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   24-JAN-2024, entry version 129.
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: Member of the eIF2 complex that functions in the early steps
CC       of protein synthesis by forming a ternary complex with GTP and
CC       initiator tRNA. This complex binds to a 40S ribosomal subunit, followed
CC       by mRNA binding to form the 43S pre-initiation complex (43S PIC).
CC       Junction of the 60S ribosomal subunit to form the 80S initiation
CC       complex is preceded by hydrolysis of the GTP bound to eIF2 and release
CC       of an eIF2-GDP binary complex. In order for eIF2 to recycle and
CC       catalyze another round of initiation, the GDP bound to eIF2 must
CC       exchange with GTP by way of a reaction catalyzed by eIF-2B (By
CC       similarity). {ECO:0000250|UniProtKB:P05198}.
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: eIF2 is an heterotrimer composed of an alpha, a beta and a
CC       gamma chain. eIF2 is member of the 43S pre-initiation complex (43S
CC       PIC). {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   CCDS; CCDS91654.1; -. [Q2VIR3-1]
DR   AlphaFoldDB; Q2VIR3; -.
DR   SMR; Q2VIR3; -.
DR   IntAct; Q2VIR3; 11.
DR   MINT; Q2VIR3; -.
DR   GlyGen; Q2VIR3; 1 site, 1 O-linked glycan (1 site).
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; 9606-ENSP00000445077; -.
DR   PeptideAtlas; Q2VIR3; -.
DR   ProteomicsDB; 61512; -. [Q2VIR3-1]
DR   ProteomicsDB; 61513; -. [Q2VIR3-2]
DR   Pumba; Q2VIR3; -.
DR   Antibodypedia; 71457; 16 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   AGR; HGNC:43863; -.
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   OMA; VILRQPH; -.
DR   OrthoDB; 1512042at2759; -.
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 male germ line stem cell (sensu Vertebrata) in testis and 80 other cell types or tissues.
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   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; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
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   PANTHER; PTHR42854; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 3 FAMILY MEMBER; 1.
DR   PANTHER; PTHR42854:SF14; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 3-RELATED; 1.
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; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
DR   Genevisible; Q2VIR3; HS.
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
//