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Ran guanine nucleotide release factor (RanGNRF) (Ran-binding protein MOG1)

 MOG1_MOUSE              Reviewed;         185 AA.
Q9JIB0; Q9CWZ0;
29-APR-2008, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
28-FEB-2018, entry version 119.
RecName: Full=Ran guanine nucleotide release factor;
Short=RanGNRF;
AltName: Full=Ran-binding protein MOG1;
Name=Rangrf; Synonyms=Mog1, Rangnrf;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RAN AND RANBP1,
AND SUBCELLULAR LOCATION.
PubMed=10811801; DOI=10.1074/jbc.C000252200;
Steggerda S.M., Paschal B.M.;
"The mammalian Mog1 protein is a guanine nucleotide release factor for
Ran.";
J. Biol. Chem. 275:23175-23180(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary tumor, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-24; ARG-29;
ASP-33; GLU-36 AND ASP-44.
PubMed=11733047; DOI=10.1034/j.1600-0854.2001.21109.x;
Steggerda S.M., Paschal B.M.;
"Identification of a conserved loop in Mog1 that releases GTP from
Ran.";
Traffic 2:804-811(2001).
[6]
DEVELOPMENTAL STAGE, AND INDUCTION.
PubMed=15716349; DOI=10.1242/dev.01658;
Li B., Nair M., Mackay D.R., Bilanchone V., Hu M., Fallahi M.,
Song H., Dai Q., Cohen P.E., Dai X.;
"Ovol1 regulates meiotic pachytene progression during spermatogenesis
by repressing Id2 expression.";
Development 132:1463-1473(2005).
[7]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SCN5A, AND TISSUE
SPECIFICITY.
PubMed=18184654; DOI=10.1074/jbc.M709721200;
Wu L., Yong S.L., Fan C., Ni Y., Yoo S., Zhang T., Zhang X.,
Obejero-Paz C.A., Rho H.J., Ke T., Szafranski P., Jones S.W., Chen Q.,
Wang Q.K.;
"Identification of a new co-factor, MOG1, required for the full
function of cardiac sodium channel Nav1.5.";
J. Biol. Chem. 283:6968-6978(2008).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
FUNCTION.
PubMed=23420830; DOI=10.1161/CIRCEP.111.000206;
Chakrabarti S., Wu X., Yang Z., Wu L., Yong S.L., Zhang C., Hu K.,
Wang Q.K., Chen Q.;
"MOG1 rescues defective trafficking of Na(v)1.5 mutations in Brugada
syndrome and sick sinus syndrome.";
Circ. Arrhythm. Electrophysiol. 6:392-401(2013).
-!- FUNCTION: May regulate the intracellular trafficking of RAN
(PubMed:10811801, PubMed:11733047). Promotes guanine nucleotide
release from RAN and inhibits binding of new GTP by preventing the
binding of the RAN guanine nucleotide exchange factor RCC1
(PubMed:10811801, PubMed:11733047). Regulates the levels of GTP-
bound RAN in the nucleus, and thereby plays a role in the
regulation of RAN-dependent mitotic spindle dynamics (By
similarity). Enhances the expression of SCN5A at the cell membrane
in cardiomyocytes (PubMed:18184654, PubMed:23420830).
{ECO:0000250|UniProtKB:Q9HD47, ECO:0000269|PubMed:10811801,
ECO:0000269|PubMed:11733047, ECO:0000269|PubMed:18184654,
ECO:0000269|PubMed:23420830}.
-!- SUBUNIT: Monomer (Probable). Interacts with RAN, both RAN-GTP and
RAN-GDP (PubMed:10811801). Competes with RCC1 for a common binding
site on RAN and thereby inhibits RCC1-mediated nucleotide exchange
(By similarity). Forms a complex with RAN-GTP and RANBP1
(PubMed:10811801). Interacts with the cytoplasmic loop 2 of SCN5A
(PubMed:18184654). {ECO:0000250|UniProtKB:Q9HD47,
ECO:0000269|PubMed:10811801, ECO:0000269|PubMed:18184654,
ECO:0000305}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10811801,
ECO:0000269|PubMed:11733047}. Cytoplasm, perinuclear region
{ECO:0000250|UniProtKB:Q9HD47}. Cytoplasm
{ECO:0000269|PubMed:18184654}. Cell membrane
{ECO:0000250|UniProtKB:Q9HD47}; Peripheral membrane protein
{ECO:0000250|UniProtKB:Q9HD47}; Cytoplasmic side
{ECO:0000250|UniProtKB:Q9HD47}. Note=Shuttles between the nucleus
and cytoplasm. {ECO:0000269|PubMed:11733047}.
-!- TISSUE SPECIFICITY: Highgly abundant in cardiac cells. Expressed
in testis during prepubertal development.
{ECO:0000269|PubMed:18184654}.
-!- INDUCTION: Down-regulated in mice lacking Ovol1.
{ECO:0000269|PubMed:15716349}.
-!- SIMILARITY: Belongs to the MOG1 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF243512; AAF91320.1; -; mRNA.
EMBL; AK010288; BAB26824.1; -; mRNA.
EMBL; AL603662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC038470; AAH38470.1; -; mRNA.
