MOG1_HUMAN
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 03-AUG-2022, entry version 138.
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};
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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; 30.
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; Q9HD47; -.
DR PeptideAtlas; Q9HD47; -.
DR PRIDE; Q9HD47; -.
DR ProteomicsDB; 81833; -. [Q9HD47-1]
DR ProteomicsDB; 81834; -. [Q9HD47-2]
DR ProteomicsDB; 81835; -. [Q9HD47-3]
DR ProteomicsDB; 81836; -. [Q9HD47-4]
DR Antibodypedia; 24637; 56 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 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; QCVSKFN; -.
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 1087 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 194 other tissues.
DR Genevisible; Q9HD47; HS.
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: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:0090226; P:regulation of microtubule nucleation by Ran protein signal transduction; IMP:UniProtKB.
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 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 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 arrhythmia
FT and in patients with Brugada syndrome; loss of function in
FT enhancing the expression of SCN5A at the cell membrane;
FT unknown pathological significance)"
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 loss of function in enhancing the expression of SCN5A at
FT the cell membrane; unknown pathological significance;
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
