GPN3_MOUSE
ID GPN3_MOUSE Reviewed; 284 AA.
AC Q9D3W4; Q8BU32;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
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}, D5Ertd708e;
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 MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Kidney, Retina, Testis, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NMRI; 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 (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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC40065.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK016996; BAB30544.1; -; mRNA.
DR EMBL; AK080720; BAC37993.1; -; mRNA.
DR EMBL; AK087968; BAC40065.1; ALT_FRAME; mRNA.
DR EMBL; AK146783; BAE27429.1; -; mRNA.
DR EMBL; BC003341; AAH03341.1; -; mRNA.
DR CCDS; CCDS19647.1; -.
DR RefSeq; NP_077178.1; NM_024216.1.
DR AlphaFoldDB; Q9D3W4; -.
DR SMR; Q9D3W4; -.
DR IntAct; Q9D3W4; 4.
DR MINT; Q9D3W4; -.
DR STRING; 10090.ENSMUSP00000031420; -.
DR PhosphoSitePlus; Q9D3W4; -.
DR EPD; Q9D3W4; -.
DR MaxQB; Q9D3W4; -.
DR PaxDb; Q9D3W4; -.
DR PeptideAtlas; Q9D3W4; -.
DR PRIDE; Q9D3W4; -.
DR ProteomicsDB; 271038; -.
DR Antibodypedia; 31008; 63 antibodies from 16 providers.
DR DNASU; 68080; -.
DR Ensembl; ENSMUST00000031420; ENSMUSP00000031420; ENSMUSG00000029464.
DR GeneID; 68080; -.
DR KEGG; mmu:68080; -.
DR UCSC; uc008zle.1; mouse.
DR CTD; 51184; -.
DR MGI; MGI:1289326; Gpn3.
DR VEuPathDB; HostDB:ENSMUSG00000029464; -.
DR eggNOG; KOG1534; Eukaryota.
DR GeneTree; ENSGT00950000183172; -.
DR InParanoid; Q9D3W4; -.
DR OMA; CFEYLLQ; -.
DR OrthoDB; 964931at2759; -.
DR PhylomeDB; Q9D3W4; -.
DR TreeFam; TF105810; -.
DR BioGRID-ORCS; 68080; 27 hits in 56 CRISPR screens.
DR ChiTaRS; Gpn3; mouse.
DR PRO; PR:Q9D3W4; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9D3W4; protein.
DR Bgee; ENSMUSG00000029464; Expressed in morula and 246 other tissues.
DR ExpressionAtlas; Q9D3W4; baseline and differential.
DR Genevisible; Q9D3W4; MM.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
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_0000304791"
FT REGION 262..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; 32790 MW; 96C1BB5BA7283756 CRC64;
MPRYAQLVMG PAGSGKSTYC STMVQHCEAL NRSVQVVNLD PAAEHFNYPV MADIRELIEV
DDVMEDESLR FGPNGGLVFC MEYFANNFDW LENCLGHVED DYILFDCPGQ IELYTHLPVM
KQLVQQLEQW EFRVCGVFLV DSQFMVESFK FISGILAALS AMVSLEIPQV NIMTKMDLLS
KKAKKEIEKF LDPDMYSLID DSTGDLRSQK FKKLTKAVCG LVDDYSMVRF LPYDQSDEES
MNIVLQHIDF AIQYGEDLEF KEPREHEEES SSMFDEYFQE RQNE
