GPN2_PIG
ID GPN2_PIG Reviewed; 310 AA.
AC Q58DD9;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RL Submitted (MAR-2005) 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}.
CC -!- CAUTION: Was originally thought to originate from Bos taurus.
CC {ECO:0000305}.
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DR EMBL; BT021658; AAX46505.1; -; mRNA.
DR RefSeq; XP_003127766.1; XM_003127718.3.
DR AlphaFoldDB; Q58DD9; -.
DR SMR; Q58DD9; -.
DR STRING; 9823.ENSSSCP00000003866; -.
DR PaxDb; Q58DD9; -.
DR GeneID; 110255194; -.
DR KEGG; ssc:110255194; -.
DR CTD; 54707; -.
DR eggNOG; KOG1533; Eukaryota.
DR HOGENOM; CLU_037460_0_2_1; -.
DR InParanoid; Q58DD9; -.
DR TreeFam; TF300828; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; Q58DD9; SS.
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_0000247828"
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"
SQ SEQUENCE 310 AA; 34576 MW; 955D42EA83E61474 CRC64;
MAGAAQTTAF GQAVIGPPGS GKTTYCLGMS EFLRALGRRV AVVNLDPANE GLPYECAVDV
GELVGLSDVM DELQLGPNGG LLYCMEYLEA NLDWLRAKLD PLRGHYFLFD CPGQVELCTH
HGALRSIFSQ MTQWDLRLTA VHLVDSHYCT DPAKFISVLC TSLATMLHVE LPHVNLLSKM
DLIEHYGKLA FNLDYYTEVL DLSYLLDHLA SDPFFRHYRQ LNEKLVQLIE DYSLVSFIPL
NIQDKESIQR VLQAVDKANG YCFGVQEQRS LEAMMSAAVG ADFHFSSTLG LQEKYLAPSD
QPVEQEAMQL
