REC8_YEAST
ID REC8_YEAST Reviewed; 680 AA.
AC Q12188; D6W418;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Meiotic recombination protein REC8 {ECO:0000303|PubMed:10412984};
DE AltName: Full=Cohesin REC8 {ECO:0000303|PubMed:10412984};
DE AltName: Full=Sporulation protein 69 {ECO:0000303|PubMed:9784122};
GN Name=REC8 {ECO:0000303|PubMed:10412984};
GN Synonyms=SPO69 {ECO:0000303|PubMed:9784122}; OrderedLocusNames=YPR007C;
GN ORFNames=LPZ7C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2996783; DOI=10.1016/0092-8674(85)90287-9;
RA Hieter P., Pridmore D., Hegemann J.H., Thomas M., Davis R.W.,
RA Philippsen P.;
RT "Functional selection and analysis of yeast centromeric DNA.";
RL Cell 42:913-921(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION, AND INDUCTION.
RX PubMed=9784122; DOI=10.1126/science.282.5389.699;
RA Chu S., DeRisi J., Eisen M., Mulholland J., Botstein D., Brown P.O.,
RA Herskowitz I.;
RT "The transcriptional program of sporulation in budding yeast.";
RL Science 282:699-705(1998).
RN [5]
RP FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10412984; DOI=10.1016/s0092-8674(00)80609-1;
RA Klein F., Mahr P., Galova M., Buonomo S.B.C., Michaelis C., Nairz K.,
RA Nasmyth K.;
RT "A central role for cohesins in sister chromatid cohesion, formation of
RT axial elements, and recombination during yeast meiosis.";
RL Cell 98:91-103(1999).
RN [6]
RP FUNCTION, CLEAVAGE BY ESP1, AND MUTAGENESIS OF GLU-428; ARG-431 AND
RP ARG-453.
RX PubMed=11081626; DOI=10.1016/s0092-8674(00)00131-8;
RA Buonomo S.B.C., Clyne R.K., Fuchs J., Loidl J., Uhlmann F., Nasmyth K.;
RT "Disjunction of homologous chromosomes in meiosis I depends on proteolytic
RT cleavage of the meiotic cohesin Rec8 by separin.";
RL Cell 103:387-398(2000).
RN [7]
RP FUNCTION.
RX PubMed=11163190; DOI=10.1016/s0092-8674(00)00217-8;
RA Toth A., Rabitsch K.P., Galova M., Schleiffer A., Buonomo S.B.C.,
RA Nasmyth K.;
RT "Functional genomics identifies monopolin: a kinetochore protein required
RT for segregation of homologs during meiosis I.";
RL Cell 103:1155-1168(2000).
RN [8]
RP FUNCTION.
RX PubMed=10691741;
RA Cha R.S., Weiner B.M., Keeney S., Dekker J., Kleckner N.;
RT "Progression of meiotic DNA replication is modulated by interchromosomal
RT interaction proteins, negatively by Spo11p and positively by Rec8p.";
RL Genes Dev. 14:493-503(2000).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12101124; DOI=10.1101/gad.975802;
RA Shonn M.A., McCarroll R., Murray A.W.;
RT "Spo13 protects meiotic cohesin at centromeres in meiosis I.";
RL Genes Dev. 16:1659-1671(2002).
RN [10]
RP FUNCTION.
RX PubMed=12665553; DOI=10.1242/jcs.00387;
RA Molnar M., Doll E., Yamamoto A., Hiraoka Y., Kohli J.;
RT "Linear element formation and their role in meiotic sister chromatid
RT cohesion and chromosome pairing.";
RL J. Cell Sci. 116:1719-1731(2003).
RN [11]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=12717442; DOI=10.1038/ncb977;
RA Clyne R.K., Katis V.L., Jessop L., Benjamin K.R., Herskowitz I.,
RA Lichten M., Nasmyth K.;
RT "Polo-like kinase Cdc5 promotes chiasmata formation and cosegregation of
RT sister centromeres at meiosis I.";
RL Nat. Cell Biol. 5:480-485(2003).
