ERF3B_MOUSE
ID ERF3B_MOUSE Reviewed; 632 AA.
AC Q149F3; O88180; Q9CY91;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Eukaryotic peptide chain release factor GTP-binding subunit ERF3B;
DE Short=Eukaryotic peptide chain release factor subunit 3b;
DE Short=eRF3b;
DE AltName: Full=G1 to S phase transition protein 2 homolog;
GN Name=Gspt2; Synonyms=Erf3b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [MRNA] OF 21-632, INTERACTION WITH ETF1, AND TISSUE
RP SPECIFICITY.
RX PubMed=9712840; DOI=10.1074/jbc.273.35.22254;
RA Hoshino S., Imai M., Mizutani M., Kikuchi Y., Hanaoka F., Ui M., Katada T.;
RT "Molecular cloning of a novel member of the eukaryotic polypeptide chain-
RT releasing factors (eRF). Its identification as eRF3 interacting with
RT eRF1.";
RL J. Biol. Chem. 273:22254-22259(1998).
RN [5]
RP INTERACTION WITH ETF1, AND FUNCTION.
RX PubMed=12354098; DOI=10.1046/j.1365-2443.2002.00585.x;
RA Le Goff C., Zemlyanko O., Moskalenko S., Berkova N., Inge-Vechtomov S.,
RA Philippe M., Zhouravleva G.;
RT "Mouse GSPT2, but not GSPT1, can substitute for yeast eRF3 in vivo.";
RL Genes Cells 7:1043-1057(2002).
RN [6]
RP DEVELOPMENTAL STAGE.
RX PubMed=15987998; DOI=10.1128/mcb.25.14.5801-5811.2005;
RA Chauvin C., Salhi S., Le Goff C., Viranaicken W., Diop D., Jean-Jean O.;
RT "Involvement of human release factors eRF3a and eRF3b in translation
RT termination and regulation of the termination complex formation.";
RL Mol. Cell. Biol. 25:5801-5811(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Involved in translation termination in response to the
CC termination codons UAA, UAG and UGA. May play a role as a potent
CC stimulator of the release factor activity of ETF1. Exhibits GTPase
CC activity, which is ribosome- and ETF1-dependent. May play a role in
CC cell cycle progression. Component of the transient SURF complex which
CC recruits UPF1 to stalled ribosomes in the context of nonsense-mediated
CC decay (NMD) of mRNAs containing premature stop codons (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:12354098}.
CC -!- SUBUNIT: Interacts with ETF1. Component of the transient SURF (SMG1-
CC UPF1-eRF1-eRF3) complex. Interacts with UPF1 and PABPC1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain. Moderately expressed in
CC spleen and lung. Weakly expressed in heart, liver and kidney.
CC Expression during the cell-cycle progression is constant.
CC {ECO:0000269|PubMed:9712840}.
CC -!- DEVELOPMENTAL STAGE: Barely detectable at 15 dpc, increased after birth
CC to reach a maximum at P15. {ECO:0000269|PubMed:15987998}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. ERF3 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01059}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA32527.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB31621.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK019241; BAB31621.1; ALT_FRAME; mRNA.
DR EMBL; AL645466; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC117825; AAI17826.1; -; mRNA.
DR EMBL; BC117826; AAI17827.1; -; mRNA.
DR EMBL; AB003503; BAA32527.1; ALT_INIT; mRNA.
DR CCDS; CCDS41064.1; -.
DR RefSeq; NP_032205.2; NM_008179.2.
DR AlphaFoldDB; Q149F3; -.
DR SMR; Q149F3; -.
DR BioGRID; 200088; 4.
DR IntAct; Q149F3; 1.
DR STRING; 10090.ENSMUSP00000109523; -.
DR iPTMnet; Q149F3; -.
DR PhosphoSitePlus; Q149F3; -.
DR SwissPalm; Q149F3; -.
DR EPD; Q149F3; -.
DR jPOST; Q149F3; -.
DR MaxQB; Q149F3; -.
DR PaxDb; Q149F3; -.
DR PeptideAtlas; Q149F3; -.
DR PRIDE; Q149F3; -.
DR ProteomicsDB; 275798; -.
