REC8_MOUSE
ID REC8_MOUSE Reviewed; 591 AA.
AC Q8C5S7; Q3UIN9; Q9JK52;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Meiotic recombination protein REC8 homolog;
DE AltName: Full=Cohesin Rec8p;
GN Name=Rec8; Synonyms=Mei8, Rec8L1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Beasley M., Warren W., McKay M.J.;
RT "mrec8, a meiotic homolog of the rad21 cohesin family.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=10207075; DOI=10.1128/mcb.19.5.3515;
RA Parisi S., McKay M.J., Molnar M., Thompson M.A., van der Spek P.J.,
RA van Drunen-Schoenmaker E., Kanaar R., Lehmann E., Hoeijmakers J.H.J.,
RA Kohli J.;
RT "Rec8p, a meiotic recombination and sister chromatid cohesion
RT phosphoprotein of the Rad21p family conserved from fission yeast to
RT humans.";
RL Mol. Cell. Biol. 19:3515-3528(1999).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12034751; DOI=10.1093/embo-reports/kvf108;
RA Prieto I., Pezzi N., Buesa J.M., Kremer L., Barthelemy I., Carreiro C.,
RA Roncal F., Martinez A., Gomez L., Fernandez R., Martinez-A C.,
RA Barbero J.L.;
RT "STAG2 and Rad21 mammalian mitotic cohesins are implicated in meiosis.";
RL EMBO Rep. 3:543-550(2002).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=12130806; DOI=10.2108/zsj.19.539;
RA Lee J., Yokota T., Yamashita M.;
RT "Analyses of mRNA expression patterns of cohesin subunits Rad21 and Rec8 in
RT mice: germ cell-specific expression of rec8 mRNA in both male and female
RT mice.";
RL Zool. Sci. 19:539-544(2002).
RN [7]
RP INTERACTION WITH SMC1B; SMC3 AND SYCP3, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND PHOSPHORYLATION.
RX PubMed=12759374; DOI=10.1242/jcs.00495;
RA Lee J., Iwai T., Yokota T., Yamashita M.;
RT "Temporally and spatially selective loss of Rec8 protein from meiotic
RT chromosomes during mammalian meiosis.";
RL J. Cell Sci. 116:2781-2790(2003).
RN [8]
RP FUNCTION.
RX PubMed=15515002; DOI=10.1002/gene.20085;
RA Bannister L.A., Reinholdt L.G., Munroe R.J., Schimenti J.C.;
RT "Positional cloning and characterization of mouse mei8, a disrupted allelle
RT of the meiotic cohesin Rec8.";
RL Genesis 40:184-194(2004).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15935783; DOI=10.1016/j.devcel.2005.03.018;
RA Xu H., Beasley M.D., Warren W.D., van der Horst G.T.J., McKay M.J.;
RT "Absence of mouse REC8 cohesin promotes synapsis of sister chromatids in
RT meiosis.";
RL Dev. Cell 8:949-961(2005).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16855401; DOI=10.4161/cc.5.13.2903;
RA Lee J., Okada K., Ogushi S., Miyano T., Miyake M., Yamashita M.;
RT "Loss of Rec8 from chromosome arm and centromere region is required for
RT homologous chromosome separation and sister chromatid separation,
RT respectively, in mammalian meiosis.";
RL Cell Cycle 5:1448-1455(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [12]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=22346761; DOI=10.1371/journal.pgen.1002485;
RA Fukuda T., Pratto F., Schimenti J.C., Turner J.M., Camerini-Otero R.D.,
RA Hoeoeg C.;
RT "Phosphorylation of chromosome core components may serve as axis marks for
RT the status of chromosomal events during mammalian meiosis.";
RL PLoS Genet. 8:E1002485-E1002485(2012).
RN [13]
RP INTERACTION WITH PRDM9; EWSR1; SYCP3 AND SYCP1.
RX PubMed=27932493; DOI=10.1091/mbc.e16-09-0686;
RA Parvanov E.D., Tian H., Billings T., Saxl R.L., Spruce C., Aithal R.,
RA Krejci L., Paigen K., Petkov P.M.;
RT "PRDM9 interactions with other proteins provide a link between
RT recombination hotspots and the chromosomal axis in meiosis.";
RL Mol. Biol. Cell 28:488-499(2017).
CC -!- FUNCTION: Required during meiosis for separation of sister chromatids
CC and homologous chromosomes. Proteolytic cleavage of REC8 on chromosome
CC arms by separin during anaphase I allows for homologous chromosome
CC separation in meiosis I and cleavage of REC8 on centromeres during
CC anaphase II allows for sister chromatid separation in meiosis II.
