REP1_YEAST
ID REP1_YEAST Reviewed; 373 AA.
AC P03871; Q04137; Q07007;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Partitioning protein REP1;
DE Short=R1;
DE AltName: Full=Protein Baker;
DE AltName: Full=Trans-acting factor B;
GN Name=REP1; OrderedLocusNames=R0020C;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 44827 / SKQ2N;
RX PubMed=2197179; DOI=10.1016/0378-1119(90)90217-f;
RA Neuville P., Bonneu M., Aigle M.;
RT "Heterogeneity among the 2 microns plasmids in Saccharomyces cerevisiae: a
RT new sequence for the REP1 gene.";
RL Gene 89:139-144(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 7754;
RX PubMed=1672551; DOI=10.1007/bf02515386;
RA Xiao W., Pelcher L.E., Rank G.H.;
RT "Evidence for cis- and trans-acting element coevolution of the 2-microns
RT circle genome in Saccharomyces cerevisiae.";
RL J. Mol. Evol. 32:145-152(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 330-373.
RX PubMed=386282; DOI=10.1093/nar/7.2.361;
RA Hindley J., Phear G.A.;
RT "Sequence of 1019 nucleotides encompassing one of the inverted repeats from
RT the yeast 2 micrometer plasmid.";
RL Nucleic Acids Res. 7:361-375(1979).
RN [5]
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 [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH REP2.
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 [7]
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 [8]
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 [9]
RP INTERACTION WITH REP2.
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 [10]
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 [11]
RP FUNCTION, INTERACTION WITH REP2 AND STB, AND MUTAGENESIS OF THR-32; TYR-43;
RP ALA-50; VAL-78; SER-93; LEU-154; GLU-200; ALA-276; LYS-297; TYR-301;
RP ILE-308; TYR-317 AND SER-330.
RX PubMed=15169893; DOI=10.1128/mcb.24.12.5290-5303.2004;
RA Yang X.-M., Mehta S., Uzri D., Jayaram M., Velmurugan S.;
RT "Mutations in a partitioning protein and altered chromatin structure at the
RT partitioning locus prevent cohesin recruitment by the Saccharomyces
RT cerevisiae plasmid and cause plasmid missegregation.";
RL Mol. Cell. Biol. 24:5290-5303(2004).
RN [12]
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).
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:15169893, ECO:0000269|PubMed:16966420,
CC ECO:0000269|PubMed:2832156}.
CC -!- SUBUNIT: Interacts with REP2. {ECO:0000269|PubMed:11244071,
CC ECO:0000269|PubMed:15169893, ECO:0000269|PubMed:9393716}.
CC -!- INTERACTION:
CC P03871; P03871: REP1; NbExp=5; IntAct=EBI-14929, EBI-14929;
CC P03871; P03872: REP2; NbExp=7; IntAct=EBI-14929, 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.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA34966.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA39080.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; J01347; AAB59341.1; -; Genomic_DNA.
DR EMBL; M31942; AAA34966.1; ALT_INIT; Genomic_DNA.
DR EMBL; X55437; CAA39080.1; ALT_INIT; Genomic_DNA.
DR PIR; A04503; PDBYB.
DR PIR; S11187; S11187.
DR PIR; S40417; S40417.
DR AlphaFoldDB; P03871; -.
DR DIP; DIP-7698N; -.
DR IntAct; P03871; 11.
DR iPTMnet; P03871; -.
DR MaxQB; P03871; -.
DR PRIDE; P03871; -.
DR SGD; S000029675; REP1.
DR InParanoid; P03871; -.
DR PRO; PR:P03871; -.
DR Proteomes; UP000002311; Plasmid 2-micron.
DR RNAct; P03871; 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:0008104; P:protein localization; IDA:SGD.
DR InterPro; IPR008897; Rep_fungi.
DR Pfam; PF05797; Rep_4; 1.
PE 1: Evidence at protein level;
KW Nucleus; Plasmid; Plasmid partition; Reference proteome.
