ERF3A_MOUSE
ID ERF3A_MOUSE Reviewed; 636 AA.
AC Q8R050; E9QK49; G3UWC0; O88179; Q8K2E1;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Eukaryotic peptide chain release factor GTP-binding subunit ERF3A;
DE Short=Eukaryotic peptide chain release factor subunit 3a;
DE Short=eRF3a;
DE AltName: Full=G1 to S phase transition protein 1 homolog;
GN Name=Gspt1; Synonyms=Erf3a;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-636 (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Eye, and Mammary tumor;
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 86-636 (ISOFORM 2).
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 PROTEIN SEQUENCE OF 441-448, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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).
RN [7]
RP STRUCTURE BY NMR OF 64-94 IN COMPLEX WITH PABPC1.
RA Osawa M., Nakanishi T., Hosoda N., Uchida S., Hoshino T., Katada I.,
RA Shimada I.;
RT "Eukaryotic translation termination factor Gspt/ERF3 recognizes Pabp with
RT chemical exchange using two overlapping motifs.";
RL Submitted (MAY-2009) to the PDB data bank.
CC -!- FUNCTION: Involved in translation termination in response to the
CC termination codons UAA, UAG and UGA (By similarity). Stimulates the
CC activity of ETF1 (By similarity). Involved in regulation of mammalian
CC cell growth. Component of the transient SURF complex which recruits
CC UPF1 to stalled ribosomes in the context of nonsense-mediated decay
CC (NMD) of mRNAs containing premature stop codons (By similarity).
CC Required for SHFL-mediated translation termination which inhibits
CC programmed ribosomal frameshifting (-1PRF) of mRNA from viruses and
CC cellular genes (By similarity). {ECO:0000250|UniProtKB:P15170,
CC ECO:0000250|UniProtKB:Q8IYD1}.
CC -!- SUBUNIT: Component of the transient SURF (SMG1-UPF1-eRF1-eRF3) complex
CC (By similarity). Interacts with PABPC1 (Ref.7). The ETF1-GSPT1 complex
CC interacts with JMJD4 (By similarity). Interacts with SHFL (By
CC similarity). {ECO:0000250|UniProtKB:P15170, ECO:0000269|Ref.7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R050-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R050-2; Sequence=VSP_043829;
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=AAH28325.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH31640.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC087541; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466521; EDK97345.1; -; Genomic_DNA.
DR EMBL; BC028325; AAH28325.1; ALT_INIT; mRNA.
DR EMBL; BC031640; AAH31640.1; ALT_INIT; mRNA.
DR EMBL; AB003502; BAA32526.1; -; mRNA.
DR CCDS; CCDS27961.2; -. [Q8R050-1]
DR CCDS; CCDS49764.1; -. [Q8R050-2]
DR RefSeq; NP_001123480.1; NM_001130008.1. [Q8R050-2]
DR RefSeq; NP_666178.2; NM_146066.2. [Q8R050-1]
DR PDB; 2RQG; NMR; -; A=64-82.
DR PDB; 2RQH; NMR; -; A=73-94.
DR PDBsum; 2RQG; -.
DR PDBsum; 2RQH; -.
DR AlphaFoldDB; Q8R050; -.
DR BMRB; Q8R050; -.
DR SMR; Q8R050; -.
DR BioGRID; 200087; 52.
DR ComplexPortal; CPX-670; Translation release factor ERF1-ERF3 complex.
DR IntAct; Q8R050; 36.
DR MINT; Q8R050; -.
DR STRING; 10090.ENSMUSP00000078940; -.
DR iPTMnet; Q8R050; -.
DR PhosphoSitePlus; Q8R050; -.
DR SwissPalm; Q8R050; -.
DR EPD; Q8R050; -.
DR jPOST; Q8R050; -.
DR MaxQB; Q8R050; -.
DR PaxDb; Q8R050; -.
DR PeptideAtlas; Q8R050; -.
DR PRIDE; Q8R050; -.
DR ProteomicsDB; 275796; -. [Q8R050-1]
DR ProteomicsDB; 275797; -. [Q8R050-2]
DR Antibodypedia; 24757; 169 antibodies from 30 providers.
DR DNASU; 14852; -.
