ERF3B_PONAB
ID ERF3B_PONAB Reviewed; 628 AA.
AC Q5R4B3;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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 -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. ERF3 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; CR861342; CAH93403.1; -; mRNA.
DR RefSeq; NP_001126997.1; NM_001133525.1.
DR AlphaFoldDB; Q5R4B3; -.
DR BMRB; Q5R4B3; -.
DR SMR; Q5R4B3; -.
DR STRING; 9601.ENSPPYP00000022791; -.
DR GeneID; 100174020; -.
DR KEGG; pon:100174020; -.
DR CTD; 23708; -.
DR eggNOG; KOG0459; Eukaryota.
DR InParanoid; Q5R4B3; -.
DR OrthoDB; 1150082at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
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; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR009818; Ataxin-2_C.
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; 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 2: Evidence at transcript level;
KW Cell cycle; Cytoplasm; GTP-binding; Nonsense-mediated mRNA decay;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..628
FT /note="Eukaryotic peptide chain release factor GTP-binding
FT subunit ERF3B"
FT /id="PRO_0000327258"
FT DOMAIN 201..425
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..217
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 266..270
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 287..290
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 349..352
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 391..393
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT COMPBIAS 81..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 210..217
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 287..291
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 349..352
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT SITE 216
FT /note="Interacts with GTP/GDP"
FT /evidence="ECO:0000250"
FT SITE 350
FT /note="Interacts with GTP/GDP"
FT /evidence="ECO:0000250"
SQ SEQUENCE 628 AA; 68839 MW; BBCC67FA1B2518AB CRC64;
MDSGSSSSDS APDCWDQVDM EAPGSAPSGD GVSSAVAEAQ REPLSSAFSR QLNVNAKPFV
PNVHAAEFVP SFLRGPSQPP TLPAGSGSND ETCTGAGYPQ GKRMGRGAPV EPSREEPLVS
LEGSNSAVTM ELSEPVVENG EVEMALEESW EHSKEVSEAE PGGGSSGDSG PPEESGQEMM
EEKEEIRKSK SVIVPSGAPK KEHVNVVFIG HVDAGKSTIG GQIMFLTGMV DKRTLEKYER
EAKEKNRETW YLSWALDTNQ EERDKGKTVE VGRAYFETER KHFTILDAPG HKSFVPNMIG
GASQADLAVL VISARKGEFE TGFEKGGQTR EHAMLAKTAG VKHLIVLINK MDDPTVNWSI
ERYEECKEKL VPFLKKVGFS PKKDIHFMPC SGLTGANVKE QSDFCPWYTG LPFIPYLDNL
PNFNRSIDGP IRLPIVDKYK DMGTVVLGKL ESGSIFKGQQ LVMMPNKHNV EVLGILSDDT
ETDFVAPGEN LKIRLKGIEE EEILPGFILC DPSNLCHSGR TFDVQIVIIE HKSIICPGYN
AVLHIHTCIE EVEITALISL VDKKSGEKSK TRPRFVKQDQ VCIARLRTAG TICLETFKDF
PQMGRFTLRD EGKTIAIGKV LKLVPEKD