RN [12]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=12663816; DOI=10.1126/science.1081846;
RA Lee B.H., Amon A.;
RT "Role of Polo-like kinase CDC5 in programming meiosis I chromosome
RT segregation.";
RL Science 300:482-486(2003).
RN [13]
RP FUNCTION.
RX PubMed=15062096; DOI=10.1016/j.cub.2004.03.001;
RA Katis V.L., Galova M., Rabitsch K.P., Gregan J., Nasmyth K.;
RT "Maintenance of cohesin at centromeres after meiosis I in budding yeast
RT requires a kinetochore-associated protein related to MEI-S332.";
RL Curr. Biol. 14:560-572(2004).
RN [14]
RP FUNCTION.
RX PubMed=15120066; DOI=10.1016/j.cub.2004.04.030;
RA Zierhut C., Berlinger M., Rupp C., Shinohara A., Klein F.;
RT "Mnd1 is required for meiotic interhomolog repair.";
RL Curr. Biol. 14:752-762(2004).
RN [15]
RP FUNCTION.
RX PubMed=15620644; DOI=10.1016/j.cub.2004.12.033;
RA Lee B.H., Kiburz B.M., Amon A.;
RT "Spo13 maintains centromeric cohesion and kinetochore coorientation during
RT meiosis I.";
RL Curr. Biol. 14:2168-2182(2004).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=16269332; DOI=10.1016/j.cell.2005.09.014;
RA Yu H.-G., Koshland D.;
RT "Chromosome morphogenesis: condensin-dependent cohesin removal during
RT meiosis.";
RL Cell 123:397-407(2005).
RN [17]
RP FUNCTION.
RX PubMed=16027219; DOI=10.1083/jcb.200501042;
RA Trelles-Sticken E., Adelfalk C., Loidl J., Scherthan H.;
RT "Meiotic telomere clustering requires actin for its formation and cohesin
RT for its resolution.";
RL J. Cell Biol. 170:213-223(2005).
RN [18]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15819623; DOI=10.1111/j.1365-2958.2005.04582.x;
RA Zhang Z., Ren Q., Yang H., Conrad M.N., Guacci V., Kateneva A.,
RA Dresser M.E.;
RT "Budding yeast PDS5 plays an important role in meiosis and is required for
RT sister chromatid cohesion.";
RL Mol. Microbiol. 56:670-680(2005).
RN [19]
RP FUNCTION, INTERACTION WITH MPS3, AND SUBCELLULAR LOCATION.
RX PubMed=30417519; DOI=10.1111/gtc.12653;
RA Bommi J.R., Rao H.B.D.P., Challa K., Higashide M., Shinmyozu K.,
RA Nakayama J.I., Shinohara M., Shinohara A.;
RT "Meiosis-specific cohesin component, Rec8, promotes the localization of
RT Mps3 SUN domain protein on the nuclear envelope.";
RL Genes Cells 24:94-106(2019).
CC -!- FUNCTION: Replaces the SCC1 mitosis-specific cohesin to ensure sister
CC chromatid cohesion during meiosis (PubMed:10412984, PubMed:10691741,
CC PubMed:11081626, PubMed:11163190, PubMed:12101124, PubMed:12663816,
CC PubMed:12665553, PubMed:12717442, PubMed:15062096, PubMed:15120066,
CC PubMed:15819623, PubMed:16027219, PubMed:9784122). Is cleaved by ESP1
CC shortly before the first meiotic division, and dissociates from
CC chromatin, allowing sister chromatids to segregate (PubMed:11081626).
