GTPB1_RAT
ID GTPB1_RAT Reviewed; 669 AA.
AC D2XV59;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=GTP-binding protein 1;
GN Name=Gtpbp1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kim T.-D., Kim K.-T.;
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH HNRNPD;
RP HNRNPR; SYNCRIP; EXOSC2; EXOSC3 AND EXOSC5, IDENTIFICATION IN A COMPLEX
RP WITH HNRNPD; HNRNPL; HNRNPQ; HNRNPR; HNRNPU AND MRNA, GTP BINDING, GTPASE
RP ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-173 AND 173-LYS-SER-174,
RP AND TISSUE SPECIFICITY.
RX PubMed=21515746; DOI=10.1096/fj.10-178715;
RA Woo K.C., Kim T.D., Lee K.H., Kim D.Y., Kim S., Lee H.R., Kang H.J.,
RA Chung S.J., Senju S., Nishimura Y., Kim K.T.;
RT "Modulation of exosome-mediated mRNA turnover by interaction of GTP-binding
RT protein 1 (GTPBP1) with its target mRNAs.";
RL FASEB J. 25:2757-2769(2011).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-44; SER-47; SER-69
RP AND SER-580, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Promotes degradation of target mRNA species. Plays a role in
CC the regulation of circadian mRNA stability. Binds GTP and has GTPase
CC activity. {ECO:0000269|PubMed:21515746}.
CC -!- SUBUNIT: Interacts with EXOSC2/RRP4, EXOSC3/RRP40, EXOSC5/RRP46,
CC HNRNPD, HNRNPR and SYNCRIP. Identified in a complex with HNRNPD,
CC HNRNPL, HNRNPQ, HNRNPR, HNRNPU and AANAT mRNA, but does not bind mRNA
CC by itself. {ECO:0000269|PubMed:21515746}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21515746}.
CC -!- TISSUE SPECIFICITY: Detected in pineal gland (at protein level).
CC {ECO:0000269|PubMed:21515746}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. GTPBP1
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; GU256773; ADB22435.1; -; mRNA.
DR EMBL; CH473950; EDM15787.1; -; Genomic_DNA.
DR RefSeq; NP_001186244.1; NM_001199315.1.
DR AlphaFoldDB; D2XV59; -.
DR SMR; D2XV59; -.
DR IntAct; D2XV59; 3.
DR STRING; 10116.ENSRNOP00000039165; -.
DR iPTMnet; D2XV59; -.
DR PhosphoSitePlus; D2XV59; -.
DR jPOST; D2XV59; -.
DR PaxDb; D2XV59; -.
DR PeptideAtlas; D2XV59; -.
DR PRIDE; D2XV59; -.
DR Ensembl; ENSRNOT00000049247; ENSRNOP00000039165; ENSRNOG00000014634.
DR GeneID; 300077; -.
DR KEGG; rno:300077; -.
DR UCSC; RGD:1306758; rat.
DR CTD; 9567; -.
DR RGD; 1306758; Gtpbp1.
DR eggNOG; KOG0463; Eukaryota.
DR GeneTree; ENSGT00940000156054; -.
DR HOGENOM; CLU_012821_2_0_1; -.
DR InParanoid; D2XV59; -.
DR OMA; FRFIQRP; -.
DR OrthoDB; 682656at2759; -.
DR PRO; PR:D2XV59; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Proteomes; UP000234681; Chromosome 7.
DR Bgee; ENSRNOG00000014634; Expressed in skeletal muscle tissue and 18 other tissues.
DR Genevisible; D2XV59; RN.
DR GO; GO:0000177; C:cytoplasmic exosome (RNase complex); IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0046039; P:GTP metabolic process; IDA:UniProtKB.
DR GO; GO:0061014; P:positive regulation of mRNA catabolic process; IDA:UniProtKB.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR CDD; cd04165; GTPBP1_like; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR039263; GTPB1.
DR InterPro; IPR035531; GTPBP1-like.
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; PTHR43721:SF9; PTHR43721:SF9; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTP-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..669
FT /note="GTP-binding protein 1"
FT /id="PRO_0000412470"
FT DOMAIN 158..389
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..174
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 206..210
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 252..255
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 308..311
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 366..368
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 573..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 167..174
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 252..256
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 308..311
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08582"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08582"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08582"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00178"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MUTAGEN 173..174
FT /note="KS->AA: Reduced decay of target mRNA. Slightly
FT reduced GTPase activity. No effect on GTP binding."
FT /evidence="ECO:0000269|PubMed:21515746"
FT MUTAGEN 173
FT /note="K->A: Reduced decay of target mRNA. No effect on GTP
FT binding."
FT /evidence="ECO:0000269|PubMed:21515746"
FT MUTAGEN 173
FT /note="K->E: Reduced decay of target mRNA. Reduced GTPase
FT activity."
FT /evidence="ECO:0000269|PubMed:21515746"
SQ SEQUENCE 669 AA; 72489 MW; 8A244D3E408E0197 CRC64;
MAAERSRSPV DSPVPASMFA PEPSSPGAAR AAAAAARLHG GFDSDCSEDG EALNGEPELD
LTSKLVLVSP TSEQYDSLLR QMWERMDEGC GETIYVIGQG SDGTEYGLSE ADMEASYATV
KSMAEQIEAD VILLRERQES GGRVRDYLVR KRVGDNDFLE VRVAVVGNVD AGKSTLLGVL
THGELDNGRG FARQKLFRHK HEIESGRTSS VGNDILGFDS EGNVVNKPDS HGGSLEWTKI
CEKSSKVITF IDLAGHEKYL KTTVFGMTGH LPDFCMLMVG SNAGIVGMTK EHLGLALALN
VPVFVVVTKI DMCPANILQE TLKLLQRLLK SPGCRKIPVL VQSKDDVIVT ASNFSSERMC
PIFQISNVTG ENLDLLKMFL NLLSPRTSYR EEEPAEFQID DTYSVPGVGT VVSGTTLRGL
IKLNDTLLLG PDPLGNFLSI AVKSIHRKRM PVKEVRGGQT ASFALKKIKR SSIRKGMVMV
SPRLNPQASW EFEAEILVLH HPTTISPRYQ AMVHCGSIRQ TATILSMDKD CLRTGDKATV
HFRFIKTPEY LHIDQRLVFR EGRTKAVGTI TKLLQTTNNS PMNSKPQQIK MQSTKKGPLS
KREEGGPSGV PAAGPPSTGD EASSLGTTQA ATSSGLQPQP KPSSGGRRRG GQRHKVKSQG
ACVTPASGC
