ID   GPN3_RAT                Reviewed;         284 AA.
AC   Q6R518;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 83.
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   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].
RC   STRAIN=Wistar;
RA   Zhou G., Li W., Zhao S.;
RL   Submitted (DEC-2003) 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; AY513752; AAR99706.1; -; mRNA.
DR   RefSeq; NP_973720.1; NM_201991.1.
DR   AlphaFoldDB; Q6R518; -.
DR   SMR; Q6R518; -.
DR   STRING; 10116.ENSRNOP00000001722; -.
DR   jPOST; Q6R518; -.
DR   PaxDb; Q6R518; -.
DR   GeneID; 360810; -.
DR   KEGG; rno:360810; -.
DR   UCSC; RGD:1303034; rat.
DR   CTD; 51184; -.
DR   RGD; 1303034; Gpn3.
DR   eggNOG; KOG1534; Eukaryota.
DR   InParanoid; Q6R518; -.
DR   OrthoDB; 964931at2759; -.
DR   PhylomeDB; Q6R518; -.
DR   PRO; PR:Q6R518; -.
DR   Proteomes; UP000002494; Unplaced.
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_0000304792"
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;  32802 MW;  DC839FA00553D63F CRC64;
     MPRYAQLVMG PAGSGKSTYC STMVQHCEAL NRSVQVVNLD PAAEHFNYPV MADIRELIEV
     DDVMEDDSLR FGPNGGLVFC MEYFANNFDW LENCLGHVED DYILFDCPGQ IELYTHLPVM
     KQLVQQLEQW EFRVCGVFLV DSQFMVESFK FISGILAALS AMISLEIPQV NIMTKMDLLS
     KKAKKEIEKF LDPDMYSLLE DSTGDLRSQK FKKLTKPVCG LVDDYSMVRF LPYDQSDEES
     MNIVLQHIDF AIQYGEDLEF KEPKEHEEES SSMFDEYFQE RQNE