SPI1_SCHPO
ID SPI1_SCHPO Reviewed; 216 AA.
AC P28748;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=GTP-binding nuclear protein spi1;
GN Name=spi1; ORFNames=SPBC1289.03c;
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 [GENOMIC DNA].
RX PubMed=1855255; DOI=10.1016/0092-8674(91)90624-8;
RA Matsumoto T., Beach D.H.;
RT "Premature initiation of mitosis in yeast lacking RCC1 or an interacting
RT GTPase.";
RL Cell 66:347-360(1991).
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 INTERACTION WITH DIS3 AND PIM1.
RX PubMed=8896453; DOI=10.1002/j.1460-2075.1996.tb00944.x;
RA Noguchi E., Hayashi N., Azuma Y., Seki T., Nakamura M., Nakashima N.,
RA Yanagida M., He X., Mueller U., Sazer S., Nishimoto T.;
RT "Dis3, implicated in mitotic control, binds directly to Ran and enhances
RT the GEF activity of RCC1.";
RL EMBO J. 15:5595-5605(1996).
RN [4]
RP FUNCTION, AND INTERACTION WITH FFT3.
RX PubMed=18422602; DOI=10.1111/j.1365-2443.2008.01190.x;
RA Ohba T., Nishijima H., Nishitani H., Nishimoto T.;
RT "Schizosaccharomyces pombe Snf2SR, a novel SNF2 family protein, interacts
RT with Ran GTPase and modulates both RanGEF and RanGAP activities.";
RL Genes Cells 13:571-582(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20, 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: GTP-binding protein involved in nucleocytoplasmic transport.
CC Required for the import of protein into the nucleus and also for RNA
CC export. {ECO:0000269|PubMed:18422602}.
CC -!- SUBUNIT: Oligomer of dis3, pim1 and spi1. Found in a nuclear export
CC complex with RanGTP, exportin and pre-miRNA (By similarity). Interacts
CC with fft3. {ECO:0000250|UniProtKB:P62825, ECO:0000269|PubMed:18422602,
CC ECO:0000269|PubMed:8896453}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ran family.
CC {ECO:0000305}.
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DR EMBL; M73527; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU329671; CAB38683.1; -; Genomic_DNA.
DR PIR; A40039; A40039.
DR RefSeq; NP_596827.1; NM_001023848.2.
DR AlphaFoldDB; P28748; -.
DR SMR; P28748; -.
DR BioGRID; 276686; 20.
DR STRING; 4896.SPBC1289.03c.1; -.
DR iPTMnet; P28748; -.
DR MaxQB; P28748; -.
DR PaxDb; P28748; -.
DR PRIDE; P28748; -.
DR EnsemblFungi; SPBC1289.03c.1; SPBC1289.03c.1:pep; SPBC1289.03c.
DR GeneID; 2540149; -.
DR KEGG; spo:SPBC1289.03c; -.
DR PomBase; SPBC1289.03c; spi1.
DR VEuPathDB; FungiDB:SPBC1289.03c; -.
DR eggNOG; KOG0096; Eukaryota.
DR HOGENOM; CLU_041217_13_0_1; -.
DR InParanoid; P28748; -.
DR OMA; TIVFHRK; -.
DR PhylomeDB; P28748; -.
DR Reactome; R-SPO-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-SPO-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR PRO; PR:P28748; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005525; F:GTP binding; ISM:PomBase.
DR GO; GO:0003924; F:GTPase activity; IDA:PomBase.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IGI:PomBase.
DR GO; GO:0006606; P:protein import into nucleus; IMP:PomBase.
DR GO; GO:0000054; P:ribosomal subunit export from nucleus; IBA:GO_Central.
DR GO; GO:0023052; P:signaling; NAS:PomBase.
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 1: Evidence at protein level;
KW GTP-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..216
FT /note="GTP-binding nuclear protein spi1"
FT /id="PRO_0000208735"
FT BINDING 17..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62825"
FT BINDING 67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62825"
FT BINDING 121..124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62825"
FT BINDING 149..151
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62825"
FT MOD_RES 20
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 216 AA; 24555 MW; 9349A9155E315442 CRC64;
MAQPQNVPTF KLVLVGDGGT GKTTFVKRHL TGEFEKKYIA TLGVEVHPLH FHTNFGEICF
NVWDTAGQEK LGGLRDGYYI QGQCGIIMFD VTSRITYKNV PHWWRDLVRV CENIPIVLCG
NKVDVKERKV KAKAITFHRK KNLQYYDISA KSNYNFEKPF LWLARKLVGN PNLEFVASPA
LAPPEVQVDQ QLLAQYQQEM NEAAAMPLPD EDDADL
