RE114_MOUSE
ID RE114_MOUSE Reviewed; 259 AA.
AC Q9CWH4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Meiotic recombination protein REC114;
GN Name=Rec114;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP FUNCTION, INTERACTION WITH MEI4, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=20551173; DOI=10.1101/gad.571710;
RA Kumar R., Bourbon H.M., de Massy B.;
RT "Functional conservation of Mei4 for meiotic DNA double-strand break
RT formation from yeasts to mice.";
RL Genes Dev. 24:1266-1280(2010).
RN [4]
RP FUNCTION, IDENTIFICATION IN THE MCD RECOMBINOSOME COMPLEX, AND INTERACTION
RP WITH IHO1.
RX PubMed=27723721; DOI=10.1038/ncb3417;
RA Stanzione M., Baumann M., Papanikos F., Dereli I., Lange J., Ramlal A.,
RA Traenkner D., Shibuya H., de Massy B., Watanabe Y., Jasin M., Keeney S.,
RA Toth A.;
RT "Meiotic DNA break formation requires the unsynapsed chromosome axis-
RT binding protein IHO1 (CCDC36) in mice.";
RL Nat. Cell Biol. 18:1208-1220(2016).
RN [5]
RP INTERACTION WITH ANKRD31.
RX PubMed=31000436; DOI=10.1016/j.molcel.2019.03.022;
RA Papanikos F., Clement J.A.J., Testa E., Ravindranathan R., Grey C.,
RA Dereli I., Bondarieva A., Valerio-Cabrera S., Stanzione M., Schleiffer A.,
RA Jansa P., Lustyk D., Fei J.F., Adams I.R., Forejt J., Barchi M.,
RA de Massy B., Toth A.;
RT "Mouse ANKRD31 regulates spatiotemporal patterning of meiotic recombination
RT initiation and ensures recombination between X and Y sex chromosomes.";
RL Mol. Cell 0:0-0(2019).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) OF 1-158 IN COMPLEX WITH ANKRD31,
RP INTERACTION WITH ANKRD31, AND MUTAGENESIS OF ARG-27; PHE-28; PHE-74; LEU-81
RP AND LEU-104.
RX PubMed=31003867; DOI=10.1016/j.molcel.2019.03.023;
RA Boekhout M., Karasu M.E., Wang J., Acquaviva L., Pratto F., Brick K.,
RA Eng D.Y., Xu J., Camerini-Otero R.D., Patel D.J., Keeney S.;
RT "REC114 partner ANKRD31 controls number, timing, and location of meiotic
RT DNA breaks.";
RL Mol. Cell 0:0-0(2019).
CC -!- FUNCTION: Required for DNA double-strand breaks (DSBs) formation in
CC unsynapsed regions during meiotic recombination (PubMed:20551173,
CC PubMed:27723721). Probably acts by forming a complex with IHO1 and
CC MEI4, which activates DSBs formation in unsynapsed regions, an
CC essential step to ensure completion of synapsis (PubMed:27723721).
CC {ECO:0000269|PubMed:20551173, ECO:0000269|PubMed:27723721}.
CC -!- SUBUNIT: Interacts with MEI4 (PubMed:20551173). Interacts with IHO1
CC (PubMed:27723721). Part of the MCD recombinosome complex, at least
CC composed of IHO1, REC114 and MEI4 (PubMed:27723721). Interacts with
CC ANKRD31; the interaction is direct (PubMed:31000436, PubMed:31003867).
CC {ECO:0000269|PubMed:20551173, ECO:0000269|PubMed:27723721,
CC ECO:0000269|PubMed:31000436, ECO:0000269|PubMed:31003867}.
CC -!- INTERACTION:
CC Q9CWH4; Q8BRM6: Mei4; NbExp=5; IntAct=EBI-9548270, EBI-9548252;
CC -!- TISSUE SPECIFICITY: Expressed in adult testis and embryonic ovary. Also
CC expressed at low levels in liver. {ECO:0000269|PubMed:20551173}.
CC -!- DEVELOPMENTAL STAGE: In the testis, expression is detected at 4 days
CC postpartum (dpp) with a peak at day 10. Levels decrease between 14-18
CC dpp with an increase in the adult. {ECO:0000269|PubMed:20551173}.
CC -!- SIMILARITY: Belongs to the REC114 family. {ECO:0000305}.
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DR EMBL; AK010725; BAB27143.1; -; mRNA.
