ID MOG1_HUMAN Reviewed; 186 AA. AC Q9HD47; D3DTR6; Q68DI3; Q9BR68; Q9HD48; Q9NRU9; Q9P001; Q9P0P2; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 147. DE RecName: Full=Ran guanine nucleotide release factor; DE Short=RanGNRF; DE AltName: Full=Ran-binding protein MOG1; GN Name=RANGRF; Synonyms=MOG1, RANGNRF; ORFNames=HSPC165, HSPC236, MDS5; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH RP RAN, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=11290418; DOI=10.1016/s0378-1119(01)00364-x; RA Marfatia K.A., Harreman M.T., Fanara P., Vertino P.M., Corbett A.H.; RT "Identification and characterization of the human MOG1 gene."; RL Gene 266:45-56(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Hematopoietic stem cell; RA Huang C., Zhang C., Tu Y., Gu W., Wang Y., Han Z., Chen Z., Zhou J., Gu J., RA Huang Q., Yu Y., Xu S., Ren S., Fu G.; RT "Novel genes expressed in hematopoietic stem/progenitor cells from RT Myelodysplastic Syndromes patient."; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Umbilical cord blood; RX PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for 300 RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor RT cells."; RL Genome Res. 10:1546-1560(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Umbilical cord blood; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Prostate; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Bone marrow, Lung, and Uterus; 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 [10] RP FUNCTION, AND INTERACTION WITH SCN5A. 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 [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] 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). RN [13] RP VARIANT 61-GLU--GLN-186 DEL, CHARACTERIZATION OF VARIANT 61-GLU--GLN-186 RP DEL, FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=21621375; DOI=10.1016/j.cjca.2011.01.003; RA Olesen M.S., Jensen N.F., Holst A.G., Nielsen J.B., Tfelt-Hansen J., RA Jespersen T., Sajadieh A., Haunsoe S., Lund J.T., Calloe K., Schmitt N., RA Svendsen J.H.; RT "A novel nonsense variant in Nav1.5 cofactor MOG1 eliminates its sodium RT current increasing effect and may increase the risk of arrhythmias."; RL Can. J. Cardiol. 27:E17-E23(2011). RN [14] RP VARIANT ASP-83, CHARACTERIZATION OF VARIANT ASP-83, FUNCTION, AND RP SUBCELLULAR LOCATION. RX PubMed=21447824; DOI=10.1161/circgenetics.110.959130; RA Kattygnarath D., Maugenre S., Neyroud N., Balse E., Ichai C., Denjoy I., RA Dilanian G., Martins R.P., Fressart V., Berthet M., Schott J.J., RA Leenhardt A., Probst V., Le Marec H., Hainque B., Coulombe A., Hatem S.N., RA Guicheney P.; RT "MOG1: a new susceptibility gene for Brugada syndrome."; RL Circ. Cardiovasc. Genet. 