MND1_MOUSE
ID MND1_MOUSE Reviewed; 205 AA.
AC Q8K396; Q9D0A1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Meiotic nuclear division protein 1 homolog;
GN Name=Mnd1 {ECO:0000312|MGI:MGI:1924165};
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] {ECO:0000312|EMBL:BAB27765.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB27765.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:BAB27765.1};
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] {ECO:0000312|EMBL:AAH27741.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II {ECO:0000312|EMBL:AAH27741.1};
RC TISSUE=Mammary tumor {ECO:0000312|EMBL:AAH27741.1};
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 [3] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH DMC1; PSMC3IP AND RAD51.
RX PubMed=15834424; DOI=10.1038/nsmb923;
RA Petukhova G.V., Pezza R.J., Vanevski F., Ploquin M., Masson J.-Y.,
RA Camerini-Otero R.D.;
RT "The Hop2 and Mnd1 proteins act in concert with Rad51 and Dmc1 in meiotic
RT recombination.";
RL Nat. Struct. Mol. Biol. 12:449-453(2005).
RN [4] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH PSMC3IP.
RX PubMed=16675459; DOI=10.1074/jbc.m601073200;
RA Pezza R.J., Petukhova G.V., Ghirlando R., Camerini-Otero R.D.;
RT "Molecular activities of meiosis-specific proteins Hop2, Mnd1, and the
RT Hop2-Mnd1 complex.";
RL J. Biol. Chem. 281:18426-18434(2006).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=17639081; DOI=10.1101/gad.1562907;
RA Pezza R.J., Voloshin O.N., Vanevski F., Camerini-Otero R.D.;
RT "Hop2/Mnd1 acts on two critical steps in Dmc1-promoted homologous
RT pairing.";
RL Genes Dev. 21:1758-1766(2007).
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=17426123; DOI=10.1093/nar/gkm174;
RA Ploquin M., Petukhova G.V., Morneau D., Dery U., Bransi A., Stasiak A.,
RA Camerini-Otero R.D., Masson J.-Y.;
RT "Stimulation of fission yeast and mouse Hop2-Mnd1 of the Dmc1 and Rad51
RT recombinases.";
RL Nucleic Acids Res. 35:2719-2733(2007).
RN [7]
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Required for proper homologous chromosome pairing and
CC efficient cross-over and intragenic recombination during meiosis.
CC Stimulates both DMC1- and RAD51-mediated homologous strand
CC assimilation, which is required for the resolution of meiotic double-
CC strand breaks. {ECO:0000269|PubMed:15834424,
CC ECO:0000269|PubMed:16675459, ECO:0000269|PubMed:17426123,
CC ECO:0000269|PubMed:17639081}.
CC -!- SUBUNIT: Heterodimer with PSMC3IP/HOP2. MND1-PSMC3IP interacts with
CC DMC1 and RAD51 and binds to ssDNA and dsDNA showing no preference for
CC either form of DNA. {ECO:0000269|PubMed:15834424,
CC ECO:0000269|PubMed:16675459}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MND1 family. {ECO:0000305}.
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DR EMBL; AK011664; BAB27765.1; -; mRNA.
DR EMBL; BC027741; AAH27741.1; -; mRNA.
DR CCDS; CCDS38464.1; -.
DR RefSeq; NP_084073.2; NM_029797.3.
DR AlphaFoldDB; Q8K396; -.
DR SMR; Q8K396; -.
DR BioGRID; 218391; 2.
DR CORUM; Q8K396; -.
DR IntAct; Q8K396; 1.
DR MINT; Q8K396; -.
DR STRING; 10090.ENSMUSP00000048262; -.
DR iPTMnet; Q8K396; -.
DR PhosphoSitePlus; Q8K396; -.
DR EPD; Q8K396; -.
DR MaxQB; Q8K396; -.
DR PaxDb; Q8K396; -.
DR PeptideAtlas; Q8K396; -.
DR PRIDE; Q8K396; -.
DR ProteomicsDB; 295696; -.
DR Antibodypedia; 27871; 164 antibodies from 23 providers.
DR Ensembl; ENSMUST00000047368; ENSMUSP00000048262; ENSMUSG00000033752.
DR GeneID; 76915; -.
DR KEGG; mmu:76915; -.
DR UCSC; uc008ppv.2; mouse.
DR CTD; 84057; -.
DR MGI; MGI:1924165; Mnd1.
DR VEuPathDB; HostDB:ENSMUSG00000033752; -.
DR eggNOG; KOG3433; Eukaryota.
DR GeneTree; ENSGT00490000043413; -.
DR HOGENOM; CLU_080628_3_1_1; -.
DR InParanoid; Q8K396; -.
DR OMA; VCYWAFP; -.
DR OrthoDB; 880961at2759; -.
DR PhylomeDB; Q8K396; -.
DR TreeFam; TF314068; -.
DR BioGRID-ORCS; 76915; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Mnd1; mouse.
DR PRO; PR:Q8K396; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8K396; protein.
DR Bgee; ENSMUSG00000033752; Expressed in primary oocyte and 65 other tissues.
DR Genevisible; Q8K396; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; ISO:MGI.
DR GO; GO:0007131; P:reciprocal meiotic recombination; ISO:MGI.
DR InterPro; IPR040661; LZ3wCH.
DR InterPro; IPR005647; Mnd1.
DR InterPro; IPR040453; Mnd1_HTH.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF18517; LZ3wCH; 1.
DR Pfam; PF03962; Mnd1; 1.
DR PIRSF; PIRSF026991; Mnd1; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; DNA recombination; DNA-binding; Meiosis; Nucleus;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9BWT6"
FT CHAIN 2..205
FT /note="Meiotic nuclear division protein 1 homolog"
FT /id="PRO_0000318082"
FT COILED 83..173
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BWT6"
FT CONFLICT 128
FT /note="S -> F (in Ref. 1; BAB27765)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 205 AA; 23849 MW; 122C3FA9E4325120 CRC64;
MSKKRGLSGE EKRTRMMEIF FETKDVFQLK DLEKLAPKEK GITAMSVKEV LQSLVDDGMV
DCERIGTSNY YWAFPSKALH ARKRKLEALN SQLSEGSQKH ADLQKSIEKA RVGRQETEER
AMLAKELSSF RDQRQQLKAE VEKYRECDPQ VVEEIREANK VAKEAANRWT DNIFAIKSWA
KRKFGFEESK IDKNFGIPED FDYID
