GPN3_BOVIN
ID GPN3_BOVIN Reviewed; 284 AA.
AC Q0P5E2;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=GPN-loop GTPase 3 {ECO:0000250|UniProtKB:Q9UHW5};
DE AltName: Full=ATP-binding domain 1 family member C {ECO:0000250|UniProtKB:Q9UHW5};
GN Name=GPN3 {ECO:0000250|UniProtKB:Q9UHW5};
GN Synonyms=ATPBD1C {ECO:0000250|UniProtKB:Q9UHW5};
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].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Small GTPase required for proper localization of RNA
CC polymerase II (RNAPII). May act at an RNAP assembly step prior to
CC nuclear import. {ECO:0000250|UniProtKB:Q9UHW5}.
CC -!- SUBUNIT: Heterodimer with GPN1. Binds to RNA polymerase II (RNAPII).
CC Interacts directly with subunits RPB4 and RPB7 and the CTD of RPB1.
CC {ECO:0000250|UniProtKB:Q9UHW5}.
CC -!- SIMILARITY: Belongs to the GPN-loop GTPase family. {ECO:0000305}.
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DR EMBL; BC120171; AAI20172.1; -; mRNA.
DR RefSeq; NP_001068740.1; NM_001075272.2.
DR AlphaFoldDB; Q0P5E2; -.
DR SMR; Q0P5E2; -.
DR STRING; 9913.ENSBTAP00000007032; -.
DR PaxDb; Q0P5E2; -.
DR PRIDE; Q0P5E2; -.
DR Ensembl; ENSBTAT00000007032; ENSBTAP00000007032; ENSBTAG00000005347.
DR GeneID; 506597; -.
DR KEGG; bta:506597; -.
DR CTD; 51184; -.
DR VEuPathDB; HostDB:ENSBTAG00000005347; -.
DR VGNC; VGNC:29540; GPN3.
DR eggNOG; KOG1534; Eukaryota.
DR GeneTree; ENSGT00950000183172; -.
DR HOGENOM; CLU_037460_0_0_1; -.
DR InParanoid; Q0P5E2; -.
DR OMA; CFEYLLQ; -.
DR OrthoDB; 964931at2759; -.
DR TreeFam; TF105810; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000005347; Expressed in oocyte and 105 other tissues.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR004130; Gpn.
DR InterPro; IPR030228; Gpn3.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR21231; PTHR21231; 1.
DR PANTHER; PTHR21231:SF7; PTHR21231:SF7; 1.
DR Pfam; PF03029; ATP_bind_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW GTP-binding; Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..284
FT /note="GPN-loop GTPase 3"
FT /id="PRO_0000304789"
FT REGION 261..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 72..74
FT /note="Gly-Pro-Asn (GPN)-loop; involved in dimer interface"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT BINDING 13..18
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT BINDING 174..177
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT SITE 74
FT /note="Stabilizes the phosphate intermediate; shared with
FT dimeric partner"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
SQ SEQUENCE 284 AA; 32691 MW; 7695115663F4EE56 CRC64;
MPRYAQLVMG PAGSGKSTYC ATMVQHCEAL NRSVQVVNLD PAAEHFNYSV MADIRELIEV
DDVMEDSTLQ FGPNGGLVFC MEYFANNFDW LENCLGHVED DYILFDCPGQ IELYTHLPVM
KQLVQQLEQW EFRVCGVFLV DSQFMVESFK FISGILAALS AMISLEIPQV NVMTKMDLLS
KKAKKEIEKF LDPDMYSLLD DSTSDLRSKK FKKLTNAICG LIDDYSMVRF LPYDQSDEES
MNIVLQHIDF AIQYGEDLEF KEPKEHEDES SSMFDEYFQE HQNE