REP2_YEAST
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 25-MAY-2022, entry version 96.
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 PRIDE; P03872; -.
DR SGD; S000029676; REP2.
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