DR Antibodypedia; 26328; 195 antibodies from 25 providers.
DR DNASU; 14853; -.
DR Ensembl; ENSMUST00000096368; ENSMUSP00000109523; ENSMUSG00000071723.
DR GeneID; 14853; -.
DR KEGG; mmu:14853; -.
DR UCSC; uc009tto.1; mouse.
DR CTD; 23708; -.
DR MGI; MGI:1316727; Gspt2.
DR VEuPathDB; HostDB:ENSMUSG00000071723; -.
DR eggNOG; KOG0459; Eukaryota.
DR GeneTree; ENSGT00940000163245; -.
DR HOGENOM; CLU_007265_3_8_1; -.
DR InParanoid; Q149F3; -.
DR OMA; ESWEHSK; -.
DR OrthoDB; 1150082at2759; -.
DR PhylomeDB; Q149F3; -.
DR TreeFam; TF300566; -.
DR Reactome; R-MMU-72764; Eukaryotic Translation Termination.
DR Reactome; R-MMU-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR BioGRID-ORCS; 14853; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q149F3; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q149F3; protein.
DR Bgee; ENSMUSG00000071723; Expressed in seminal vesicle and 217 other tissues.
DR ExpressionAtlas; Q149F3; baseline and differential.
DR Genevisible; Q149F3; MM.
DR GO; GO:0018444; C:translation release factor complex; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0003747; F:translation release factor activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR009818; Ataxin-2_C.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
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 InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR Pfam; PF07145; PAM2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cytoplasm; GTP-binding; Nonsense-mediated mRNA decay;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..632
FT /note="Eukaryotic peptide chain release factor GTP-binding
FT subunit ERF3B"
FT /id="PRO_0000327257"
FT DOMAIN 205..429
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..221
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 270..274
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 291..294
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 353..356
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 395..397
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT COMPBIAS 178..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 214..221
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 291..295
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 353..356
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT SITE 220
FT /note="Interacts with GTP/GDP"
FT /evidence="ECO:0000250"
FT SITE 354
FT /note="Interacts with GTP/GDP"
FT /evidence="ECO:0000250"
FT CONFLICT 21
FT /note="A -> G (in Ref. 4; BAA32527)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="A -> P (in Ref. 4; BAA32527)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="S -> A (in Ref. 4; BAA32527)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="T -> K (in Ref. 1; BAB31621)"
FT /evidence="ECO:0000305"
FT CONFLICT 510
FT /note="G -> A (in Ref. 1; BAB31621)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 632 AA; 69147 MW; 9783F5C867D8EB13 CRC64;
MDLGSSSDSA PDCWDQVDME APGSAPSGDG IAPAAMAAAE AAEAEAQRKH LSLAFSSQLN
IHAKPFVPSV SAAEFVPSFL PGSAQPPAPT ASSCDETCIG GAGEPEGKRM EWGAPVEPSK
DGPLVSWEGS SSVVTMELSE PVVENGEVEM ALEESWELKE VSEAKPEASL GDAGPPEESV
KEVMEEKEEV RKSKSVSIPS GAPKKEHVNV VFIGHVDAGK STIGGQIMFL TGMVDRRTLE
KYEREAKEKN RETWYLSWAL DTNQEERDKG KTVEVGRAYF ETEKKHFTIL DAPGHKSFVP
NMIGGASQAD LAVLVISARK GEFETGFEKG GQTREHAMLA KTAGVKYLIV LINKMDDPTV
DWSSERYEEC KEKLVPFLKK VGFSPKKDIH FMPCSGLTGA NIKEQSDFCP WYTGLPFIPY
LDSLPNFNRS IDGPIRLPIV DKYKDMGTVV LGKLESGSIF KGQQLVMMPN KHSVEVLGIV
SDDAETDFVA PGENLKIRLK GIEEEEILPG FILCEPSNLC HSGRTFDVQI VIIEHKSIIC
PGYNAVLHIH TCIEEVEITA LISLVDKKSG EKSKTRPRFV KQDQVCIARL RTAGTICLET
FKDFPQMGRF TLRDEGKTIA IGKVLKLVPE KD