CC Is protected from cleavage by SPO13 (PubMed:15620644). Promotes
CC localization of the LINC complex subunit MPS3 on nuclear envelope in
CC mitotic cells (PubMed:30417519). {ECO:0000269|PubMed:10412984,
CC ECO:0000269|PubMed:10691741, ECO:0000269|PubMed:11081626,
CC ECO:0000269|PubMed:11163190, ECO:0000269|PubMed:12101124,
CC ECO:0000269|PubMed:12663816, ECO:0000269|PubMed:12665553,
CC ECO:0000269|PubMed:12717442, ECO:0000269|PubMed:15062096,
CC ECO:0000269|PubMed:15120066, ECO:0000269|PubMed:15620644,
CC ECO:0000269|PubMed:15819623, ECO:0000269|PubMed:16027219,
CC ECO:0000269|PubMed:30417519, ECO:0000269|PubMed:9784122}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10412984,
CC ECO:0000269|PubMed:12101124, ECO:0000269|PubMed:16269332,
CC ECO:0000269|PubMed:30417519}. Chromosome {ECO:0000269|PubMed:10412984,
CC ECO:0000269|PubMed:12101124, ECO:0000269|PubMed:15819623,
CC ECO:0000269|PubMed:16269332}. Chromosome, centromere
CC {ECO:0000269|PubMed:10412984, ECO:0000269|PubMed:16269332}.
CC Note=Localizes at chromosome cores during pachytene. Disappears from
CC chromosome arms shortly before the first meiotic division, but persists
CC in the vincinity of centromeres until the onset of anaphase II.
CC {ECO:0000269|PubMed:10412984, ECO:0000269|PubMed:16269332}.
CC -!- INDUCTION: During meiosis. {ECO:0000269|PubMed:10412984,
CC ECO:0000269|PubMed:9784122}.
CC -!- PTM: Proteolytically cleaved by ESP1. {ECO:0000269|PubMed:11081626}.
CC -!- PTM: Phosphorylated by CDC5. CDC5 phosphorylation is necessary for
CC cleavage by ESP1 and subsequent removal from chromosome arms.
CC {ECO:0000269|PubMed:11081626, ECO:0000269|PubMed:12663816,
CC ECO:0000269|PubMed:12717442}.
CC -!- SIMILARITY: Belongs to the rad21 family. {ECO:0000305}.
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DR EMBL; U31900; AAA97586.1; -; Genomic_DNA.
DR EMBL; Z48951; CAA88785.1; -; Genomic_DNA.
DR EMBL; Z71255; CAA95047.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11434.1; -; Genomic_DNA.
DR PIR; S52820; S52820.
DR RefSeq; NP_015332.1; NM_001184104.1.
DR AlphaFoldDB; Q12188; -.
DR BioGRID; 36184; 103.
DR ComplexPortal; CPX-1408; Nuclear meiotic cohesin complex.
DR ELM; Q12188; -.
DR IntAct; Q12188; 1.
DR MINT; Q12188; -.
DR STRING; 4932.YPR007C; -.
DR iPTMnet; Q12188; -.
DR PaxDb; Q12188; -.
DR PRIDE; Q12188; -.
DR EnsemblFungi; YPR007C_mRNA; YPR007C; YPR007C.
DR GeneID; 856115; -.
DR KEGG; sce:YPR007C; -.
DR SGD; S000006211; REC8.
DR VEuPathDB; FungiDB:YPR007C; -.
DR eggNOG; ENOG502QWJ1; Eukaryota.
DR HOGENOM; CLU_399675_0_0_1; -.
DR InParanoid; Q12188; -.
DR OMA; YGVTICY; -.
DR BioCyc; YEAST:G3O-34169-MON; -.
DR PRO; PR:Q12188; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12188; protein.
DR GO; GO:0008278; C:cohesin complex; IBA:GO_Central.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:SGD.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:SGD.
DR GO; GO:0034991; C:nuclear meiotic cohesin complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR GO; GO:0034089; P:establishment of meiotic sister chromatid cohesion; IC:ComplexPortal.
DR GO; GO:0042138; P:meiotic DNA double-strand break formation; IMP:SGD.
