ID   GPN3_XENLA              Reviewed;         285 AA.
AC   Q4V7Z0;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 57.
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   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2005) 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       {ECO:0000250|UniProtKB:Q9UHW5}.
CC   -!- SIMILARITY: Belongs to the GPN-loop GTPase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC097651; AAH97651.1; -; mRNA.
DR   RefSeq; NP_001089469.1; NM_001096000.1.
DR   AlphaFoldDB; Q4V7Z0; -.
DR   SMR; Q4V7Z0; -.
DR   BioGRID; 592301; 2.
DR   IntAct; Q4V7Z0; 1.
DR   MaxQB; Q4V7Z0; -.
DR   DNASU; 734520; -.
DR   GeneID; 734520; -.
DR   KEGG; xla:734520; -.
DR   CTD; 734520; -.
DR   Xenbase; XB-GENE-973722; gpn3.L.
DR   OMA; CFEYLLQ; -.
DR   OrthoDB; 964931at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 734520; Expressed in blastula and 19 other tissues.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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..285
FT                   /note="GPN-loop GTPase 3"
FT                   /id="PRO_0000304794"
FT   REGION          261..285
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   285 AA;  33058 MW;  AE582D40267A0003 CRC64;
     MPRYAQLVMG PAGSGKSTYC STMVQHCETL NRSVQVVNLD PAAEHFDYPV LADIRELIEV
     DDVMEDRSLR FGPNGGLVYC MEYFANNFDW LESCLGHTED DYILFDCPGQ IELYTHLPVM
     KYLVEQLQQW EFRVCGVFLV DSQFMVESFK FLSGVLAALS AMVSLEIPQC NIMTKMDLLS
     KKAKKEIEKF LDPDMYSMIE DTPSRFKSTK FKKLTEALCG LVDDYSMVRF LPFDRSDEEC
     MNIVLQHIDF AIQYGEDLEF KEPRENEEDK SENFDEYFQD RTDES