ID   GTPB1_PONAB             Reviewed;         602 AA.
AC   Q5R8Q7;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=GTP-binding protein 1;
DE   Flags: Fragment;
GN   Name=GTPBP1;
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=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with EXOSC2/RRP4, EXOSC3/RRP40, EXOSC5/RRP46,
CC       HNRNPD, HNRNPR and SYNCRIP. Identified in a complex with AANAT mRNA,
CC       but does not bind mRNA by itself (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAH91853.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CR859694; CAH91853.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001126073.1; NM_001132601.1.
DR   AlphaFoldDB; Q5R8Q7; -.
DR   SMR; Q5R8Q7; -.
DR   STRING; 9601.ENSPPYP00000013394; -.
DR   GeneID; 100173025; -.
DR   KEGG; pon:100173025; -.
DR   CTD; 9567; -.
DR   eggNOG; KOG0463; Eukaryota.
DR   InParanoid; Q5R8Q7; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0000177; C:cytoplasmic exosome (RNase complex); ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0046039; P:GTP metabolic process; ISS:UniProtKB.
DR   GO; GO:0061014; P:positive regulation of mRNA catabolic process; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Cytoplasm; GTP-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           <1..602
FT                   /note="GTP-binding protein 1"
FT                   /id="PRO_0000122471"
FT   DOMAIN          91..322
FT                   /note="tr-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          100..107
FT                   /note="G1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          139..143
FT                   /note="G2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          185..188
FT                   /note="G3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          241..244
FT                   /note="G4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          299..301
FT                   /note="G5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          506..602
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        506..528
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        561..575
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         100..107
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         185..189
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         241..244
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00178"
FT   MOD_RES         513
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00178"
FT   NON_TER         1
SQ   SEQUENCE   602 AA;  65637 MW;  767ADD2642F30E20 CRC64;
     VSPTSEQYDS LLRQMWERMD EGCGGTIYVI GQGSDGTEYG LSEADMEASY ATVKSMAEQI
     EADVILLRER QEAGGRVRDY LVRKRVGDND FLEVRVAVVG NVDAGKSTLL GVLTHGELDN
     GRGFARQKLF RHKHEIESGR TSSVGNDILG FDSEGNVVNK PDSHGGSLEW TKICEKSTKV
     ITFIDLAGHE KYLKTTVFGM TGHLPDFCML MVGSNAGIVG MTKEHLGLAL ALNVPVFVVV
     TKIDMCPANI LQETLKLLQR LLKSPGCRKI PVLVQSKDDV IVTASNFSSE RMCPIFQISN
     VTGENLDLLK MFLNLLSPRT SYREEEPAEF QIDDTYSVPG VGTVVSGTTL RGLIKLNDTL
     LLGPDPLGNF LSIAVKSIHR KRMPVKEVRG GQTASFALKK IKRSSIRKGM VMVSPRLNPQ
     ASWEFEAEIL VLHHPTTISP RYQAMVHCGS IRQTATILSM DKDCLRTGDK ATVHFRFIKT
     PEYLHIDQRL VFREGRTKAV GTITKLLQTT NNSPMNSKPQ QIKMQSTKKG PLTKRDEGGP
     SGGPAVGAPP PGDEASSLGA GQPAASCNLQ PQPKPSSGGR RRGGQRYKVK SQGACVTPAS
     GC