BRME1_MOUSE
ID BRME1_MOUSE Reviewed; 600 AA.
AC Q6DIA7; A0A0R4J144; E9QNR8; Q9D5J2;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-DEC-2020, sequence version 2.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Break repair meiotic recombinase recruitment factor 1 {ECO:0000305};
GN Name=Brme1 {ECO:0000312|MGI:MGI:1921916};
GN Synonyms=Meiok21 {ECO:0000303|PubMed:32463460};
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:BBO60545.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR
RP LOCATION, INTERACTION WITH HSF2BP AND BRCA2, DEVELOPMENTAL STAGE, AND
RP TISSUE SPECIFICITY.
RX PubMed=32460033; DOI=10.1016/j.celrep.2020.107686;
RA Takemoto K., Tani N., Takada-Horisawa Y., Fujimura S., Tanno N., Yamane M.,
RA Okamura K., Sugimoto M., Araki K., Ishiguro K.I.;
RT "Meiosis-Specific C19orf57/4930432K21Rik/BRME1 Modulates Localization of
RT RAD51 and DMC1 to DSBs in Mouse Meiotic Recombination.";
RL Cell Rep. 31:107686-107686(2020).
RN [2] {ECO:0000312|EMBL:BCB65306.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH HSF2BP; BRCA2;
RP SPATA22; MEIOB AND RAD51, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=32345962; DOI=10.1038/s41467-020-15954-x;
RA Zhang J., Gurusaran M., Fujiwara Y., Zhang K., Echbarthi M., Vorontsov E.,
RA Guo R., Pendlebury D.F., Alam I., Livera G., Emmanuelle M., Wang P.J.,
RA Nandakumar J., Davies O.R., Shibuya H.;
RT "The BRCA2-MEILB2-BRME1 complex governs meiotic recombination and impairs
RT the mitotic BRCA2-RAD51 function in cancer cells.";
RL Nat. Commun. 11:2055-2055(2020).
RN [3] {ECO:0000312|Ensembl:ENSMUSP00000113651, ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Ensembl:ENSMUSP00000113651,
RC ECO:0000312|Proteomes:UP000000589};
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-191; SER-192 AND
RP SER-195, AND 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).
RN [7]
RP FUNCTION, INTERACTION WITH HSF2BP; RAD51 AND PALB2, SUBCELLULAR LOCATION,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=32845237; DOI=10.7554/elife.56996;
RA Felipe-Medina N., Caburet S., Sanchez-Saez F., Condezo Y.B., de Rooij D.G.,
RA Gomez-H L., Garcia-Valiente R., Todeschini A.L., Duque P.,
RA Sanchez-Martin M.A., Shalev S.A., Llano E., Veitia R.A., Pendas A.M.;
RT "A missense in HSF2BP causing primary ovarian insufficiency affects meiotic
RT recombination by its novel interactor C19ORF57/BRME1.";
RL Elife 9:0-0(2020).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY,
RP INTERACTION WITH HSF2BP, AND SUBCELLULAR LOCATION.
RX PubMed=32463460; DOI=10.1093/nar/gkaa406;
RA Shang Y., Huang T., Liu H., Liu Y., Liang H., Yu X., Li M., Zhai B.,
RA Yang X., Wei Y., Wang G., Chen Z., Wang S., Zhang L.;
RT "MEIOK21: a new component of meiotic recombination bridges required for
RT spermatogenesis.";
RL Nucleic Acids Res. 48:6624-6639(2020).
CC -!- FUNCTION: Meiotic recombination factor component of recombination
CC bridges involved in meiotic double-strand break repair
CC (PubMed:32463460, PubMed:32460033). Modulates the localization of
CC recombinases DMC1:RAD51 to meiotic double-strand break (DSB) sites
CC through the interaction with and stabilization of the BRCA2:HSF2BP
CC complex during meiotic recombination (PubMed:32460033,
CC PubMed:32463460). Indispensable for the DSB repair, homologous
CC synapsis, and crossover formation that are needed for progression past
CC metaphase I, is essential for spermatogenesis and male fertility
CC (PubMed:32463460, PubMed:32460033). {ECO:0000269|PubMed:32460033,
CC ECO:0000269|PubMed:32463460, ECO:0000269|PubMed:32845237}.
