGVG TKIDPTLCRA DRMVGQILGA
VGALPEIFTE LEISYFLLRR LLGVRTEGDK KAAKVQKLSK NEVLMVNIGS LSTGGRVSAV
KADLGKIVLT NPVCTEVGEK IALSRRVEKH WRLIGWGQIR RGVTIKPTVD DD
