GPN2_XENLA
ID GPN2_XENLA Reviewed; 318 AA.
AC Q66KF6; Q7ZYS2;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=GPN-loop GTPase 2 {ECO:0000250|UniProtKB:Q9H9Y4};
DE AltName: Full=ATP-binding domain 1 family member B {ECO:0000250|UniProtKB:Q9H9Y4};
GN Name=gpn2 {ECO:0000250|UniProtKB:Q9H9Y4};
GN Synonyms=atpbd1b {ECO:0000250|UniProtKB:Q9H9Y4};
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=Kidney;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Small GTPase required for proper localization of RNA
CC polymerase II and III (RNAPII and RNAPIII). May act at an RNAP assembly
CC step prior to nuclear import. {ECO:0000250|UniProtKB:Q08726}.
CC -!- SUBUNIT: Heterodimers with gpn1 or gpn3. Binds to RNA polymerase II
CC (RNAPII). {ECO:0000250|UniProtKB:Q08726, ECO:0000250|UniProtKB:Q9H9Y4}.
CC -!- SIMILARITY: Belongs to the GPN-loop GTPase family. {ECO:0000305}.
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DR EMBL; BC041519; AAH41519.1; -; mRNA.
DR EMBL; BC080422; AAH80422.1; -; mRNA.
DR RefSeq; NP_001082424.1; NM_001088955.1.
DR AlphaFoldDB; Q66KF6; -.
DR SMR; Q66KF6; -.
DR BioGRID; 99792; 1.
DR IntAct; Q66KF6; 1.
DR DNASU; 398460; -.
DR GeneID; 398460; -.
DR KEGG; xla:398460; -.
DR CTD; 398460; -.
DR Xenbase; XB-GENE-5751928; gpn2.S.
DR OrthoDB; 964931at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 398460; Expressed in egg cell 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; IPR030231; Gpn2.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR21231; PTHR21231; 1.
DR PANTHER; PTHR21231:SF3; PTHR21231:SF3; 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..318
FT /note="GPN-loop GTPase 2"
FT /id="PRO_0000247833"
FT MOTIF 85..87
FT /note="Gly-Pro-Asn (GPN)-loop; involved in dimer interface"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT BINDING 29..34
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT BINDING 187..190
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT SITE 87
FT /note="Stabilizes the phosphate intermediate; shared with
FT dimeric partner"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
SQ SEQUENCE 318 AA; 35346 MW; D34B317B808C4983 CRC64;
MADACSEMDR GAEKYPLLGF GQAVIGPPGS GKSTYVRAMQ ALLARMGRKS AIINLDPAGE
DEPGAAVSLR ELLGLEEVMS ELRLGPNGSL LYCMEYLQEN LDWLRARLQG LRGTYLLLDC
PGQVELYTHH PALPDILRRL GGWGLRLCAV HLVDSHYCTD PAKFISVLCT SLSTMLHVEL
PHINVLSKMD LIEQYGRLAF NLDYYTEVMD LSFLVEQLTS DPFFRRHKRL HEKLAGVIED
YGLVTFMPLS IKDDKSLQLV LSAVDKASGF CFGEAKQSLG NLMSVAVGAD FQFTSTLAFQ
EKYVENDGRT VEEETLDL