CC -!- SUBUNIT: Interacts with HSF2BP (via N-terminus) and BRCA2; the
CC interaction with HSF2BP is direct and allows the formation of a ternary
CC complex (PubMed:32345962, PubMed:32460033, PubMed:32463460,
CC PubMed:32845237). The complex BRME1:HSF2BP:BRCA2 interacts with
CC SPATA22, MEIOB and RAD51 (PubMed:32345962).
CC {ECO:0000269|PubMed:32345962, ECO:0000269|PubMed:32460033,
CC ECO:0000269|PubMed:32463460, ECO:0000269|PubMed:32845237}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:32345962,
CC ECO:0000269|PubMed:32460033, ECO:0000269|PubMed:32463460,
CC ECO:0000269|PubMed:32845237}. Note=During meiosis, recruited to
CC chromosomes and localizes on recombination sites in a double-strand
CC break-dependent manner. First appears on the chromosome axis at
CC leptotene. Along with the progression of meiotic recombination,
CC released from the axis to form bridge-like structures linking homolog
CC axes before they are synapsed. Finally, located between synapsed
CC homolog axes and on the synaptonemal complex (SC).
CC {ECO:0000269|PubMed:32345962, ECO:0000269|PubMed:32460033,
CC ECO:0000269|PubMed:32463460, ECO:0000269|PubMed:32845237}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6DIA7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6DIA7-2; Sequence=VSP_027045;
CC -!- TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:32345962,
CC ECO:0000269|PubMed:32460033, ECO:0000269|PubMed:32463460}.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal ovaries but not in adult
CC ovaries. {ECO:0000269|PubMed:32460033, ECO:0000269|PubMed:32463460}.
CC -!- DISRUPTION PHENOTYPE: Male mutants are infertile (PubMed:32463460,
CC PubMed:32460033, PubMed:32345962). They have smaller-than-normal testes
CC with reduced diameters of seminiferous tubules and sperm density
CC (PubMed:32460033, PubMed:32345962). Female mutants exhibit normal
CC fertility with no apparent defect in adult ovaries (PubMed:32460033,
CC PubMed:32345962). They show a strong reduction of the follicle pool.
CC {ECO:0000269|PubMed:32345962, ECO:0000269|PubMed:32460033,
CC ECO:0000269|PubMed:32463460, ECO:0000269|PubMed:32845237}.
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DR EMBL; LC507101; BBO60545.1; -; mRNA.
DR EMBL; LC532163; BCB65306.1; -; mRNA.
DR EMBL; AC159266; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK015293; BAB29783.1; -; mRNA.
DR EMBL; BC075658; AAH75658.1; -; mRNA.
DR CCDS; CCDS52616.1; -. [Q6DIA7-1]
DR CCDS; CCDS52617.1; -. [Q6DIA7-2]
DR RefSeq; NP_001157224.1; NM_001163752.1. [Q6DIA7-2]
DR RefSeq; NP_083321.2; NM_029045.2. [Q6DIA7-1]
DR AlphaFoldDB; Q6DIA7; -.
DR STRING; 10090.ENSMUSP00000113651; -.
DR iPTMnet; Q6DIA7; -.
DR PhosphoSitePlus; Q6DIA7; -.
DR PaxDb; Q6DIA7; -.
DR PRIDE; Q6DIA7; -.
DR ProteomicsDB; 320780; -.
DR ProteomicsDB; 357185; -.
DR Antibodypedia; 50171; 43 antibodies from 14 providers.
DR DNASU; 74666; -.