CC {ECO:0000269|PubMed:12034751, ECO:0000269|PubMed:15515002,
CC ECO:0000269|PubMed:15935783, ECO:0000269|PubMed:16855401}.
CC -!- SUBUNIT: Interacts (phosphorylated and unphosphorylated form) with
CC SMC3. Interacts with SYCP3. Interacts (phosphorylated and
CC unphosphorylated form) with SMC1B. Does not interact with SMC1A.
CC Interacts with RAD51. Forms a complex with EWSR1, PRDM9, SYCP3 and
CC SYCP1; complex formation is dependent of phosphorylated form of REC8
CC and requires PRDM9 bound to hotspot DNA; EWSR1 joins PRDM9 with the
CC chromosomal axis through REC8 (PubMed:27932493).
CC {ECO:0000269|PubMed:12759374, ECO:0000269|PubMed:27932493}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12034751,
CC ECO:0000269|PubMed:12759374, ECO:0000269|PubMed:16855401,
CC ECO:0000269|PubMed:22346761}. Chromosome {ECO:0000269|PubMed:12034751,
CC ECO:0000269|PubMed:12759374, ECO:0000269|PubMed:16855401,
CC ECO:0000269|PubMed:22346761}. Chromosome, centromere
CC {ECO:0000269|PubMed:12034751, ECO:0000269|PubMed:12759374,
CC ECO:0000269|PubMed:16855401, ECO:0000269|PubMed:22346761}. Note=In
CC meiotic chromosomes, localized along axial elements in prophase from
CC the leptotene to diplotene stages. At later prophase stages, diakinesis
CC and metaphase I, localized along interstitial axes of chromosomes
CC including both centromere and arm regions. No longer detected in arm
CC regions in anaphase I but persists on centromere regions until
CC metaphase II. {ECO:0000269|PubMed:12034751,
CC ECO:0000269|PubMed:12759374, ECO:0000269|PubMed:16855401,
CC ECO:0000269|PubMed:22346761}.
CC -!- TISSUE SPECIFICITY: Expressed primarily in the gonads. In the testis,
CC expressed in pachytene spermatocytes and in spermatids. Not expressed
CC in spermatogonia or somatic cells. In the ovary, expressed only in
CC oocytes. Low levels also detected in a number of somatic tissues
CC including thymus, lung, liver, kidney and small intestine.
CC {ECO:0000269|PubMed:10207075, ECO:0000269|PubMed:12130806,
CC ECO:0000269|PubMed:12759374, ECO:0000269|PubMed:15935783}.
CC -!- DEVELOPMENTAL STAGE: Expressed from 2 weeks postpartum (at protein
CC level). {ECO:0000269|PubMed:12759374}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:12759374,
CC ECO:0000269|PubMed:22346761}.
CC -!- DISRUPTION PHENOTYPE: Mice display a high mortality rate, both during
CC embryogenesis and after birth, germ cell failure and sterility. Mutant
CC females exhibit ovarian dysgenesis and lack ovarian follicles at
CC reproductive maturity. Affected males have small testes due to arrest
CC of spermatogenesis during meiotic prophase I. Early chromosome pairing
CC appears normal but synapsis occurs between sister chromatids rather
CC than between homologous chromosomes. {ECO:0000269|PubMed:15935783}.
CC -!- SIMILARITY: Belongs to the rad21 family. {ECO:0000305}.
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DR EMBL; AF262055; AAF69524.1; -; mRNA.
DR EMBL; AK077167; BAC36657.1; -; mRNA.
DR EMBL; AK146832; BAE27467.1; -; mRNA.
DR EMBL; BC052155; AAH52155.1; -; mRNA.
DR CCDS; CCDS27120.1; -.
DR RefSeq; NP_064386.2; NM_020002.3.
DR AlphaFoldDB; Q8C5S7; -.
DR SMR; Q8C5S7; -.
DR BioGRID; 208153; 1.
DR CORUM; Q8C5S7; -.
DR DIP; DIP-60730N; -.
DR IntAct; Q8C5S7; 5.
DR MINT; Q8C5S7; -.
DR STRING; 10090.ENSMUSP00000002395; -.
DR iPTMnet; Q8C5S7; -.
DR PhosphoSitePlus; Q8C5S7; -.
DR PaxDb; Q8C5S7; -.
DR PeptideAtlas; Q8C5S7; -.
DR PRIDE; Q8C5S7; -.
DR ProteomicsDB; 254910; -.
DR Antibodypedia; 22688; 248 antibodies from 29 providers.
DR DNASU; 56739; -.
DR Ensembl; ENSMUST00000002395; ENSMUSP00000002395; ENSMUSG00000002324.
