GPN2_MOUSE
ID GPN2_MOUSE Reviewed; 310 AA.
AC Q8VEJ1; A2A9E9;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 132.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; AL627228; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC018407; AAH18407.1; -; mRNA.
DR CCDS; CCDS18753.1; -.
DR RefSeq; NP_598645.2; NM_133884.2.
DR AlphaFoldDB; Q8VEJ1; -.
DR SMR; Q8VEJ1; -.
DR IntAct; Q8VEJ1; 1.
DR STRING; 10090.ENSMUSP00000030661; -.
DR iPTMnet; Q8VEJ1; -.
DR PhosphoSitePlus; Q8VEJ1; -.
DR EPD; Q8VEJ1; -.
DR MaxQB; Q8VEJ1; -.
DR PaxDb; Q8VEJ1; -.
DR PRIDE; Q8VEJ1; -.
DR ProteomicsDB; 267657; -.
DR Antibodypedia; 30698; 35 antibodies from 12 providers.
DR Ensembl; ENSMUST00000030661; ENSMUSP00000030661; ENSMUSG00000028848.
DR GeneID; 100210; -.
DR KEGG; mmu:100210; -.
DR UCSC; uc008vdb.2; mouse.
DR CTD; 54707; -.
DR MGI; MGI:2140368; Gpn2.
DR VEuPathDB; HostDB:ENSMUSG00000028848; -.
DR eggNOG; KOG1533; Eukaryota.
DR GeneTree; ENSGT00950000183172; -.
DR InParanoid; Q8VEJ1; -.
DR OMA; YAPLPFN; -.
DR OrthoDB; 964931at2759; -.
DR PhylomeDB; Q8VEJ1; -.
DR TreeFam; TF300828; -.
DR BioGRID-ORCS; 100210; 27 hits in 72 CRISPR screens.
DR ChiTaRS; Gpn2; mouse.
DR PRO; PR:Q8VEJ1; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8VEJ1; protein.
DR Bgee; ENSMUSG00000028848; Expressed in animal zygote and 214 other tissues.
DR ExpressionAtlas; Q8VEJ1; baseline and differential.
DR Genevisible; Q8VEJ1; MM.
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; 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 Acetylation; GTP-binding; Hydrolase; Nucleotide-binding;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H9Y4"
FT CHAIN 2..310
FT /note="GPN-loop GTPase 2"
FT /id="PRO_0000247831"
FT MOTIF 76..78
FT /note="Gly-Pro-Asn (GPN)-loop; involved in dimer interface"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT BINDING 19..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT BINDING 178..181
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT SITE 78
FT /note="Stabilizes the phosphate intermediate; shared with
FT dimeric partner"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9Y4"
FT CONFLICT 174
FT /note="I -> V (in Ref. 2; AAH18407)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="A -> T (in Ref. 2; AAH18407)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 310 AA; 34540 MW; 9C3FC9F66E263987 CRC64;
MAGAAPTTAF GQAVIGPPGS GKTTYCLGMS EFLRALGRRV AVVNLDPAND GLPYECAVDV
GELVGLGDVM DALRLGPNGG LLYCMEYLEA NLDWLRAKLE PLRGHYFLFD CPGQVELCTH
HTALRSIFSQ MAQWDLRLTA VHLVDSHYCT DPAKFISVLC TSLATMLHVE LPHINLLSKM
DLIEHYGKLA FNLDYYTEVL DLSYLLEHLA SDPFFRRYRQ LNEKLVQLVE DYSLVSFIPL
NIQDKDSIQR VLQAVDKANG YCFGVQEQRS LEAMMSAAMG ADFHFSSTLG IQEKYLAPSE
QTAEQEAMQL
