ID   REP2_YEAST              Reviewed;         296 AA.
AC   P03872;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   13-SEP-2023, entry version 99.
DE   RecName: Full=Partitioning protein REP2;
DE            Short=R2;
DE   AltName: Full=Protein Charlie;
DE   AltName: Full=Trans-acting factor C;
GN   Name=REP2; OrderedLocusNames=R0040C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OG   Plasmid 2-micron.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A364A D5;
RX   PubMed=6251374; DOI=10.1038/286860a0;
RA   Hartley J.L., Donelson J.E.;
RT   "Nucleotide sequence of the yeast plasmid.";
RL   Nature 286:860-864(1980).
RN   [2]
RP   FUNCTION.
RX   PubMed=2832156; DOI=10.1002/j.1460-2075.1987.tb02768.x;
RA   Murray J.A.H., Scarpa M., Rossi N., Cesareni G.;
RT   "Antagonistic controls regulate copy number of the yeast 2 micron
RT   plasmid.";
RL   EMBO J. 6:4205-4212(1987).
RN   [3]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH REP1.
RX   PubMed=9393716; DOI=10.1128/jb.179.23.7497-7506.1997;
RA   Ahn Y.-T., Wu X.-L., Biswal S., Velmurugan S., Volkert F.C., Jayaram M.;
RT   "The 2 micrometer-plasmid-encoded Rep1 and Rep2 proteins interact with each
RT   other and colocalize to the Saccharomyces cerevisiae nucleus.";
RL   J. Bacteriol. 179:7497-7506(1997).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=9819432; DOI=10.1128/mcb.18.12.7466;
RA   Velmurugan S., Ahn Y.-T., Yang X.-M., Wu X.-L., Jayaram M.;
RT   "The 2 micrometer plasmid stability system: analyses of the interactions
RT   among plasmid- and host-encoded components.";
RL   Mol. Cell. Biol. 18:7466-7477(1998).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=10791970; DOI=10.1083/jcb.149.3.553;
RA   Velmurugan S., Yang X.-M., Chan C.S.-M., Dobson M.J., Jayaram M.;
RT   "Partitioning of the 2-micrometer circle plasmid of Saccharomyces
RT   cerevisiae. Functional coordination with chromosome segregation and
RT   plasmid-encoded Rep protein distribution.";
RL   J. Cell Biol. 149:553-566(2000).
RN   [6]
RP   INTERACTION WITH REP1, AND DNA-BINDING.
RX   PubMed=11244071; DOI=10.1128/jb.183.7.2306-2315.2001;
RA   Sengupta A., Blomqvist K., Pickett A.J., Zhang Y., Chew J.S.K.,
RA   Dobson M.J.;
RT   "Functional domains of yeast plasmid-encoded Rep proteins.";
RL   J. Bacteriol. 183:2306-2315(2001).
RN   [7]
RP   FUNCTION.
RX   PubMed=12177044; DOI=10.1083/jcb.200204136;
RA   Mehta S., Yang X.-M., Chan C.S.-M., Dobson M.J., Jayaram M., Velmurugan S.;
RT   "The 2 micron plasmid purloins the yeast cohesin complex: a mechanism for
RT   coupling plasmid partitioning and chromosome segregation?";
RL   J. Cell Biol. 158:625-637(2002).
RN   [8]
RP   FUNCTION.
RX   PubMed=16966420; DOI=10.1083/jcb.200603042;
RA   Hajra S., Ghosh S.K., Jayaram M.;
RT   "The centromere-specific histone variant Cse4p (CENP-A) is essential for
RT   functional chromatin architecture at the yeast 2-micrometer circle
RT   partitioning locus and promotes equal plasmid segregation.";
RL   J. Cell Biol. 174:779-790(2006).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Part of the plasmid partitioning system, which ensures the
CC       equal distribution of replicated plasmid molecules to daughter cells.
