MOG1_MOUSE
ID MOG1_MOUSE Reviewed; 185 AA.
AC Q9JIB0; Q9CWZ0;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Ran guanine nucleotide release factor;
DE Short=RanGNRF;
DE AltName: Full=Ran-binding protein MOG1;
GN Name=Rangrf; Synonyms=Mog1, Rangnrf;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RAN AND RANBP1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=10811801; DOI=10.1074/jbc.c000252200;
RA Steggerda S.M., Paschal B.M.;
RT "The mammalian Mog1 protein is a guanine nucleotide release factor for
RT Ran.";
RL J. Biol. Chem. 275:23175-23180(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-24; ARG-29; ASP-33;
RP GLU-36 AND ASP-44.
RX PubMed=11733047; DOI=10.1034/j.1600-0854.2001.21109.x;
RA Steggerda S.M., Paschal B.M.;
RT "Identification of a conserved loop in Mog1 that releases GTP from Ran.";
RL Traffic 2:804-811(2001).
RN [6]
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=15716349; DOI=10.1242/dev.01658;
RA Li B., Nair M., Mackay D.R., Bilanchone V., Hu M., Fallahi M., Song H.,
RA Dai Q., Cohen P.E., Dai X.;
RT "Ovol1 regulates meiotic pachytene progression during spermatogenesis by
RT repressing Id2 expression.";
RL Development 132:1463-1473(2005).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SCN5A, AND TISSUE
RP SPECIFICITY.
RX PubMed=18184654; DOI=10.1074/jbc.m709721200;
RA Wu L., Yong S.L., Fan C., Ni Y., Yoo S., Zhang T., Zhang X.,
RA Obejero-Paz C.A., Rho H.J., Ke T., Szafranski P., Jones S.W., Chen Q.,
RA Wang Q.K.;
RT "Identification of a new co-factor, MOG1, required for the full function of
RT cardiac sodium channel Nav1.5.";
RL J. Biol. Chem. 283:6968-6978(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP FUNCTION.
RX PubMed=23420830; DOI=10.1161/circep.111.000206;
RA Chakrabarti S., Wu X., Yang Z., Wu L., Yong S.L., Zhang C., Hu K.,
RA Wang Q.K., Chen Q.;
RT "MOG1 rescues defective trafficking of Na(v)1.5 mutations in Brugada
RT syndrome and sick sinus syndrome.";
RL Circ. Arrhythm. Electrophysiol. 6:392-401(2013).
CC -!- FUNCTION: May regulate the intracellular trafficking of RAN
CC (PubMed:10811801, PubMed:11733047). Promotes guanine nucleotide release
CC from RAN and inhibits binding of new GTP by preventing the binding of
CC the RAN guanine nucleotide exchange factor RCC1 (PubMed:10811801,
CC PubMed:11733047). Regulates the levels of GTP-bound RAN in the nucleus,
CC and thereby plays a role in the regulation of RAN-dependent mitotic
CC spindle dynamics (By similarity). Enhances the expression of SCN5A at
CC the cell membrane in cardiomyocytes (PubMed:18184654, PubMed:23420830).
CC {ECO:0000250|UniProtKB:Q9HD47, ECO:0000269|PubMed:10811801,
CC ECO:0000269|PubMed:11733047, ECO:0000269|PubMed:18184654,
CC ECO:0000269|PubMed:23420830}.
CC -!- SUBUNIT: Monomer (Probable). Interacts with RAN, both RAN-GTP and RAN-
CC GDP (PubMed:10811801). Competes with RCC1 for a common binding site on
CC RAN and thereby inhibits RCC1-mediated nucleotide exchange (By
CC similarity). Forms a complex with RAN-GTP and RANBP1 (PubMed:10811801).
CC Interacts with the cytoplasmic loop 2 of SCN5A (PubMed:18184654).
CC {ECO:0000250|UniProtKB:Q9HD47, ECO:0000269|PubMed:10811801,
CC ECO:0000269|PubMed:18184654, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10811801,
CC ECO:0000269|PubMed:11733047}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q9HD47}. Cytoplasm
CC {ECO:0000269|PubMed:18184654}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9HD47}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9HD47}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9HD47}. Note=Shuttles between the nucleus and
CC cytoplasm. {ECO:0000269|PubMed:11733047}.
CC -!- TISSUE SPECIFICITY: Highgly abundant in cardiac cells. Expressed in
CC testis during prepubertal development. {ECO:0000269|PubMed:18184654}.
CC -!- INDUCTION: Down-regulated in mice lacking Ovol1.
CC {ECO:0000269|PubMed:15716349}.
CC -!- SIMILARITY: Belongs to the MOG1 family. {ECO:0000305}.
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DR EMBL; AF243512; AAF91320.1; -; mRNA.
DR EMBL; AK010288; BAB26824.1; -; mRNA.
DR EMBL; AL603662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC038470; AAH38470.1; -; mRNA.
DR EMBL; BC087921; AAH87921.1; -; mRNA.
DR CCDS; CCDS24875.1; -.
DR RefSeq; NP_001272370.1; NM_001285441.1.
DR RefSeq; NP_001272372.1; NM_001285443.1.
DR RefSeq; NP_067304.1; NM_021329.3.
DR AlphaFoldDB; Q9JIB0; -.
DR SMR; Q9JIB0; -.
DR BioGRID; 208331; 2.
DR IntAct; Q9JIB0; 2.