4:261-268(2011). RN [15] RP VARIANT 61-GLU--GLN-186 DEL. RX PubMed=24142675; DOI=10.5603/cj.a2013.0125; RA Campuzano O., Berne P., Selga E., Allegue C., Iglesias A., Brugada J., RA Brugada R.; RT "Brugada syndrome and p.E61X_RANGRF."; RL Cardiol. J. 21:121-127(2014). RN [16] RP STRUCTURE BY NMR, FUNCTION, INTERACTION WITH RAN, AND MUTAGENESIS OF RP ASP-27; GLU-50; GLU-53 AND ASP-70. RX PubMed=29040603; DOI=10.1093/jmcb/mjx045; RA Bao X., Liu H., Liu X., Ruan K., Zhang Y., Zhang Z., Hu Q., Liu Y., RA Akram S., Zhang J., Gong Q., Wang W., Yuan X., Li J., Zhao L., Dou Z., RA Tian R., Yao X., Wu J., Shi Y.; RT "Mitosis-specific acetylation tunes Ran effector binding for chromosome RT segregation."; RL J. Mol. Cell Biol. 10:18-32(2018). CC -!- FUNCTION: May regulate the intracellular trafficking of RAN CC (PubMed:11290418). Promotes guanine nucleotide release from RAN and CC inhibits binding of new GTP by preventing the binding of the RAN CC guanine nucleotide exchange factor RCC1 (PubMed:29040603). Regulates CC the levels of GTP-bound RAN in the nucleus, and thereby plays a role in CC the regulation of RAN-dependent mitotic spindle dynamics CC (PubMed:29040603). Enhances the expression of SCN5A at the cell CC membrane in cardiomyocytes (PubMed:18184654, PubMed:23420830, CC PubMed:21621375). {ECO:0000269|PubMed:11290418, CC ECO:0000269|PubMed:18184654, ECO:0000269|PubMed:21621375, CC ECO:0000269|PubMed:23420830, ECO:0000269|PubMed:29040603}. CC -!- SUBUNIT: Monomer. Interacts with RAN, both RAN-GTP and RAN-GDP CC (PubMed:11290418, PubMed:29040603). Competes with RCC1 for a common CC binding site on RAN and thereby inhibits RCC1-mediated nucleotide CC exchange (PubMed:29040603). Forms a complex with RAN-GTP and RANBP1 (By CC similarity). Interacts with the cytoplasmic loop 2 of SCN5A CC (PubMed:18184654). {ECO:0000250|UniProtKB:Q9JIB0, CC ECO:0000269|PubMed:11290418, ECO:0000269|PubMed:18184654, CC ECO:0000269|PubMed:29040603}. CC -!- INTERACTION: CC Q9HD47-3; P55212: CASP6; NbExp=3; IntAct=EBI-9089733, EBI-718729; CC Q9HD47-3; P41091: EIF2S3; NbExp=3; IntAct=EBI-9089733, EBI-1054228; CC Q9HD47-3; P22607: FGFR3; NbExp=3; IntAct=EBI-9089733, EBI-348399; CC Q9HD47-3; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-9089733, EBI-10226858; CC Q9HD47-3; P06396: GSN; NbExp=3; IntAct=EBI-9089733, EBI-351506; CC Q9HD47-3; P54652: HSPA2; NbExp=3; IntAct=EBI-9089733, EBI-356991; CC Q9HD47-3; P13473-2: LAMP2; NbExp=3; IntAct=EBI-9089733, EBI-21591415; CC Q9HD47-3; P62826: RAN; NbExp=3; IntAct=EBI-9089733, EBI-286642; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11290418}. Cytoplasm, CC perinuclear region {ECO:0000269|PubMed:21447824}. Cytoplasm CC {ECO:0000269|PubMed:11290418, ECO:0000269|PubMed:21447824}. Cell CC membrane {ECO:0000269|PubMed:21447824}; Peripheral membrane protein CC {ECO:0000305|PubMed:21447824}; Cytoplasmic side CC {ECO:0000305|PubMed:21447824}. Note=May shuttle between the nucleus and CC cytoplasm. {ECO:0000269|PubMed:11290418}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=MOG1a; CC IsoId=Q9HD47-1; Sequence=Displayed; CC Name=2; Synonyms=MOG1b; CC IsoId=Q9HD47-2; Sequence=VSP_033060; CC Name=3; CC IsoId=Q9HD47-3; Sequence=VSP_033059, VSP_033061; CC Name=4; CC IsoId=Q9HD47-4; Sequence=VSP_033057, VSP_033058; CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are ubiquitously expressed CC (PubMed:11290418). Detected in heart and brain (PubMed:21621375). CC {ECO:0000269|PubMed:11290418, ECO:0000269|PubMed:21621375}. CC -!