DR Ensembl; ENSMUST00000093375; ENSMUSP00000091067; ENSMUSG00000008129. [Q6DIA7-2]
DR Ensembl; ENSMUST00000118856; ENSMUSP00000113651; ENSMUSG00000008129. [Q6DIA7-1]
DR GeneID; 74666; -.
DR KEGG; mmu:74666; -.
DR UCSC; uc009mmc.2; mouse.
DR CTD; 79173; -.
DR MGI; MGI:1921916; Brme1.
DR VEuPathDB; HostDB:ENSMUSG00000008129; -.
DR eggNOG; ENOG502SVQQ; Eukaryota.
DR GeneTree; ENSGT00390000016855; -.
DR HOGENOM; CLU_029361_0_0_1; -.
DR InParanoid; Q6DIA7; -.
DR OMA; HETQEPT; -.
DR OrthoDB; 573895at2759; -.
DR PhylomeDB; Q6DIA7; -.
DR TreeFam; TF337646; -.
DR BioGRID-ORCS; 74666; 4 hits in 71 CRISPR screens.
DR ChiTaRS; 4930432K21Rik; mouse.
DR PRO; PR:Q6DIA7; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q6DIA7; protein.
DR Bgee; ENSMUSG00000008129; Expressed in meninx and 101 other tissues.
DR ExpressionAtlas; Q6DIA7; baseline and differential.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:1990918; P:double-strand break repair involved in meiotic recombination; IDA:UniProtKB.
DR GO; GO:0007144; P:female meiosis I; IMP:UniProtKB.
DR GO; GO:0007141; P:male meiosis I; IDA:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR InterPro; IPR031441; Brme1.
DR PANTHER; PTHR14583; PTHR14583; 2.
DR Pfam; PF15710; Brme1; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosome; Meiosis; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..600
FT /note="Break repair meiotic recombinase recruitment factor
FT 1"
FT /id="PRO_0000295738"
FT REGION 1..150
FT /note="Required for nuclear location"
FT /evidence="ECO:0000269|PubMed:32463460"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..600
FT /note="Required for interaction with HSF2BP"
FT /evidence="ECO:0000269|PubMed:32845237"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 89..123
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027045"
FT CONFLICT 28
FT /note="Q -> H (in Ref. 5; AAH75658)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="V -> A (in Ref. 5; AAH75658)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 600 AA; 64440 MW; FAC1EB6464F0D402 CRC64;
MNKKKQRNSG VGLHPSKPSK NPRLRDSQSS MMVHSHYSRE SEDSSEPAPS VELGGEEPLH
EAFSCPVEDT GAASDLAGSP KELVPLPPSQ NSVGKFVPQF AKPRKTVTRK AKAWEEDLEG
CTTSQETRPE LGALKAASQP QRESLRFPPH DIRPEVQTQP DGTLSKERTI SLDNRSLGNN
GFEMATVQDS SSPLSDAAAE GREADSRDPQ ERDAQGGEAG AQHSGEPQEG EDILYTSALA
PASEPTWSVA QDLSVPTYTL SSTAAAPSST SPADASLMDT VITEVSLDPS VLQQSAPQVA
KLLGSLDEQI PDGGCIGTLL SSTPLAEETT AGREEARWEE RCHGDTLASF TETEPEKQEP
VTEAGDSGHI AQEMDPVVKT KDSGSDEQSP GDIGMLPLPA QSMNQMLVEL RGLTCDQDLE
GLSTPHTSSQ LEHTCAASDP PQSTKDCHSS PGIPVHLAAP CPRDQAAWQE SSAMELDFLP
DSQIQDALDA TNMEQGFPSG SMPDLGWPVP SSQSIGGSPK AVTKPQSRSH VETWAQETYR
MQDATDTVRG LVVELSGLNR LIMSTHRDLE AFKRRKTKSL PYLTKGLGSL PRGDQSWRDL
