RCC1_SCHPO
ID RCC1_SCHPO Reviewed; 539 AA.
AC P28745; Q9USS3;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 25-MAY-2022, entry version 157.
DE RecName: Full=Protein pim1;
DE AltName: Full=Poly(A)+ RNA transport protein 2;
GN Name=pim1; Synonyms=dcd1, ptr2; ORFNames=SPBC557.03c;
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 SPI1.
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 INTERACTION WITH NED1.
RX PubMed=12376568; DOI=10.1242/jcs.00135;
RA Tange Y., Hirata A., Niwa O.;
RT "An evolutionarily conserved fission yeast protein, Ned1, implicated in
RT normal nuclear morphology and chromosome stability, interacts with Dis3,
RT Pim1/RCC1 and an essential nucleoporin.";
RL J. Cell Sci. 115:4375-4385(2002).
CC -!- FUNCTION: Promotes the exchange of Ran(spi1)-bound GDP by GTP. Involved
CC in the control of mitosis. Regulates a variety of nuclear events,
CC including mitotic check-point, chromosome decondensation and mRNA
CC processing/transport.
CC -!- SUBUNIT: Oligomer of dis3, pim1 and spi1. Interacts with ned1.
CC {ECO:0000269|PubMed:12376568, ECO:0000269|PubMed:8896453}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
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DR EMBL; M73528; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU329671; CAB60670.1; -; Genomic_DNA.
DR PIR; B40039; B40039.
DR PIR; T50368; T50368.
DR RefSeq; NP_596026.1; NM_001021935.2.
DR AlphaFoldDB; P28745; -.
DR SMR; P28745; -.
DR BioGRID; 277574; 13.
DR STRING; 4896.SPBC557.03c.1; -.
DR iPTMnet; P28745; -.
DR MaxQB; P28745; -.
DR PaxDb; P28745; -.
DR EnsemblFungi; SPBC557.03c.1; SPBC557.03c.1:pep; SPBC557.03c.
DR PomBase; SPBC557.03c; pim1.
DR VEuPathDB; FungiDB:SPBC557.03c; -.
DR eggNOG; KOG1426; Eukaryota.
DR HOGENOM; CLU_005210_4_2_1; -.
DR OMA; WSWGTND; -.
DR PhylomeDB; P28745; -.
DR Reactome; R-SPO-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR PRO; PR:P28745; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:1990023; C:mitotic spindle midzone; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IGI:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0101024; P:mitotic nuclear membrane organization; IMP:PomBase.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; IMP:PomBase.
DR GO; GO:0031291; P:Ran protein signal transduction; IGI:PomBase.
DR GO; GO:0007096; P:regulation of exit from mitosis; IMP:PomBase.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; IMP:PomBase.
DR GO; GO:0032888; P:regulation of mitotic spindle elongation; IMP:PomBase.
DR Gene3D; 2.130.10.30; -; 1.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR Pfam; PF00415; RCC1; 5.
DR PRINTS; PR00633; RCCNDNSATION.
DR SUPFAM; SSF50985; SSF50985; 1.
DR PROSITE; PS00625; RCC1_1; 1.
DR PROSITE; PS00626; RCC1_2; 3.
DR PROSITE; PS50012; RCC1_3; 7.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Guanine-nucleotide releasing factor; Mitosis;
KW Nucleus; Reference proteome; Repeat.
FT CHAIN 1..539
FT /note="Protein pim1"
FT /id="PRO_0000206636"
FT REPEAT 70..125
FT /note="RCC1 1"
FT REPEAT 127..191
FT /note="RCC1 2"
FT REPEAT 192..243
FT /note="RCC1 3"
FT REPEAT 244..296
FT /note="RCC1 4"
FT REPEAT 298..353
FT /note="RCC1 5"
FT REPEAT 354..417
FT /note="RCC1 6"
FT REPEAT 419..472
FT /note="RCC1 7"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 124
FT /note="S -> L (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 526
FT /note="E -> D (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 539 AA; 58349 MW; 35C0AF47CF6581F3 CRC64;
MTSNRSTRSS TKREEVSKNG VEKRELDESD VMKNGKKPVK RAKVSSLPKP VRVPGSAKRI
NKIPELPTER LNVYVFGSGS MNELGMGEEE MDVVYRPRLN PILSTDKVGV VDLAVGGMHS
AALSHDGRVY TWGVNDDYAL GRLTKDQKDE NGDKVDNDLL EGTPSKVEGA LSHLRVTKVI
CSDNLTAAIT DNGCCFTWGT FRCSDGVLGY SDSQKRTAEP TQMRLPEICQ LATGTDHIIA
LTTTGKVYTW GNGQQFQLGR RMLERRRLQG LTPQPLALKN IISVGAGSYH SFAIDNKGRV
YAWGLNITRQ CGIEVEDEEE GAVITKPTLV DALEGYNVKS ITGGEHHTLA LLEDGRVLAW
GRDDRHQLGI PDNALPETVV KDEKGNNYYL STPTIIPGLT NVIQVVCGTH HNLAVTSDGK
VYSWGSAENY EVGQGDNDED VAVPTLVRSK AIKEVAIRVA GAGGQFSIIA GIPNASEEPV
ANGIKSEPEN EKKLKTEETS KTDDSPVTDA KPDVTSNGEP STATSESKDS VLEPSSTTA