FT CHAIN 1..373
FT /note="Partitioning protein REP1"
FT /id="PRO_0000150892"
FT REGION 1..129
FT /note="Interaction with REP2 and self-association"
FT REGION 1..76
FT /note="Interaction with REP2"
FT REGION 349..373
FT /note="Nuclear localization"
FT VARIANT 8
FT /note="A -> V (in strain: ATCC 44827 and ATCC 7754)"
FT VARIANT 22
FT /note="V -> I (in strain: ATCC 44827 and ATCC 7754)"
FT VARIANT 38
FT /note="P -> S (in strain: ATCC 44827 and ATCC 7754)"
FT VARIANT 87
FT /note="I -> R (in strain: ATCC 44827 and ATCC 7754)"
FT VARIANT 107
FT /note="T -> A (in strain: ATCC 44827 and ATCC 7754)"
FT VARIANT 111..123
FT /note="GLDINVKGTLNRR -> VRYQCKRHVKPQ (in strain: ATCC
FT 44827)"
FT VARIANT 117
FT /note="K -> R (in strain: ATCC 7754)"
FT VARIANT 131..132
FT /note="KG -> N (in strain: ATCC 44827)"
FT VARIANT 149
FT /note="A -> D (in strain: ATCC 44827 and ATCC 7754)"
FT VARIANT 177
FT /note="Q -> K (in strain: ATCC 44827 and ATCC 7754)"
FT VARIANT 184
FT /note="P -> Q (in strain: ATCC 44827 and ATCC 7754)"
FT VARIANT 198
FT /note="I -> V (in strain: ATCC 44827 and ATCC 7754)"
FT VARIANT 204
FT /note="K -> R (in strain: ATCC 44827 and ATCC 7754)"
FT VARIANT 211..214
FT /note="DKGH -> GL (in strain: ATCC 44827 and ATCC 7754)"
FT VARIANT 220..222
FT /note="LPP -> QPR (in strain: ATCC 44827)"
FT VARIANT 225..228
FT /note="DPSR -> NSSP (in strain: ATCC 44827)"
FT VARIANT 231
FT /note="N -> S (in strain: ATCC 44827)"
FT VARIANT 239..241
FT /note="SLT -> NLI (in strain: ATCC 44827 and ATCC 7754)"
FT VARIANT 246
FT /note="E -> A (in strain: ATCC 44827 and ATCC 7754)"
FT VARIANT 253
FT /note="G -> S (in strain: ATCC 44827 and ATCC 7754)"
FT VARIANT 261
FT /note="K -> R (in strain: ATCC 7754)"
FT VARIANT 270
FT /note="T -> A (in strain: ATCC 44827 and ATCC 7754)"
FT VARIANT 372..373
FT /note="DG -> NE (in strain: ATCC 44827 and ATCC 7754)"
FT MUTAGEN 32
FT /note="T->K: Abolishes interaction with REP2 and STB."
FT /evidence="ECO:0000269|PubMed:15169893"
FT MUTAGEN 43
FT /note="Y->A: Abolishes interaction with REP2, but not with
FT STB."
FT /evidence="ECO:0000269|PubMed:15169893"
FT MUTAGEN 50
FT /note="A->D: Abolishes interaction with REP2, but not with
FT STB."
FT /evidence="ECO:0000269|PubMed:15169893"
FT MUTAGEN 78
FT /note="V->K: Abolishes interaction with REP2, but not with
FT STB."
FT /evidence="ECO:0000269|PubMed:15169893"
FT MUTAGEN 93
FT /note="S->Y: Abolishes interaction with REP2, but not with
FT STB."
FT /evidence="ECO:0000269|PubMed:15169893"
FT MUTAGEN 154
FT /note="L->S: Abolishes interaction with STB, but not with
FT REP2."
FT /evidence="ECO:0000269|PubMed:15169893"
FT MUTAGEN 200
FT /note="E->A: Abolishes interaction with REP2, but not with
FT STB."
FT /evidence="ECO:0000269|PubMed:15169893"
FT MUTAGEN 276
FT /note="A->P: Abolishes interaction with REP2, but not with
FT STB."
FT /evidence="ECO:0000269|PubMed:15169893"
FT MUTAGEN 297
FT /note="K->Q: Abolishes interaction with STB, but not with
FT REP2."
FT /evidence="ECO:0000269|PubMed:15169893"
FT MUTAGEN 301
FT /note="Y->L: Abolishes interaction with REP2, but not with
FT STB."
FT /evidence="ECO:0000269|PubMed:15169893"
FT MUTAGEN 308
FT /note="I->Y: Abolishes interaction with REP2, but not with
FT STB."
FT /evidence="ECO:0000269|PubMed:15169893"
FT MUTAGEN 317
FT /note="Y->I: Abolishes interaction with STB, but not with
FT REP2."
FT /evidence="ECO:0000269|PubMed:15169893"
FT MUTAGEN 330
FT /note="S->Y: Abolishes interaction with STB, but not with
FT REP2."
FT /evidence="ECO:0000269|PubMed:15169893"
SQ SEQUENCE 373 AA; 43231 MW; FD52FC966A3BA11E CRC64;
MNGERLLACI KQCIMQHFQP MVYDESRCVI ETTRGTFPVP DNYKKYKTLA FAFVGHVLNT
DDTPVIEKEL DWPDPALVYN TIVDRIINHP ELSQFISVAF ISQLKATIGE GLDINVKGTL
NRRGKGIRRP KGVFFRYMES PFVNTKVTAF FSYLRDYNKI ASEYHNNTKF ILTFSCQAYW
ASGPNFSALK NVIRCSIIHE YISKFVEREQ DKGHIGDQEL PPEEDPSREL NNVQHEVNSL
TEQDAEADEG LWGEIDSLCE KWQSEAEDQT EAEIIADRII GNSQRMANLK IRRTKFKSVL
YHILKELIQS QGTVKVYRGS SFSHDSIKIS LHYEEQHITA VWVYLTVKFE EHWKPVDVEV
EFRCKFKERK VDG
