GTPB1_BOVIN
ID GTPB1_BOVIN Reviewed; 669 AA.
AC Q58DC5;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=GTP-binding protein 1;
GN Name=GTPBP1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 440-631 (ISOFORM 1).
RA Baumann R.G., Baldwin R.L., Sonstegard T.S., Van Tassell C.P.,
RA Matukumalli L.K.;
RT "Construction and analysis of a cDNA library generated from intestinal
RT muscle and epithelial tissues of Holstein cattle.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 551-669 (ISOFORM 1).
RA Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y.,
RA Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C.,
RA Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J.,
RA Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J.,
RA Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D., Siddiqui A.,
RA Holt R., Jones S.J., Marra M.A.;
RT "Bovine genome sequencing program: full-length cDNA sequencing.";
RL Submitted (MAR-2006) 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q58DC5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q58DC5-2; Sequence=VSP_026490, VSP_026491;
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=AAX46519.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BT021672; AAX46519.1; ALT_INIT; mRNA.
DR EMBL; CK833772; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; DV883035; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001017938.1; NM_001017938.1.
DR RefSeq; XP_005207379.1; XM_005207322.3. [Q58DC5-1]
DR AlphaFoldDB; Q58DC5; -.
DR SMR; Q58DC5; -.
DR STRING; 9913.ENSBTAP00000013635; -.
DR PaxDb; Q58DC5; -.
DR Ensembl; ENSBTAT00000013635; ENSBTAP00000013635; ENSBTAG00000010324. [Q58DC5-1]
DR GeneID; 513922; -.
DR KEGG; bta:513922; -.
DR CTD; 9567; -.
DR VEuPathDB; HostDB:ENSBTAG00000010324; -.
DR eggNOG; KOG0463; Eukaryota.
DR GeneTree; ENSGT00940000156054; -.
DR InParanoid; Q58DC5; -.
DR OMA; FRFIQRP; -.
DR OrthoDB; 682656at2759; -.
DR TreeFam; TF350446; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000010324; Expressed in retina and 106 other tissues.
DR ExpressionAtlas; Q58DC5; baseline and differential.
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:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0046039; P:GTP metabolic process; ISS:UniProtKB.
DR GO; GO:0061014; P:positive regulation of mRNA catabolic process; ISS: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 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; GTP-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..669
FT /note="GTP-binding protein 1"
FT /id="PRO_0000293472"
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..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..642
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:0000250|UniProtKB:O00178"
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:0000250|UniProtKB:O00178"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00178"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00178"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00178"
FT VAR_SEQ 578..603
FT /note="NNSPMNSKPQQIKMQSTKKGPLPKRE -> SPPSPTLHHSSCVQTTGPLSSP
FT PSNY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16305752"
FT /id="VSP_026490"
FT VAR_SEQ 604..669
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16305752"
FT /id="VSP_026491"
SQ SEQUENCE 669 AA; 72585 MW; 0AD3B7B4115F86DE CRC64;
MAAERSRSPM ESPVPASMFA PEPSSPGAAR AAAAAARLHG GFDSDCSEDG EALNGEPELD
LTSKLVLVSP TSEQYDSLLR QMWERMDEGC GETIYVIGQG SDGTEYGLSE ADMEASYATV
KSMAEQIEAD VILLRERQEA GGRVRDYLVR KRVGDNDFLE VRVAVVGNVD AGKSTLLGVL
THGELDNGRG FARQKLFRHK HEIESGRTSS VGNDILGFDS EGNVVNKPDS HGGSLEWTKI
CEKSTKVITF 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 MQSTKKGPLP
KREEGGPSGG PTVGGPPPGD EACSLGATQL AASSSLQPQP KPSSGGRRRG GQRHKVKSQG
ACMTPASGC