- MISCELLANEOUS: Overexpression can rescue the trafficking defect caused CC by some SCN5A mutations that impair trafficking to the cell membrane. CC {ECO:0000269|PubMed:23420830}. CC -!- SIMILARITY: Belongs to the MOG1 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF29129.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAF87316.1; Type=Frameshift; Evidence={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; AF265205; AAG01291.1; -; mRNA. DR EMBL; AF265206; AAG01292.1; -; mRNA. DR EMBL; AF168714; AAF87316.1; ALT_FRAME; mRNA. DR EMBL; AF151070; AAF36156.1; -; mRNA. DR EMBL; AF161514; AAF29129.1; ALT_FRAME; mRNA. DR EMBL; AK290399; BAF83088.1; -; mRNA. DR EMBL; CR457206; CAG33487.1; -; mRNA. DR EMBL; CR749387; CAH18237.1; -; mRNA. DR EMBL; CH471108; EAW90064.1; -; Genomic_DNA. DR EMBL; CH471108; EAW90065.1; -; Genomic_DNA. DR EMBL; CH471108; EAW90066.1; -; Genomic_DNA. DR EMBL; BC006486; AAH06486.1; -; mRNA. DR EMBL; BC012552; AAH12552.1; -; mRNA. DR EMBL; BC100017; AAI00018.1; -; mRNA. DR CCDS; CCDS11137.1; -. [Q9HD47-1] DR CCDS; CCDS54086.1; -. [Q9HD47-2] DR CCDS; CCDS54087.1; -. [Q9HD47-3] DR CCDS; CCDS82066.1; -. [Q9HD47-4] DR RefSeq; NP_001171272.1; NM_001177801.1. [Q9HD47-2] DR RefSeq; NP_001171273.1; NM_001177802.1. [Q9HD47-3] DR RefSeq; NP_001317056.1; NM_001330127.1. [Q9HD47-4] DR RefSeq; NP_057576.2; NM_016492.4. [Q9HD47-1] DR PDB; 5YFG; NMR; -; A=1-186. DR PDBsum; 5YFG; -. DR AlphaFoldDB; Q9HD47; -. DR SMR; Q9HD47; -. DR BioGRID; 118866; 31. DR IntAct; Q9HD47; 23. DR STRING; 9606.ENSP00000226105; -. DR iPTMnet; Q9HD47; -. DR PhosphoSitePlus; Q9HD47; -. DR BioMuta; RANGRF; -. DR DMDM; 74718913; -. DR EPD; Q9HD47; -. DR jPOST; Q9HD47; -. DR MassIVE; Q9HD47; -. DR MaxQB; Q9HD47; -. DR PaxDb; 9606-ENSP00000226105; -. DR PeptideAtlas; Q9HD47; -. DR ProteomicsDB; 81833; -. [Q9HD47-1] DR ProteomicsDB; 81834; -. [Q9HD47-2] DR ProteomicsDB; 81835; -. [Q9HD47-3] DR ProteomicsDB; 81836; -. [Q9HD47-4] DR Pumba; Q9HD47; -. DR Antibodypedia; 24637; 69 antibodies from 18 providers. DR DNASU; 29098; -. DR Ensembl; ENST00000226105.11; ENSP00000226105.6; ENSG00000108961.14. [Q9HD47-1] DR Ensembl; ENST00000407006.8; ENSP00000383940.4; ENSG00000108961.14. [Q9HD47-2] DR Ensembl; ENST00000439238.3; ENSP00000413190.3; ENSG00000108961.14. [Q9HD47-3] DR Ensembl; ENST00000580434.5; ENSP00000462310.1; ENSG00000108961.14. [Q9HD47-4] DR GeneID; 29098; -. DR KEGG; hsa:29098; -. DR MANE-Select; ENST00000226105.11; ENSP00000226105.6; NM_016492.5; NP_057576.2. DR UCSC; uc002gkv.4; human. [Q9HD47-1] DR AGR; HGNC:17679; -. DR CTD; 29098; -. DR DisGeNET; 29098; -. DR GeneCards; RANGRF; -. DR GeneReviews; RANGRF; -. DR HGNC; HGNC:17679; RANGRF. DR HPA; ENSG00000108961; Low tissue specificity. DR MalaCards; RANGRF; -. DR MIM; 607954; gene. DR neXtProt; NX_Q9HD47; -. DR OpenTargets; ENSG00000108961; -. DR Orphanet; 