DR Ensembl; ENSMUST00000080030; ENSMUSP00000078940; ENSMUSG00000062203. [Q8R050-1]
DR Ensembl; ENSMUST00000167571; ENSMUSP00000130583; ENSMUSG00000062203. [Q8R050-2]
DR GeneID; 14852; -.
DR KEGG; mmu:14852; -.
DR UCSC; uc007yfe.2; mouse. [Q8R050-1]
DR UCSC; uc007yff.2; mouse. [Q8R050-2]
DR CTD; 2935; -.
DR MGI; MGI:1316728; Gspt1.
DR VEuPathDB; HostDB:ENSMUSG00000062203; -.
DR eggNOG; KOG0459; Eukaryota.
DR GeneTree; ENSGT00940000155582; -.
DR HOGENOM; CLU_007265_3_8_1; -.
DR InParanoid; Q8R050; -.
DR OMA; PGHVEYT; -.
DR OrthoDB; 1150082at2759; -.
DR PhylomeDB; Q8R050; -.
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; 14852; 23 hits in 71 CRISPR screens.
DR ChiTaRS; Gspt1; mouse.
DR PRO; PR:Q8R050; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8R050; protein.
DR Bgee; ENSMUSG00000062203; Expressed in embryonic post-anal tail and 262 other tissues.
DR ExpressionAtlas; Q8R050; baseline and differential.
DR Genevisible; Q8R050; MM.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0018444; C:translation release factor complex; ISO:MGI.
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; ISS:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR GO; GO:0006479; P:protein methylation; ISO:MGI.
DR GO; GO:0006449; P:regulation of translational termination; ISS:UniProtKB.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR GO; GO:0006415; P:translational termination; ISO:MGI.
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 3D-structure; Alternative splicing; Direct protein sequencing; GTP-binding;
KW Nonsense-mediated mRNA decay; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..636
FT /note="Eukaryotic peptide chain release factor GTP-binding
FT subunit ERF3A"
FT /id="PRO_0000091481"
FT DOMAIN 209..435
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..225
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 274..278
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 295..298
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 357..360
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 399..401
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT COMPBIAS 11..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 218..225
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 295..299
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 357..360
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT VAR_SEQ 145
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9712840"
FT /id="VSP_043829"
FT CONFLICT 41
FT /note="G -> A (in Ref. 3; AAH31640)"
FT /evidence="ECO:0000305"
FT CONFLICT 485
FT /note="S -> C (in Ref. 4; BAA32526)"
FT /evidence="ECO:0000305"
FT CONFLICT 615
FT /note="T -> R (in Ref. 4; BAA32526)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 636 AA; 68625 MW; 28EC54B408D3F5A3 CRC64;
MDPSSGGGGG GGGGGSSSSS DSAPDCWDQT DMEAPGPGPC GGGGSGSGSM AAVAEAQREN
LSAAFSRQLN VNAKPFVPNV HAAEFVPSFL RGPAQPPLSP AGAAGGDHGA GSGAGGPSEP
VESSQDQSCE GSNSTVSMEL SEPVVENGET EMSPEESWEH KEEISEAEPG GGSSGDGRPP
EESTQEMMEE EEEIPKPKSA VAPPGAPKKE HVNVVFIGHV DAGKSTIGGQ IMYLTGMVDK
RTLEKYEREA KEKNRETWYL SWALDTNQEE RDKGKTVEVG RAYFETEKKH FTILDAPGHK
SFVPNMIGGA SQADLAVLVI SARKGEFETG FEKGGQTREH AMLAKTAGVK HLIVLINKMD
DPTVNWSNER YEECKEKLVP FLKKVGFNPK KDIHFMPCSG LTGANLKEQS DFCPWYIGLP
FIPYLDNLPN FNRSVDGPIR LPIVDKYKDM GTVVLGKLES GSICKGQQLV MMPNKHNVEV
LGILSDDVET DSVAPGENLK IRLKGIEEEE ILPGFILCDL NNLCHSGRTF DAQIVIIEHK
SIICPGYNAV LHIHTCIEEV EITALICLVD KKSGEKSKTR PRFVKQDQVC IARLRTAGTI
CLETFKDFPQ MGRFTLRDEG KTIAIGKVLK LVPEKD
