GPN2_SCHPO
ID GPN2_SCHPO Reviewed; 315 AA.
AC Q9UTL7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=GPN-loop GTPase 2 {ECO:0000250|UniProtKB:Q08726};
DE EC=3.6.5.- {ECO:0000250|UniProtKB:Q08726};
DE AltName: Full=ATP-binding domain 1 family member B homolog {ECO:0000250|UniProtKB:Q9H9Y4};
GN Name=gpn2 {ECO:0000250|UniProtKB:Q08726};
GN ORFNames=SPAC144.07c {ECO:0000312|PomBase:SPAC144.07c};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Small GTPase required for proper nuclear import 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 fet5/gpn3. Binds to RNA polymerase
CC II (RNAPII). {ECO:0000250|UniProtKB:Q08726}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the GPN-loop GTPase family. {ECO:0000305}.
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DR EMBL; CU329670; CAB59687.1; -; Genomic_DNA.
DR PIR; T37674; T37674.
DR RefSeq; NP_594668.1; NM_001020097.2.
DR AlphaFoldDB; Q9UTL7; -.
DR SMR; Q9UTL7; -.
DR BioGRID; 279343; 2.
DR STRING; 4896.SPAC144.07c.1; -.
DR MaxQB; Q9UTL7; -.
DR PaxDb; Q9UTL7; -.
DR PRIDE; Q9UTL7; -.
DR EnsemblFungi; SPAC144.07c.1; SPAC144.07c.1:pep; SPAC144.07c.
DR GeneID; 2542899; -.
DR KEGG; spo:SPAC144.07c; -.
DR PomBase; SPAC144.07c; gpn2.
DR VEuPathDB; FungiDB:SPAC144.07c; -.
DR eggNOG; KOG1533; Eukaryota.
DR HOGENOM; CLU_037460_0_2_1; -.
DR InParanoid; Q9UTL7; -.
DR OMA; YAPLPFN; -.
DR PhylomeDB; Q9UTL7; -.
DR PRO; PR:Q9UTL7; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISM:PomBase.
DR GO; GO:0006606; P:protein import into nucleus; ISO:PomBase.
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 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..315
FT /note="GPN-loop GTPase 2"
FT /id="PRO_0000315978"
FT MOTIF 69..71
FT /note="Gly-Pro-Asn (GPN)-loop; involved in dimer interface"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT BINDING 12..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT BINDING 172..175
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT SITE 71
FT /note="Stabilizes the phosphate intermediate; shared with
FT dimeric partner"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
SQ SEQUENCE 315 AA; 35728 MW; 50B55E966907F770 CRC64;
MPFCQVVVGP PGSGKSTYCF GMYQLLSAIG RSSIIVNLDP ANDFIKYPCA IDIRKVLDVE
MIQKDYDLGP NGALIYAMEA IEYHVEWLLK ELKKHRDSYV IFDCPGQVEL FTNHNSLQKI
IKTLEKELDY RPVSVQLVDA YCCTNPSAYV SALLVCLKGM LQLDMPHVNI LSKADLLCTY
GTLPMKLDFF TEVQDLSYLA PLLDRDKRLQ RYSDLNKAIC ELVEDFNLVS FEVVAVENKA
SMLRVLRKID QAGGYAYGST EIGGDAVWVN AVRQGGDPLQ GISPQERWID KKEEYDKYEW
ELEQKSTMDE DENEG
