GPN1_CAEEL
ID GPN1_CAEEL Reviewed; 355 AA.
AC P46577;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=GPN-loop GTPase 1 {ECO:0000250|UniProtKB:Q9HCN4};
DE EC=3.6.5.- {ECO:0000250|UniProtKB:Q9HCN4};
DE AltName: Full=Gro-1 operon protein 2 {ECO:0000312|WormBase:C34E10.2};
DE AltName: Full=XPA-binding protein 1 homolog {ECO:0000250|UniProtKB:Q9HCN4};
GN Name=gop-2 {ECO:0000312|WormBase:C34E10.2}; ORFNames=C34E10.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Bristol N2;
RX PubMed=11560893; DOI=10.1093/genetics/159.1.147;
RA Lemieux J., Lakowski B., Webb A., Meng Y., Ubach A., Bussiere F.,
RA Barnes T., Hekimi S.;
RT "Regulation of physiological rates in Caenorhabditis elegans by a tRNA-
RT modifying enzyme in the mitochondria.";
RL Genetics 159:147-157(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Small GTPase required for proper nuclear import of RNA
CC polymerase II (RNAPII). May act at an RNAP assembly step prior to
CC nuclear import. {ECO:0000250|UniProtKB:Q9HCN4}.
CC -!- SUBUNIT: Heterodimer with GPN3. Binds to RNA polymerase II (RNAPII).
CC {ECO:0000250|UniProtKB:Q9HCN4}.
CC -!- INTERACTION:
CC P46577; Q9XW68: CELE_Y75B8A.14; NbExp=3; IntAct=EBI-316619, EBI-316631;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9HCN4}. Nucleus
CC {ECO:0000250|UniProtKB:Q9HCN4}. Note=Shuttles between the nucleus and
CC the cytoplasm. {ECO:0000250|UniProtKB:Q9HCN4}.
CC -!- SIMILARITY: Belongs to the GPN-loop GTPase family. {ECO:0000305}.
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DR EMBL; AY052770; AAL14109.1; -; mRNA.
DR EMBL; FO080774; CCD66646.1; -; Genomic_DNA.
DR PIR; T15759; T15759.
DR RefSeq; NP_498118.1; NM_065717.5.
DR AlphaFoldDB; P46577; -.
DR SMR; P46577; -.
DR BioGRID; 40953; 5.
DR DIP; DIP-24754N; -.
DR IntAct; P46577; 2.
DR STRING; 6239.C34E10.2; -.
DR EPD; P46577; -.
DR PaxDb; P46577; -.
DR PeptideAtlas; P46577; -.
DR EnsemblMetazoa; C34E10.2.1; C34E10.2.1; WBGene00001661.
DR GeneID; 175722; -.
DR KEGG; cel:CELE_C34E10.2; -.
DR UCSC; C34E10.2; c. elegans.
DR CTD; 175722; -.
DR WormBase; C34E10.2; CE01182; WBGene00001661; gop-2.
DR eggNOG; KOG1532; Eukaryota.
DR GeneTree; ENSGT00950000183172; -.
DR HOGENOM; CLU_037460_1_0_1; -.
DR InParanoid; P46577; -.
DR OMA; MIIVFNK; -.
DR OrthoDB; 1096688at2759; -.
DR PhylomeDB; P46577; -.
DR PRO; PR:P46577; -.
DR Proteomes; UP000001940; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IPR030230; Gpn1/Npa3/XAB1.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR21231; PTHR21231; 1.
DR PANTHER; PTHR21231:SF8; PTHR21231:SF8; 1.
DR Pfam; PF03029; ATP_bind_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; GTP-binding; Hydrolase; Nucleotide-binding;
KW Nucleus; Reference proteome.
FT CHAIN 1..355
FT /note="GPN-loop GTPase 1"
FT /id="PRO_0000087541"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 286..311
FT /evidence="ECO:0000255"
FT MOTIF 97..99
FT /note="Gly-Pro-Asn (GPN)-loop; involved in dimer interface"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT COMPBIAS 9..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 40..45
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT BINDING 200..203
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT SITE 99
FT /note="Stabilizes the phosphate intermediate; shared with
FT dimeric partner"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
SQ SEQUENCE 355 AA; 39657 MW; B4534B08CD0AB3DD CRC64;
MAEKAENLPS SSAEASEEPS PQTGPNVNQK PSILVLGMAG SGKTTFVQRL TAFLHARKTP
PYVINLDPAV SKVPYPVNVD IRDTVKYKEV MKEFGMGPNG AIMTCLNLMC TRFDKVIELI
NKRSSDFSVC LLDTPGQIEA FTWSASGSII TDSLASSHPT VVMYIVDSAR ATNPTTFMSN
MLYACSILYR TKLPFIVVFN KADIVKPTFA LKWMQDFERF DEALEDARSS YMNDLSRSLS
LVLDEFYCGL KTVCVSSATG EGFEDVMTAI DESVEAYKKE YVPMYEKVLA EKKLLDEEER
KKRDEETLKG KAVHDLNKVA NPDEFLESEL NSKIDRIHLG GVDEENEEDA ELERS
