GPN1_BOVIN
ID GPN1_BOVIN Reviewed; 373 AA.
AC A4FUD1;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=GPN-loop GTPase 1 {ECO:0000250|UniProtKB:Q9HCN4};
DE EC=3.6.5.- {ECO:0000250|UniProtKB:Q9HCN4};
DE AltName: Full=XPA-binding protein 1 {ECO:0000250|UniProtKB:Q9HCN4};
GN Name=GPN1 {ECO:0000250|UniProtKB:Q9HCN4};
GN Synonyms=XAB1 {ECO:0000250|UniProtKB:Q9HCN4};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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. Forms an interface between the RNA polymerase II enzyme
CC and chaperone/scaffolding proteins, suggesting that it is required to
CC connect RNA polymerase II to regulators of protein complex formation.
CC May be involved in nuclear localization of XPA.
CC {ECO:0000250|UniProtKB:Q9HCN4}.
CC -!- SUBUNIT: Heterodimer with GPN3. Binds to RNA polymerase II (RNAPII).
CC Interacts directly with RNAPII subunits RPB4 and RPB7 and the CTD of
CC RPB1. Interacts with XPA. {ECO:0000250|UniProtKB:Q9HCN4}.
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; BC114712; AAI14713.1; -; mRNA.
DR RefSeq; NP_001076861.1; NM_001083392.1.
DR AlphaFoldDB; A4FUD1; -.
DR SMR; A4FUD1; -.
DR STRING; 9913.ENSBTAP00000005098; -.
DR PaxDb; A4FUD1; -.
DR PRIDE; A4FUD1; -.
DR Ensembl; ENSBTAT00000005098; ENSBTAP00000005098; ENSBTAG00000003904.
DR GeneID; 508522; -.
DR KEGG; bta:508522; -.
DR CTD; 11321; -.
DR VEuPathDB; HostDB:ENSBTAG00000003904; -.
DR VGNC; VGNC:29538; GPN1.
DR eggNOG; KOG1532; Eukaryota.
DR GeneTree; ENSGT00950000183172; -.
DR HOGENOM; CLU_037460_1_2_1; -.
DR InParanoid; A4FUD1; -.
DR OMA; MIIVFNK; -.
DR OrthoDB; 1096688at2759; -.
DR TreeFam; TF313204; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000003904; Expressed in olfactory segment of nasal mucosa and 105 other tissues.
DR ExpressionAtlas; A4FUD1; baseline.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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; IPR003593; AAA+_ATPase.
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 SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; GTP-binding; Hydrolase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9HCN4"
FT CHAIN 2..373
FT /note="GPN-loop GTPase 1"
FT /id="PRO_0000330934"
FT REGION 304..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 86..88
FT /note="Gly-Pro-Asn (GPN)-loop; involved in dimer interface"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT COMPBIAS 304..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 29..34
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT BINDING 189..192
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT SITE 88
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:Q9HCN4"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCN4"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCN4"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCN4"
FT MOD_RES 328
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCN4"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCN4"
FT MOD_RES 340
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCN4"
SQ SEQUENCE 373 AA; 41450 MW; 4FA0B8B9FB696A84 CRC64;
MAAPASATES QASGGPRPPA CLLVLGMAGS GKTTFVQRLT GYLHSQGCPP YVINLDPAVH
EVPFPANIDI RDTVKYKEVM KQYGLGPNGG IVTSLNLFAT RFDQVMKFIE KAQNMSKYVL
IDTPGQIEVF TWSASGTIIT EALASSFPTI VIYVMDTSRS TNPVTFMSNM LYACSILYKT
KLPFIVVMNK TDIIDHSFAV EWMQDFEAFQ DALNQETTYV SNLTRSMSLV LDEFYSSLRV
VGVSAVLGTG LDELFVQVAS ATEEYEREYR PEYERLKKSL ASAQSQQQKE QLERLQKDMG
SVALDTGTAT GSSSPVLDPS DLILTRGTLD EEDEEADSDT DDIDHRVTEE SREEPAFQNF
MQESMAQYWK KNK