DR EMBL; AC140054; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC159102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT030640; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS52814.1; -.
DR RefSeq; NP_082874.1; NM_028598.1.
DR PDB; 6HFG; X-ray; 2.50 A; B=15-159.
DR PDB; 6NXF; X-ray; 2.79 A; A/B=1-158.
DR PDBsum; 6HFG; -.
DR PDBsum; 6NXF; -.
DR AlphaFoldDB; Q9CWH4; -.
DR SMR; Q9CWH4; -.
DR BioGRID; 216182; 1.
DR IntAct; Q9CWH4; 1.
DR STRING; 10090.ENSMUSP00000096271; -.
DR PhosphoSitePlus; Q9CWH4; -.
DR MaxQB; Q9CWH4; -.
DR PaxDb; Q9CWH4; -.
DR PRIDE; Q9CWH4; -.
DR Ensembl; ENSMUST00000098674; ENSMUSP00000096271; ENSMUSG00000074269.
DR GeneID; 73673; -.
DR KEGG; mmu:73673; -.
DR UCSC; uc009pxh.2; mouse.
DR CTD; 283677; -.
DR MGI; MGI:1920923; Rec114.
DR VEuPathDB; HostDB:ENSMUSG00000074269; -.
DR eggNOG; ENOG502S157; Eukaryota.
DR GeneTree; ENSGT00390000007235; -.
DR HOGENOM; CLU_101822_0_0_1; -.
DR InParanoid; Q9CWH4; -.
DR OMA; GHFFISH; -.
DR OrthoDB; 1491802at2759; -.
DR PhylomeDB; Q9CWH4; -.
DR TreeFam; TF332765; -.
DR BioGRID-ORCS; 73673; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q9CWH4; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9CWH4; protein.
DR Bgee; ENSMUSG00000074269; Expressed in blood and 114 other tissues.
DR ExpressionAtlas; Q9CWH4; baseline and differential.
DR Genevisible; Q9CWH4; MM.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR InterPro; IPR029168; REC114L.
DR PANTHER; PTHR34921; PTHR34921; 1.
DR Pfam; PF15165; REC114-like; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA recombination; Meiosis; Reference proteome.
FT CHAIN 1..259
FT /note="Meiotic recombination protein REC114"
FT /id="PRO_0000321519"
FT REGION 150..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 27
FT /note="R->A: Strongly reduced interaction with ANKRD31."
FT /evidence="ECO:0000269|PubMed:31003867"
FT MUTAGEN 28
FT /note="F->A: Strongly reduced interaction with ANKRD31;
FT when associated with A-104."
FT /evidence="ECO:0000269|PubMed:31003867"
FT MUTAGEN 74
FT /note="F->A: Strongly reduced interaction with ANKRD31;
FT when associated with A-81."
FT /evidence="ECO:0000269|PubMed:31003867"
FT MUTAGEN 81
FT /note="L->A: Strongly reduced interaction with ANKRD31;
FT when associated with A-74."
FT /evidence="ECO:0000269|PubMed:31003867"
FT MUTAGEN 104
FT /note="L->A: Strongly reduced interaction with ANKRD31;
FT when associated with A-28."
FT /evidence="ECO:0000269|PubMed:31003867"
FT STRAND 15..28
FT /evidence="ECO:0007829|PDB:6HFG"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:6HFG"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:6HFG"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:6HFG"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:6HFG"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:6HFG"
FT TURN 88..93
FT /evidence="ECO:0007829|PDB:6HFG"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:6HFG"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:6HFG"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:6HFG"
FT HELIX 125..139
FT /evidence="ECO:0007829|PDB:6HFG"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:6HFG"
SQ SEQUENCE 259 AA; 28211 MW; 26FB5D90CA9B010D CRC64;
MSEAGNVASG LGLPGEVSQW SLKRYGRFML LDNVGSPGPS SEAAAAGSPT WKVFESSEES
GSLVLTIVVS GHFFISQGQT LLEGFSLIGS KNWLKIVRRM DCLLFGTTIK NKSRMFRVQF
SGESKEEALE RCCGCVQTLA QYVTVQEPDS TTQELQQSQG PREAGESQGK DPLQQGPSLT
LEQHVCMAAG AGVLQERTSV THRAQSILAP EKLTLAYEGS SWGTEELGPF LRLCLMDQNF
PAFVEEVEKE LKKITGLRN
