RANT_MOUSE
ID RANT_MOUSE Reviewed; 216 AA.
AC Q61820; Q4FZF4; Q6P8M7; Q80YD4; Q9D9Y0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=GTP-binding nuclear protein Ran, testis-specific isoform;
DE EC=3.6.5.- {ECO:0000250|UniProtKB:P62826};
GN Name=Rasl2-9;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=7849398; DOI=10.1007/bf00411457;
RA Coutavas E.E., Hsieh C.M., Ren M., Drivas G.T., Rush M.G.,
RA D'Eustachio P.D.;
RT "Tissue-specific expression of Ran isoforms in the mouse.";
RL Mamm. Genome 5:623-628(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 MRNA].
RC TISSUE=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).
CC -!- FUNCTION: GTP-binding protein involved in nucleocytoplasmic transport
CC (By similarity). Required for the import of protein into the nucleus
CC and also for RNA export (By similarity). Involved in chromatin
CC condensation and control of cell cycle (By similarity).
CC {ECO:0000250|UniProtKB:P62826}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000250|UniProtKB:P62826};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:P62826};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P62826}.
CC -!- TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:7849398}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ran family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH49619.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L32752; AAA64248.1; -; mRNA.
DR EMBL; AK006350; BAB24542.1; -; mRNA.
DR EMBL; BC049619; AAH49619.1; ALT_INIT; mRNA.
DR EMBL; BC061180; AAH61180.2; -; mRNA.
DR EMBL; BC099553; AAH99553.2; -; mRNA.
DR CCDS; CCDS20760.1; -.
DR PIR; I76676; I76676.
DR RefSeq; NP_033054.1; NM_009028.2.
DR AlphaFoldDB; Q61820; -.
DR SMR; Q61820; -.
DR BioGRID; 202603; 1.
DR IntAct; Q61820; 1.
DR MINT; Q61820; -.
DR STRING; 10090.ENSMUSP00000129559; -.
DR iPTMnet; Q61820; -.
DR PhosphoSitePlus; Q61820; -.
DR SwissPalm; Q61820; -.
DR jPOST; Q61820; -.
DR MaxQB; Q61820; -.
DR PaxDb; Q61820; -.
DR PRIDE; Q61820; -.
DR ProteomicsDB; 254897; -.
DR DNASU; 19428; -.
DR Ensembl; ENSMUST00000147835; ENSMUSP00000129559; ENSMUSG00000083649.
DR GeneID; 19428; -.
DR KEGG; mmu:19428; -.
DR UCSC; uc009fac.1; mouse.
DR CTD; 19428; -.
DR MGI; MGI:104605; Rasl2-9.
DR VEuPathDB; HostDB:ENSMUSG00000083649; -.
DR eggNOG; KOG0096; Eukaryota.
DR GeneTree; ENSGT00940000153786; -.
DR HOGENOM; CLU_041217_13_0_1; -.
DR InParanoid; Q61820; -.
DR OMA; AQCAVIM; -.
DR OrthoDB; 1083175at2759; -.
DR PhylomeDB; Q61820; -.
DR TreeFam; TF106302; -.
DR BioGRID-ORCS; 19428; 5 hits in 74 CRISPR screens.
DR PRO; PR:Q61820; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q61820; protein.
DR Bgee; ENSMUSG00000083649; Expressed in spermatid and 49 other tissues.
DR ExpressionAtlas; Q61820; baseline and differential.
DR Genevisible; Q61820; MM.
DR GO; GO:0005814; C:centriole; ISO:MGI.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR GO; GO:0042565; C:RNA nuclear export complex; ISO:MGI.
DR GO; GO:0019003; F:GDP binding; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; ISO:MGI.
DR GO; GO:0003924; F:GTPase activity; ISO:MGI.
DR GO; GO:0000287; F:magnesium ion binding; ISO:MGI.
DR GO; GO:0070883; F:pre-miRNA binding; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0046039; P:GTP metabolic process; ISO:MGI.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; ISO:MGI.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISO:MGI.
DR GO; GO:0006611; P:protein export from nucleus; ISO:MGI.
DR GO; GO:0006606; P:protein import into nucleus; ISO:MGI.
DR GO; GO:1902570; P:protein localization to nucleolus; ISO:MGI.
DR GO; GO:0000055; P:ribosomal large subunit export from nucleus; ISO:MGI.
DR GO; GO:0000056; P:ribosomal small subunit export from nucleus; ISO:MGI.
DR GO; GO:0000054; P:ribosomal subunit export from nucleus; IBA:GO_Central.
DR GO; GO:0061015; P:snRNA import into nucleus; ISO:MGI.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002041; Ran_GTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR PANTHER; PTHR24071; PTHR24071; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00627; GTPRANTC4.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51418; RAN; 1.
PE 2: Evidence at transcript level;
KW Acetylation; GTP-binding; Hydrolase; Isopeptide bond; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Protein transport; Reference proteome; Transport;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P62826"
FT CHAIN 2..216
FT /note="GTP-binding nuclear protein Ran, testis-specific
FT isoform"
FT /id="PRO_0000208699"
FT BINDING 17..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 65..69
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 122..125
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P62826"
FT MOD_RES 24
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P62826"
FT MOD_RES 60
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62826"
FT MOD_RES 71
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62826"
FT MOD_RES 99
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62826"
FT MOD_RES 134
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62826"
FT MOD_RES 159
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62826"
FT MOD_RES 159
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62827"
FT CROSSLNK 71
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P62826"
FT CROSSLNK 71
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P62826"
FT CONFLICT 8
FT /note="Q -> R (in Ref. 2; BAB24542)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 216 AA; 24452 MW; 23BA7E723B96B808 CRC64;
MAAQGEPQVQ FKVVLVGDGG TGKTTFMKRH LTGEFEKEYV ATLGVEVHTL VFHTNRGPIK
FNVWDTAGQE KFGGLRDGYY IQAQCAIIMF DVTSRVTYKN VPSWHKDLVR VCENIPIVLC
GNKVDVKDMK VKAKPILFHR KKNLQYYDIS ARSNYNFEKP FFWLARKLIG DPNLEFVAMP
ALAPPEVVMD PALAAQYEHD LEVAQTTALP DEEDDL