130; Brugada syndrome. DR PharmGKB; PA162400661; -. DR VEuPathDB; HostDB:ENSG00000108961; -. DR eggNOG; KOG3329; Eukaryota. DR GeneTree; ENSGT00390000013834; -. DR HOGENOM; CLU_081345_2_1_1; -. DR InParanoid; Q9HD47; -. DR OMA; CSSAWML; -. DR OrthoDB; 167716at2759; -. DR PhylomeDB; Q9HD47; -. DR TreeFam; TF332074; -. DR PathwayCommons; Q9HD47; -. DR Reactome; R-HSA-5576892; Phase 0 - rapid depolarisation. DR SignaLink; Q9HD47; -. DR BioGRID-ORCS; 29098; 11 hits in 1165 CRISPR screens. DR GenomeRNAi; 29098; -. DR Pharos; Q9HD47; Tbio. DR PRO; PR:Q9HD47; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q9HD47; Protein. DR Bgee; ENSG00000108961; Expressed in left testis and 196 other cell types or tissues. DR GO; GO:0005901; C:caveola; IDA:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0014704; C:intercalated disc; ISS:BHF-UCL. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IC:BHF-UCL. DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:BHF-UCL. DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:BHF-UCL. DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB. DR GO; GO:0017080; F:sodium channel regulator activity; IDA: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; IMP:BHF-UCL. DR GO; GO:0060047; P:heart contraction; IBA:GO_Central. DR GO; GO:0090307; P:mitotic spindle assembly; IMP:UniProtKB. DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; IDA:BHF-UCL. DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IMP:BHF-UCL. DR GO; GO:0032527; P:protein exit from endoplasmic reticulum; IMP:BHF-UCL. 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; IMP:BHF-UCL. DR GO; GO:0098909; P:regulation of cardiac muscle cell action potential involved in regulation of contraction; IMP:BHF-UCL. DR GO; GO:0002027; P:regulation of heart rate; TAS:BHF-UCL. DR GO; GO:0003254; P:regulation of membrane depolarization; IDA:BHF-UCL. DR GO; GO:1900825; P:regulation of membrane depolarization during cardiac muscle cell action potential; IMP:BHF-UCL. DR GO; GO:0042391; P:regulation of membrane potential; IDA:BHF-UCL. DR GO; GO:1902305; P:regulation of sodium ion transmembrane transport; IDA:BHF-UCL. DR GO; GO:2000649; P:regulation of sodium ion transmembrane transporter activity; IDA:BHF-UCL. DR CDD; cd00224; Mog1; 1. DR Gene3D; 3.40.1000.10; Mog1/PsbP, alpha/beta/alpha sandwich; 1. DR InterPro; IPR007681; Mog1. DR InterPro; IPR016123; Mog1/PsbP_a/b/a-sand. DR PANTHER; PTHR15837; RAN GUANINE NUCLEOTIDE RELEASE FACTOR; 1. DR PANTHER; PTHR15837:SF0; RAN GUANINE NUCLEOTIDE RELEASE FACTOR; 1. DR Pfam; PF04603; Mog1; 1. DR SUPFAM; SSF55724; Mog1p/PsbP-like; 1. DR Genevisible; Q9HD47; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Cytoplasm; KW Guanine-nucleotide releasing factor; Membrane; Nucleus; Protein transport; KW Reference proteome; Transport. FT CHAIN 1..186 FT /note="Ran guanine nucleotide release factor" FT /id="PRO_0000330636" FT REGION 27..70 FT /note="Interaction with RAN" FT /evidence="ECO:0000269|PubMed:29040603" FT VAR_SEQ 118 FT /note="V -> P (in