位置:首页 > 蛋白库 > GPN2_RAT
GPN2_RAT
ID   GPN2_RAT                Reviewed;         310 AA.
AC   D4A7C0;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   03-AUG-2022, entry version 65.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AABR03040772; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001257888.1; NM_001270959.1.
DR   AlphaFoldDB; D4A7C0; -.
DR   SMR; D4A7C0; -.
DR   STRING; 10116.ENSRNOP00000009275; -.
DR   PaxDb; D4A7C0; -.
DR   PeptideAtlas; D4A7C0; -.
DR   Ensembl; ENSRNOT00000009275; ENSRNOP00000009275; ENSRNOG00000007083.
DR   GeneID; 362614; -.
DR   KEGG; rno:362614; -.
DR   UCSC; RGD:1311749; rat.
DR   CTD; 54707; -.
DR   RGD; 1311749; Gpn2.
DR   eggNOG; KOG1533; Eukaryota.
DR   GeneTree; ENSGT00950000183172; -.
DR   HOGENOM; CLU_037460_0_2_1; -.
DR   InParanoid; D4A7C0; -.
DR   OMA; YAPLPFN; -.
DR   OrthoDB; 964931at2759; -.
DR   PhylomeDB; D4A7C0; -.
DR   TreeFam; TF300828; -.
DR   PRO; PR:D4A7C0; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000007083; Expressed in spleen and 20 other tissues.
DR   Genevisible; D4A7C0; RN.
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   3: Inferred from homology;
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_0000394804"
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;  34393 MW;  2ABDFD9986A2213F CRC64;
     MAGAAPTTAF GQAVIGPPGS GKTTYCLGMS EFLRALGRRV AVVNLDPANE GLPYECAVDV
     GELVGLGDVM DALRLGPNGG LLYCMEYLEA NLDWLRAKLE PLRGHYFLFD CPGQVELCTH
     HTSLRSIFSQ MAQWDLRLTA VHLVDSHYCT DPAKFISVLC TSLATMLHVE LPHVNLLSKM
     DLIEHYGKLA FNLDYYTEVL DLSYLLDHLA SDPFFSHYRQ LNEKLVQLIE DYSLVSFIPL
     NIQDKDSIQR VLQAVDKANG YCFGVQEQRS LEALMSAAVG ADFHFSSTLG IQEKYLASSD
     QTAEQEAMQL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024