DR MINT; Q9JIB0; -.
DR STRING; 10090.ENSMUSP00000038485; -.
DR iPTMnet; Q9JIB0; -.
DR PhosphoSitePlus; Q9JIB0; -.
DR EPD; Q9JIB0; -.
DR jPOST; Q9JIB0; -.
DR MaxQB; Q9JIB0; -.
DR PaxDb; Q9JIB0; -.
DR PeptideAtlas; Q9JIB0; -.
DR PRIDE; Q9JIB0; -.
DR ProteomicsDB; 290095; -.
DR Antibodypedia; 24637; 56 antibodies from 18 providers.
DR DNASU; 57785; -.
DR Ensembl; ENSMUST00000038644; ENSMUSP00000038485; ENSMUSG00000032892.
DR GeneID; 57785; -.
DR KEGG; mmu:57785; -.
DR UCSC; uc007jor.2; mouse.
DR CTD; 29098; -.
DR MGI; MGI:1889073; Rangrf.
DR VEuPathDB; HostDB:ENSMUSG00000032892; -.
DR eggNOG; KOG3329; Eukaryota.
DR GeneTree; ENSGT00390000013834; -.
DR HOGENOM; CLU_081345_2_1_1; -.
DR InParanoid; Q9JIB0; -.
DR OMA; QCVSKFN; -.
DR OrthoDB; 1579830at2759; -.
DR PhylomeDB; Q9JIB0; -.
DR TreeFam; TF332074; -.
DR Reactome; R-MMU-5576892; Phase 0 - rapid depolarisation.
DR BioGRID-ORCS; 57785; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Rangrf; mouse.
DR PRO; PR:Q9JIB0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9JIB0; protein.
DR Bgee; ENSMUSG00000032892; Expressed in spermatid and 67 other tissues.
DR Genevisible; Q9JIB0; MM.
DR GO; GO:0005901; C:caveola; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0014704; C:intercalated disc; IDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:MGI.
DR GO; GO:0031267; F:small GTPase binding; IDA:MGI.
DR GO; GO:0017080; F:sodium channel regulator activity; IMP:BHF-UCL.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISO:MGI.
DR GO; GO:0060047; P:heart contraction; IBA:GO_Central.
DR GO; GO:0006913; P:nucleocytoplasmic transport; TAS:MGI.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; ISO:MGI.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0032527; P:protein exit from endoplasmic reticulum; ISO:MGI.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR GO; GO:0098905; P:regulation of bundle of His cell action potential; ISO:MGI.
DR GO; GO:0098909; P:regulation of cardiac muscle cell action potential involved in regulation of contraction; ISO:MGI.
DR GO; GO:0003254; P:regulation of membrane depolarization; IMP:BHF-UCL.
DR GO; GO:1900825; P:regulation of membrane depolarization during cardiac muscle cell action potential; ISO:MGI.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:MGI.
DR GO; GO:0090226; P:regulation of microtubule nucleation by Ran protein signal transduction; ISO:MGI.
DR GO; GO:1902305; P:regulation of sodium ion transmembrane transport; IMP:BHF-UCL.
DR GO; GO:2000649; P:regulation of sodium ion transmembrane transporter activity; IMP:BHF-UCL.
DR CDD; cd00224; Mog1; 1.
DR InterPro; IPR007681; Mog1.
DR InterPro; IPR016123; Mog1/PsbP_a/b/a-sand.
DR PANTHER; PTHR15837; PTHR15837; 1.
DR Pfam; PF04603; Mog1; 1.
DR SUPFAM; SSF55724; SSF55724; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Guanine-nucleotide releasing factor; Membrane;
KW Nucleus; Protein transport; Reference proteome; Transport.
FT CHAIN 1..185
FT /note="Ran guanine nucleotide release factor"
FT /id="PRO_0000330637"
FT REGION 27..70
FT /note="Interaction with RAN"
FT /evidence="ECO:0000250|UniProtKB:Q9HD47"
FT MUTAGEN 24
FT /note="D->A: Deficient in binding to RAN-GTP and in GTP
FT release activity."
FT /evidence="ECO:0000269|PubMed:11733047"
FT MUTAGEN 29
FT /note="R->A: Increases GTP release from RAN."
FT /evidence="ECO:0000269|PubMed:11733047"
FT MUTAGEN 33
FT /note="D->A: Deficient in binding to RAN-GTP and in GTP
FT release activity."
FT /evidence="ECO:0000269|PubMed:11733047"
FT MUTAGEN 36
FT /note="E->A: Deficient in binding to RAN-GTP and in GTP
FT release activity."
FT /evidence="ECO:0000269|PubMed:11733047"
FT MUTAGEN 44
FT /note="D->A: Increases GTP release from RAN."
FT /evidence="ECO:0000269|PubMed:11733047"
FT CONFLICT 62..63
FT /note="AA -> RG (in Ref. 2; BAB26824)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 185 AA; 20413 MW; 4526DD06C7D3190B CRC64;
MEPNRNCPLF GGAFSAILPT GAIDVSDLRP VPDNQEVFCH PVTDQSLIIE LLELQAHVQG
EAAARYHFED VGRVQGARAV HVLSVQPLCL ENLSLRGCCQ DAWSLSGKQQ VAKENQQVAK
DVTLHQALLR LPQYQTDLLL TFNQPPCHSR SLGPENLSCP PWSLSNFEQL VTSLTLHDPN
LFGPQ