DR GO; GO:0051177; P:meiotic sister chromatid cohesion; IMP:SGD.
DR GO; GO:0010789; P:meiotic sister chromatid cohesion involved in meiosis I; IBA:GO_Central.
DR GO; GO:0051754; P:meiotic sister chromatid cohesion, centromeric; IBA:GO_Central.
DR GO; GO:0051455; P:monopolar spindle attachment to meiosis I kinetochore; IBA:GO_Central.
DR GO; GO:1905339; P:positive regulation of cohesin unloading; IMP:SGD.
DR GO; GO:0071459; P:protein localization to chromosome, centromeric region; IGI:SGD.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:SGD.
DR GO; GO:0007062; P:sister chromatid cohesion; IBA:GO_Central.
DR GO; GO:0007130; P:synaptonemal complex assembly; IMP:SGD.
DR InterPro; IPR039781; Rad21/Rec8-like.
DR InterPro; IPR006910; Rad21_Rec8_N.
DR PANTHER; PTHR12585; PTHR12585; 1.
DR Pfam; PF04825; Rad21_Rec8_N; 1.
PE 1: Evidence at protein level;
KW Centromere; Chromosome; Chromosome partition; Meiosis; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..680
FT /note="Meiotic recombination protein REC8"
FT /id="PRO_0000268699"
FT REGION 278..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 431..432
FT /note="Cleavage; by ESP1"
FT SITE 453..454
FT /note="Cleavage; by ESP1"
FT MUTAGEN 428
FT /note="E->R: Abolishes cleavage by ESP1 at position R-431;
FT when associated with E-431."
FT /evidence="ECO:0000269|PubMed:11081626"
FT MUTAGEN 431
FT /note="R->E: Reduces cleavage by ESP1 at position R-431.
FT Abolishes cleavage by ESP1 at position R-431; when
FT associated with R-428."
FT /evidence="ECO:0000269|PubMed:11081626"
FT MUTAGEN 453
FT /note="R->E: Abolishes cleavage by ESP1 at position R-453."
FT /evidence="ECO:0000269|PubMed:11081626"
SQ SEQUENCE 680 AA; 77202 MW; DCA8F2029724B1B6 CRC64;
MAPLSLNFKD DKKYKGLTTV WLLSALGNSI VKESNNYYSN KSNSTGNISS STVKKKDIVN
ISIPKTCDEI QNFENDFSLR YISNLLYGVT ICYNKKTEYV LNDLNHLLVQ LQKNDVYAFK
AKNKSTRING LNSNNSIIGN KNNNYTWEEC VFFDDDPLYD ITKVPALEFL NTTLQDNVSF
IEEAKSIRRQ DYINELSNSN RFELHGDMTN SDAQSNLGSN VRNSFPLDEI PVDVDFNLDL
DDIVSHQGTP LGSHSSSQKD GNDFKFNYQG DELVLNFEND NENNSNGGED TSVENEGPVA
NLKDYELGLE AQASEEENDL QQKLNTRMQR GHRADVGGQF SKVQFDAKTS YPNEVLKFNH
GNYSHLMEKN RIRKLTGQNF LTSNISSLVR SCGEEEFFST NWLSIFNDFS NIKTSEWDLY
PQGFSSVERG RKRAHSLVST QSSSSTRSHE YGRKSFRNNK NDNYSSDMEN DNLLLNLEQI
NEDLEDGHYI EENSQGNILD FNLNLPPSSF GRSHTRNSTR SSGFNEDIVG ALRRRVGPSE
QNFAEEDDSS NSCFSDGSQQ NLQQDKTNFQ DVILDYQTKK FYDYIKERSI VVGRTTRSNP
PFKRKMLLVD IIPSRMGEAQ TGANFDDVER GVSRQIAASA FLSLLNLATK GMVKLNEYPV
ADAVTKDLKL RREDEIIVYA