DR GeneID; 56739; -.
DR KEGG; mmu:56739; -.
DR UCSC; uc007tzo.2; mouse.
DR CTD; 9985; -.
DR MGI; MGI:1929645; Rec8.
DR VEuPathDB; HostDB:ENSMUSG00000002324; -.
DR eggNOG; KOG1213; Eukaryota.
DR GeneTree; ENSGT00390000011379; -.
DR HOGENOM; CLU_036680_0_0_1; -.
DR InParanoid; Q8C5S7; -.
DR OMA; RVYFQQC; -.
DR OrthoDB; 1582475at2759; -.
DR PhylomeDB; Q8C5S7; -.
DR TreeFam; TF338144; -.
DR BioGRID-ORCS; 56739; 6 hits in 108 CRISPR screens.
DR PRO; PR:Q8C5S7; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8C5S7; protein.
DR Bgee; ENSMUSG00000002324; Expressed in spermatid and 122 other tissues.
DR Genevisible; Q8C5S7; MM.
DR GO; GO:0008278; C:cohesin complex; IBA:GO_Central.
DR GO; GO:0000793; C:condensed chromosome; IDA:MGI.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:MGI.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:MGI.
DR GO; GO:0000776; C:kinetochore; IDA:MGI.
DR GO; GO:0000800; C:lateral element; IDA:MGI.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0030893; C:meiotic cohesin complex; IDA:MGI.
DR GO; GO:0034991; C:nuclear meiotic cohesin complex; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0000795; C:synaptonemal complex; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IGI:MGI.
DR GO; GO:0009566; P:fertilization; IMP:MGI.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IMP:MGI.
DR GO; GO:0007141; P:male meiosis I; IMP:MGI.
DR GO; GO:0051321; P:meiotic cell cycle; IPI:MGI.
DR GO; GO:0051177; P:meiotic sister chromatid cohesion; IBA:GO_Central.
DR GO; GO:0001556; P:oocyte maturation; IMP:MGI.
DR GO; GO:0072520; P:seminiferous tubule development; IGI:MGI.
DR GO; GO:0007062; P:sister chromatid cohesion; IBA:GO_Central.
DR GO; GO:0007286; P:spermatid development; IMP:MGI.
DR GO; GO:0007130; P:synaptonemal complex assembly; IGI:MGI.
DR Gene3D; 1.10.10.580; -; 1.
DR InterPro; IPR039781; Rad21/Rec8-like.
DR InterPro; IPR006909; Rad21/Rec8_C_eu.
DR InterPro; IPR006910; Rad21_Rec8_N.
DR InterPro; IPR023093; ScpA-like_C.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR12585; PTHR12585; 1.
DR Pfam; PF04824; Rad21_Rec8; 1.
DR Pfam; PF04825; Rad21_Rec8_N; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW Centromere; Chromosome; Chromosome partition; Meiosis; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..591
FT /note="Meiotic recombination protein REC8 homolog"
FT /id="PRO_0000097879"
FT REGION 163..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 164
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYJ4"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYJ4"
FT CONFLICT 49
FT /note="V -> E (in Ref. 1; AAF69524)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 591 AA; 67425 MW; 622986F564735700 CRC64;
MFYYPNVLQR HTGCFATIWL AATRGSRLVK REYLNVNVVK TCEEILNYVL VRVQPPVAGL
PRPRFSLYLS AQLQIGVIRV YFQQCQYLVE DIQHILEHLH RAQLRIRIDM EEADLPSLLL
PNCLAMMETL EDAPEPFFGK MSVDPRLPSP FDIPQIRHLL EAATPEKTRK ETLPEATPDP
RKPDRTLATV QSPEVITLQE AEPIRMLQIE GEQDLPEISR GDLELLIAEK DDAILLEERQ
RGRLLRQRRA SLPLDESREE PRALEGAGLV SALSPPAPAQ VEGIQEALPG QVFPPEVQKM
TGWEPGALLT EVTPPQELRL PAPPSTEKRL PSLQRPLPRR HRRRQLLFWD KETQISREKF
EEQLQTGAHC WEYPVAQPPK RMLTSPAELF RTPTLSGWLP PELLGLWTHC AQVPQRMLRQ
RPQLETEETV EEERAADEEE RRKTEALSEI EVLREAQEPS GPLMLSSELS LEAAEDEKSR
TSLIPPEWWA WSEEGQPEPP ALPMLPELPE VPMEMPPRPE LSSEAVLRAV ALKLQANKEL
DFSSLVPPLS PRKLASRVFY LLLVLSTQKI LLVEQQKPYG PLLIRPGPKF P