isoform 4)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_033057" FT VAR_SEQ 119..186 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_033058" FT VAR_SEQ 119..163 FT /note="AKDVTLHQALLRLPQYQTDLLLTFNQPPPDNRSSLGPENLSPAPW -> RAR FT ECVMSWKGGSGDAEIQVSILTLIPLGSKGRDTSSGLAEAAPVPD (in isoform FT 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_033059" FT VAR_SEQ 147..186 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11290418, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334, FT ECO:0000303|Ref.5" FT /id="VSP_033060" FT VAR_SEQ 164..186 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_033061" FT VARIANT 61..186 FT /note="Missing (found in patients with cardiac arrhythmias FT including Brugada syndrome; uncertain significance; loss of FT function in enhancing the expression of SCN5A at the cell FT membrane)" FT /evidence="ECO:0000269|PubMed:21621375, FT ECO:0000269|PubMed:24142675" FT /id="VAR_080079" FT VARIANT 83 FT /note="E -> D (found in patients with Brugada syndrome; FT uncertain significance; loss of function in enhancing the FT expression of SCN5A at the cell membrane; FT dbSNP:rs751751942)" FT /evidence="ECO:0000269|PubMed:21447824" FT /id="VAR_080080" FT MUTAGEN 27 FT /note="D->K: Decreased binding to RAN." FT /evidence="ECO:0000269|PubMed:29040603" FT MUTAGEN 50 FT /note="E->K: Strongly decreased binding to RAN. Abolishes FT binding to RAN; when associated with K-53." FT /evidence="ECO:0000269|PubMed:29040603" FT MUTAGEN 53 FT /note="E->K: Decreased binding to RAN. Abolishes binding to FT RAN; when associated with K-50." FT /evidence="ECO:0000269|PubMed:29040603" FT MUTAGEN 70 FT /note="D->K: Decreased binding to RAN." FT /evidence="ECO:0000269|PubMed:29040603" FT CONFLICT 94..96 FT /note="ALR -> PE (in Ref. 3; AAF36156)" FT /evidence="ECO:0000305" FT STRAND 6..8 FT /evidence="ECO:0007829|PDB:5YFG" FT TURN 10..12 FT /evidence="ECO:0007829|PDB:5YFG" FT STRAND 13..17 FT /evidence="ECO:0007829|PDB:5YFG" FT HELIX 25..27 FT /evidence="ECO:0007829|PDB:5YFG" FT STRAND 35..40 FT /evidence="ECO:0007829|PDB:5YFG" FT TURN 41..44 FT /evidence="ECO:0007829|PDB:5YFG" FT STRAND 45..50 FT /evidence="ECO:0007829|PDB:5YFG" FT HELIX 61..71 FT /evidence="ECO:0007829|PDB:5YFG" FT TURN 72..74 FT /evidence="ECO:0007829|PDB:5YFG" FT STRAND 81..87 FT /evidence="ECO:0007829|PDB:5YFG" FT HELIX 90..92 FT /evidence="ECO:0007829|PDB:5YFG" FT STRAND 100..108 FT /evidence="ECO:0007829|PDB:5YFG" FT STRAND 123..131 FT /evidence="ECO:0007829|PDB:5YFG" FT TURN 132..135 FT /evidence="ECO:0007829|PDB:5YFG" FT STRAND 136..144 FT /evidence="ECO:0007829|PDB:5YFG" FT STRAND 156..159 FT /evidence="ECO:0007829|PDB:5YFG" FT HELIX 165..172 FT /evidence="ECO:0007829|PDB:5YFG" FT HELIX 173..175 FT /evidence="ECO:0007829|PDB:5YFG" SQ SEQUENCE 186 AA; 20448 MW; BE2C459C90459042 CRC64; MEPTRDCPLF GGAFSAILPM GAIDVSDLRP VPDNQEVFCH PVTDQSLIVE LLELQAHVRG EAAARYHFED VGGVQGARAV HVESVQPLSL ENLALRGRCQ EAWVLSGKQQ IAKENQQVAK DVTLHQALLR LPQYQTDLLL TFNQPPPDNR SSLGPENLSP APWSLGDFEQ LVTSLTLHDP NIFGPQ //