ID   RCC1_MESAU              Reviewed;         421 AA.
AC   P23800;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Regulator of chromosome condensation;
DE   AltName: Full=Chromosome condensation protein 1;
GN   Name=RCC1; Synonyms=CHC1;
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF SER-256.
RX   PubMed=2300055; DOI=10.1128/mcb.10.2.577-584.1990;
RA   Uchida S., Sekiguchi T., Nishitani H., Miyauchi K., Ohtsubo M.,
RA   Nishimoto T.;
RT   "Premature chromosome condensation is induced by a point mutation in the
RT   hamster RCC1 gene.";
RL   Mol. Cell. Biol. 10:577-584(1990).
RN   [2]
RP   CHARACTERIZATION, AND FUNCTION.
RX   PubMed=2022190; DOI=10.1002/j.1460-2075.1991.tb08068.x;
RA   Ohtsubo M., Yoshida T., Seino H., Nishitani H., Clark K.L.,
RA   Sprague G.F. Jr., Frasch M., Nishimoto T.;
RT   "Mutation of the hamster cell cycle gene RCC1 is complemented by the
RT   homologous genes of Drosophila and S.cerevisiae.";
RL   EMBO J. 10:1265-1273(1991).
CC   -!- FUNCTION: Guanine-nucleotide releasing factor that promotes the
CC       exchange of Ran-bound GDP by GTP, and thereby plays an important role
CC       in RAN-mediated functions in nuclear import and mitosis. Contributes to
CC       the generation of high levels of chromosome-associated, GTP-bound RAN,
CC       which is important for mitotic spindle assembly and normal progress
CC       through mitosis. Via its role in maintaining high levels of GTP-bound
CC       RAN in the nucleus, contributes to the release of cargo proteins from
CC       importins after nuclear import (By similarity). Involved in the
CC       regulation of onset of chromosome condensation in the S phase
CC       (PubMed:2300055, PubMed:2022190). Binds both to the nucleosomes and
CC       double-stranded DNA (By similarity). {ECO:0000250|UniProtKB:P18754,
CC       ECO:0000269|PubMed:2022190, ECO:0000269|PubMed:2300055}.
CC   -!- SUBUNIT: Interacts with RAN. Interacts (via N-terminus and RCC1
CC       repeats) with KPNA4. Interacts with ARRB2; the interaction is detected
CC       in the nucleus upon OR1D2 stimulation. {ECO:0000250|UniProtKB:P18754}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P18754}.
CC       Chromosome {ECO:0000250|UniProtKB:P18754}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P18754}. Note=Predominantly nuclear in
CC       interphase cells. Binds to mitotic chromosomes.
CC       {ECO:0000250|UniProtKB:P18754}.
CC   -!- PTM: N-terminal methylation by METTL11A/NTM1 is required for binding
CC       double-stranded DNA and stable chromatin association. Dimethylation
CC       produces a permanent positive charge on the amino group, which
CC       facilitates electrostatic binding to the phosphate groups on DNA, while
CC       inhibiting histone-binding. Methylated tail helps retain RCC1 on
CC       chromosomes during nucleotide exchange on Ran.
CC       {ECO:0000250|UniProtKB:P18754}.
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DR   EMBL; M33579; AAA36964.1; -; mRNA.
DR   PIR; A34726; A34726.
DR   AlphaFoldDB; P23800; -.
DR   SMR; P23800; -.
DR   STRING; 10036.XP_005079698.1; -.
DR   eggNOG; KOG1426; Eukaryota.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0031492; F:nucleosomal DNA binding; ISS:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR   GO; GO:0051225; P:spindle assembly; ISS:UniProtKB.
DR   Gene3D; 2.130.10.30; -; 1.
DR   InterPro; IPR009091; RCC1/BLIP-II.
DR   InterPro; IPR000408; Reg_chr_condens.
DR   Pfam; PF00415; RCC1; 7.
DR   PRINTS; PR00633; RCCNDNSATION.
DR   SUPFAM; SSF50985; SSF50985; 1.
DR   PROSITE; PS00625; RCC1_1; 1.
DR   PROSITE; PS00626; RCC1_2; 4.
DR   PROSITE; PS50012; RCC1_3; 7.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Chromosome; Cytoplasm; DNA-binding;
KW   Guanine-nucleotide releasing factor; Methylation; Mitosis; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VE37"
FT   CHAIN           2..421
FT                   /note="Regulator of chromosome condensation"
FT                   /id="PRO_0000206629"
FT   REPEAT          34..84
FT                   /note="RCC1 1"
FT   REPEAT          85..136
FT                   /note="RCC1 2"
FT   REPEAT          138..189
FT                   /note="RCC1 3"
FT   REPEAT          191..257
FT                   /note="RCC1 4"
FT   REPEAT          258..311
FT                   /note="RCC1 5"
FT   REPEAT          312..362
FT                   /note="RCC1 6"
FT   REPEAT          363..416
FT                   /note="RCC1 7"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           4..24
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:P18754"
FT   COMPBIAS        7..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N,N-dimethylproline; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VE37"
FT   MOD_RES         2
FT                   /note="N-methylproline; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VE37"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18754"
FT   MUTAGEN         256
FT                   /note="S->F: In tsBN2; temperature-sensitive mutant that
FT                   induces a premature entry into mitosis."
FT                   /evidence="ECO:0000269|PubMed:2300055"
SQ   SEQUENCE   421 AA;  45101 MW;  F090DA7325A8B03C CRC64;
     MPPKRIAKRR SPPEDAIPKS KKVKVSHRSH KTEPGLVLTL GQGDVGQLGL GESVLERKKP
     ALVPLLQDVV QAEAGGMHTV CLNQSGQVYS FGCNDEGALG RDTSVEGSEM VPGKVELQEK
     VVQVSAGDSH TAALTEDGRV FLWGSFRDNN GVIGLLEPMK KSMVPVQVQL DMPVVKVASG
     NDHLVMLTTD GDLYTLGCGE QGQLGRVPEL FANRGGRQGL ERLLVPKCVL LKSRGSRGRV
     RFQDAFCGAY LTFAISREGH VYGFGLSNYH QLGTPGTASC FIPQNLTSFK NSTKSWVGFS
     GGQHHTICMD SEGKAYSLGR AEYGRLGLGE GAEEKSIPTL ISRLPVVSSV ACGASVGYAV
     SKDGRVFAWG MGTNYQLGTG QDEDAWSPVE MTGKQLENRV VLTVSSGGQH TVLLVKDKEQ
     S