ID   RANG_SCHPO              Reviewed;         215 AA.
AC   Q09717; O42635;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Ran-specific GTPase-activating protein 1;
DE   AltName: Full=Ran-binding protein 1;
DE            Short=RANBP1;
DE   AltName: Full=Spi1-binding protein;
GN   Name=sbp1; Synonyms=yrb1; ORFNames=SPBC1773.07c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=9504913; DOI=10.1093/genetics/148.2.645;
RA   Ho X., Hayashi N., Walcott N.G., Azuma Y., Patterson T.E., Bischoff F.R.,
RA   Nishimoto T., Sazer S.;
RT   "The identification of cDNAs that affect the mitosis-to-interphase
RT   transition in Schizosaccharomyces pombe, including sbp1, which encodes a
RT   spi1p-GTP-binding protein.";
RL   Genetics 148:645-656(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- FUNCTION: Stimulates the GTPase activity in the presence of RNA1. May
CC       potentiate the action of RanGAP1 (RNA1), thus playing the role of a
CC       negative regulator.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Mainly cytoplasmic.
CC   -!- SIMILARITY: Belongs to the RANBP1 family. {ECO:0000305}.
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DR   EMBL; D86381; BAA13080.1; -; Genomic_DNA.
DR   EMBL; D76431; BAA23793.1; -; mRNA.
DR   EMBL; CU329671; CAA21912.1; -; Genomic_DNA.
DR   PIR; T43209; T43209.
DR   PIR; T51307; T51307.
DR   RefSeq; NP_595122.1; NM_001021029.2.
DR   AlphaFoldDB; Q09717; -.
DR   SMR; Q09717; -.
DR   BioGRID; 276679; 3.
DR   STRING; 4896.SPBC1773.07c.1; -.
DR   iPTMnet; Q09717; -.
DR   MaxQB; Q09717; -.
DR   PaxDb; Q09717; -.
DR   PRIDE; Q09717; -.
DR   EnsemblFungi; SPBC1773.07c.1; SPBC1773.07c.1:pep; SPBC1773.07c.
DR   GeneID; 2540142; -.
DR   KEGG; spo:SPBC1773.07c; -.
DR   PomBase; SPBC1773.07c; sbp1.
DR   VEuPathDB; FungiDB:SPBC1773.07c; -.
DR   eggNOG; KOG0864; Eukaryota.
DR   HOGENOM; CLU_067861_0_1_1; -.
DR   InParanoid; Q09717; -.
DR   OMA; CANHLLM; -.
DR   PhylomeDB; Q09717; -.
DR   Reactome; R-SPO-159227; Transport of the SLBP independent Mature mRNA.
DR   Reactome; R-SPO-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR   Reactome; R-SPO-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR   Reactome; R-SPO-3232142; SUMOylation of ubiquitinylation proteins.
DR   Reactome; R-SPO-4085377; SUMOylation of SUMOylation proteins.
DR   Reactome; R-SPO-4551638; SUMOylation of chromatin organization proteins.
DR   Reactome; R-SPO-4570464; SUMOylation of RNA binding proteins.
DR   Reactome; R-SPO-5578749; Transcriptional regulation by small RNAs.
DR   PRO; PR:Q09717; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:PomBase.
DR   GO; GO:0005643; C:nuclear pore; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; TAS:PomBase.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0006606; P:protein import into nucleus; ISO:PomBase.
DR   GO; GO:0031291; P:Ran protein signal transduction; IC:PomBase.
DR   GO; GO:0006405; P:RNA export from nucleus; ISO:PomBase.
DR   CDD; cd13179; RanBD_RanBP1; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR000156; Ran_bind_dom.
DR   InterPro; IPR045255; RanBP1-like.
DR   InterPro; IPR045256; RanBP1_RanBD.
DR   PANTHER; PTHR23138; PTHR23138; 1.
DR   Pfam; PF00638; Ran_BP1; 1.
DR   SMART; SM00160; RanBD; 1.
DR   PROSITE; PS50196; RANBD1; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; GTPase activation; Phosphoprotein; Reference proteome.
FT   CHAIN           1..215
FT                   /note="Ran-specific GTPase-activating protein 1"
FT                   /id="PRO_0000213669"
FT   DOMAIN          74..210
FT                   /note="RanBD1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT   REGION          1..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..71
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         70
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   CONFLICT        135
FT                   /note="V -> G (in Ref. 1; BAA23793)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   215 AA;  24150 MW;  5C4DA85823F1E4B2 CRC64;
     MSAEQEKKTQ GTTKEEQKSS FASEDVASKQ TEEAKAVFGD GVAKQENKSG ASTNDEKKPA
     EGDEDAEPAS PEVHFEPIVK LSAVETKTNE EEETVEFKMR AKLFRFDKAA SEWKERGTGD
     ARLLKHKETG KTRLVMRRDK TLKVCANHLL MPEMKLTPNV GSDRSWVWTV AADVSEGEPT
     AETFAIRFAN SENANLFKEN FEKYQEENAK ILKKN