EMBL; BC087921; AAH87921.1; -; mRNA.
CCDS; CCDS24875.1; -.
RefSeq; NP_001272370.1; NM_001285441.1.
RefSeq; NP_001272372.1; NM_001285443.1.
RefSeq; NP_067304.1; NM_021329.3.
UniGene; Mm.143774; -.
UniGene; Mm.371612; -.
ProteinModelPortal; Q9JIB0; -.
SMR; Q9JIB0; -.
IntAct; Q9JIB0; 1.
MINT; Q9JIB0; -.
STRING; 10090.ENSMUSP00000038485; -.
iPTMnet; Q9JIB0; -.
PhosphoSitePlus; Q9JIB0; -.
EPD; Q9JIB0; -.
MaxQB; Q9JIB0; -.
PaxDb; Q9JIB0; -.
PeptideAtlas; Q9JIB0; -.
PRIDE; Q9JIB0; -.
Ensembl; ENSMUST00000038644; ENSMUSP00000038485; ENSMUSG00000032892.
GeneID; 57785; -.
KEGG; mmu:57785; -.
UCSC; uc007jor.2; mouse.
CTD; 29098; -.
MGI; MGI:1889073; Rangrf.
eggNOG; KOG3329; Eukaryota.
eggNOG; ENOG4111I9Z; LUCA.
GeneTree; ENSGT00390000013834; -.
HOGENOM; HOG000247047; -.
HOVERGEN; HBG075266; -.
InParanoid; Q9JIB0; -.
OMA; NQPPPDN; -.
OrthoDB; EOG091G0KIN; -.
PhylomeDB; Q9JIB0; -.
TreeFam; TF332074; -.
Reactome; R-MMU-5576892; Phase 0 - rapid depolarisation.
ChiTaRS; Rangrf; mouse.
PRO; PR:Q9JIB0; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000032892; -.
Genevisible; Q9JIB0; MM.
GO; GO:0005901; C:caveola; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0014704; C:intercalated disc; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005791; C:rough endoplasmic reticulum; ISO:MGI.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:MGI.
GO; GO:0044325; F:ion channel binding; IPI:BHF-UCL.
GO; GO:0008565; F:protein transporter activity; ISO:MGI.
GO; GO:0008536; F:Ran GTPase binding; IDA:MGI.
GO; GO:0005087; F:Ran guanyl-nucleotide exchange factor activity; IDA:MGI.
GO; GO:0017080; F:sodium channel regulator activity; IMP:BHF-UCL.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; ISO:MGI.
GO; GO:0006913; P:nucleocytoplasmic transport; TAS:MGI.
GO; GO:2000010; P:positive regulation of protein localization to cell surface; ISO:MGI.
GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:MGI.
GO; GO:0032527; P:protein exit from endoplasmic reticulum; ISO:MGI.
GO; GO:0098905; P:regulation of bundle of His cell action potential; ISO:MGI.
GO; GO:0098909; P:regulation of cardiac muscle cell action potential involved in regulation of contraction; ISO:MGI.
GO; GO:0003254; P:regulation of membrane depolarization; IMP:BHF-UCL.
GO; GO:1900825; P:regulation of membrane depolarization during cardiac muscle cell action potential; ISO:MGI.
GO; GO:0042391; P:regulation of membrane potential; ISO:MGI.
GO; GO:0090226; P:regulation of microtubule nucleation by Ran protein signal transduction; ISO:MGI.
GO; GO:1902305; P:regulation of sodium ion transmembrane transport; IMP:BHF-UCL.
GO; GO:2000649; P:regulation of sodium ion transmembrane transporter activity; IMP:BHF-UCL.
CDD; cd00224; Mog1; 1.
Gene3D; 3.40.1000.10; -; 1.
InterPro; IPR007681; Mog1.
InterPro; IPR016123; Mog1/PsbP_a/b/a-sand.
PANTHER; PTHR15837; PTHR15837; 1.
Pfam; PF04603; Mog1; 1.
SUPFAM; SSF55724; SSF55724; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Cytoplasm;
Guanine-nucleotide releasing factor; Membrane; Nucleus;
Protein transport; Reference proteome; Transport.
CHAIN 1 185 Ran guanine nucleotide release factor.
/FTId=PRO_0000330637.
REGION 27 70 Interaction with RAN.
{ECO:0000250|UniProtKB:Q9HD47}.
MUTAGEN 24 24 D->A: Deficient in binding to RAN-GTP and
in GTP release activity.
{ECO:0000269|PubMed:11733047}.
MUTAGEN 29 29 R->A: Increases GTP release from RAN.
{ECO:0000269|PubMed:11733047}.
MUTAGEN 33 33 D->A: Deficient in binding to RAN-GTP and
in GTP release activity.
{ECO:0000269|PubMed:11733047}.
MUTAGEN 36 36 E->A: Deficient in binding to RAN-GTP and
in GTP release activity.
{ECO:0000269|PubMed:11733047}.
MUTAGEN 44 44 D->A: Increases GTP release from RAN.
{ECO:0000269|PubMed:11733047}.
CONFLICT 62 63 AA -> RG (in Ref. 2; BAB26824).
{ECO:0000305}.
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


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