CC       The plasmids exist as well-organized plasmid foci within the nucleus
CC       that stay together throughout the cell-cycle and act as entity during
CC       segregation, effetively reducing copy number to one. Plasmid
CC       partitioning requires the proteins REP1, REP2, and a cis-acting locus
CC       STB (REP3). REP1-REP2 stably associate with CSE4-containing chromatin
CC       at STB during S-phase, marking the locus with a centromeric tag, and
CC       thereby probably catching mitotic spindle microtubules to the plasmid
CC       cluster and coupling plasmid segregation to chromosome segregation.
CC       REP1-REP2 are required to recruit the cohesin complex to the STB locus
CC       for pairing of the replicated plasmid cluster, a prerequisite for
CC       successful plasmid segregation. REP1-REP2 also negatively regulate
CC       expression of site-specific recombinase FLP and of RAF1.
CC       {ECO:0000269|PubMed:10791970, ECO:0000269|PubMed:12177044,
CC       ECO:0000269|PubMed:16966420, ECO:0000269|PubMed:2832156}.
CC   -!- SUBUNIT: Interacts with REP1. {ECO:0000269|PubMed:11244071,
CC       ECO:0000269|PubMed:9393716}.
CC   -!- INTERACTION:
CC       P03872; P03871: REP1; NbExp=7; IntAct=EBI-2125362, EBI-14929;
CC       P03872; P03872: REP2; NbExp=5; IntAct=EBI-2125362, EBI-2125362;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10791970,
CC       ECO:0000269|PubMed:9393716, ECO:0000269|PubMed:9819432}.
CC       Note=Colocalizes with the STB locus of the 2-micron plasmid as foci in
CC       the nucleus near the spindle pole body. Is expelled from STB during a
CC       short interval between late G1 and early S phases.
CC   -!- MISCELLANEOUS: The plasmid 2-micron circle is a extrachromosomal
CC       element that resides in the nucleus and propagates itself stably in
CC       host cell populations. It provides no obvious advantage to the host but
CC       imposes no significant disadvantage either at its steady-state copy
CC       number of 40-60 molecules/cell.
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DR   EMBL; J01347; AAB59343.1; -; Genomic_DNA.
DR   PIR; A04504; PDBYC.
DR   AlphaFoldDB; P03872; -.
DR   DIP; DIP-7245N; -.
DR   IntAct; P03872; 2.
DR   iPTMnet; P03872; -.
DR   MaxQB; P03872; -.
DR   PeptideAtlas; P03872; -.
DR   AGR; SGD:S000029676; -.
DR   SGD; S000029676; REP2.
DR   InParanoid; P03872; -.
DR   PRO; PR:P03872; -.
DR   Proteomes; UP000002311; Plasmid 2-micron.
DR   RNAct; P03872; Protein.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0030543; P:2-micrometer plasmid partitioning; IDA:SGD.
DR   GO; GO:0050821; P:protein stabilization; IMP:SGD.
PE   1: Evidence at protein level;
KW   Acetylation; Nucleus; Plasmid; Plasmid partition; Reference proteome.
FT   CHAIN           1..296
FT                   /note="Partitioning protein REP2"
FT                   /id="PRO_0000150898"
FT   REGION          1..57
FT                   /note="Interaction with REP1"
FT   REGION          58..296
FT                   /note="DNA-binding, and self-association"
FT   REGION          228..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          276..296
FT                   /note="Nuclear localization"
FT   COMPBIAS        228..256
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..296
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
SQ   SEQUENCE   296 AA;  33196 MW;  FF54CBC6B90F5FAF CRC64;
     MDDIETAKNL TVKARTAYSV WDVCRLFIEM IAPDVDIDIE SKRKSDELLF PGYVIRPMES
     LTTGRPYGLD SSAEDSSVSS DSSAEVILPA AKMVKERFDS IGNGMLSSQE ASQAAIDLML
     QNNKLLDNRK QLYKSIAIII GRLPEKDKKR ATEMLMRKMD CTQLLVPPAP TEEDVMKLVS
     VVTQLLTLVP PDRQAALIGD LFIPESLKDI FNSFNELAAE NRLQQKKSEL EGRTEVNHAN
     TNEEVPSRRT RSRDTNARGA YKLQNTITEG PKAVPTKKRR VATRVRGRKS RNTSRV
//