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MEIOB_MOUSE
ID   MEIOB_MOUSE             Reviewed;         470 AA.
AC   Q9D513; E9QLG1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Meiosis-specific with OB domain-containing protein {ECO:0000305};
DE            EC=3.1.-.-;
DE   AltName: Full=Protein expressed in male leptotene and zygotene spermatocytes 675;
DE            Short=MLZ-675;
GN   Name=Meiob {ECO:0000312|MGI:MGI:1922428};
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 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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 227-470.
RC   TISSUE=Testis;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 241-470.
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   [4]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=20339383; DOI=10.1038/jhg.2010.26;
RA   Kogo H., Kowa-Sugiyama H., Yamada K., Bolor H., Tsutsumi M., Ohye T.,
RA   Inagaki H., Taniguchi M., Toda T., Kurahashi H.;
RT   "Screening of genes involved in chromosome segregation during meiosis I:
RT   toward the identification of genes responsible for infertility in humans.";
RL   J. Hum. Genet. 55:293-299(2010).
RN   [5]
RP   FUNCTION, DNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, MUTAGENESIS OF ARG-235 AND
RP   SER-251, AND INTERACTION WITH RPA2 AND SPATA22.
RX   PubMed=24240703; DOI=10.1038/ncomms3788;
RA   Luo M., Yang F., Leu N.A., Landaiche J., Handel M.A., Benavente R.,
RA   La Salle S., Wang P.J.;
RT   "MEIOB exhibits single-stranded DNA-binding and exonuclease activities and
RT   is essential for meiotic recombination.";
RL   Nat. Commun. 4:2788-2788(2013).
RN   [6]
RP   FUNCTION, DNA-BINDING, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION
RP   PHENOTYPE, AND SUBCELLULAR LOCATION.
RX   PubMed=24068956; DOI=10.1371/journal.pgen.1003784;
RA   Souquet B., Abby E., Herve R., Finsterbusch F., Tourpin S., Le Bouffant R.,
RA   Duquenne C., Messiaen S., Martini E., Bernardino-Sgherri J., Toth A.,
RA   Habert R., Livera G.;
RT   "MEIOB targets single-strand DNA and is necessary for meiotic
RT   recombination.";
RL   PLoS Genet. 9:E1003784-E1003784(2013).
RN   [7]
RP   INTERACTION WITH BRME1.
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).
CC   -!- FUNCTION: Single-stranded DNA-binding protein required for homologous
CC       recombination in meiosis I. Required for double strand breaks (DSBs)
CC       repair and crossover formation and promotion of faithful and complete
CC       synapsis. Not required for the initial loading of recombinases but
CC       required to maintain a proper number of RAD51 and DMC1 foci after the
CC       zygotene stage. May act by ensuring the stabilization of recombinases,
CC       which is required for successful homology search and meiotic
CC       recombination. Displays Single-stranded DNA 3'-5' exonuclease activity
CC       in vitro. {ECO:0000269|PubMed:20339383, ECO:0000269|PubMed:24068956,
CC       ECO:0000269|PubMed:24240703}.
CC   -!- SUBUNIT: Component of a multiprotein complex with RPA2 and SPATA22.
CC       Interacts with the complex BRME1:HSF2BP:BRCA2 (PubMed:32345962).
CC       {ECO:0000269|PubMed:32345962}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20339383}. Nucleus
CC       {ECO:0000269|PubMed:24068956, ECO:0000269|PubMed:24240703}. Chromosome
CC       {ECO:0000269|PubMed:24068956, ECO:0000269|PubMed:24240703}. Note=Co-
CC       localizes with the RPA complex on meiotic chromosome axes. Accumulates
CC       on resected DNA. Localization is dependent on SPATA22.
CC       {ECO:0000269|PubMed:24068956, ECO:0000269|PubMed:24240703}.
CC   -!- TISSUE SPECIFICITY: Sprecifically expressed in early meiotic germ
CC       cells: in adult and fetal tissues, detected in fetal ovary, postnatal
CC       testis and liver. In the ovary, expression starts at 12.5 dpc, reaches
CC       a maximum at 15.5 dpc and decreases to become undetectable in post
CC       natal life. In testis, expression starts at 10 days post partum (dpp),
CC       reaches a maximum at 20 dpp and is maintained throughout adult life.
CC       {ECO:0000269|PubMed:24068956, ECO:0000269|PubMed:24240703}.
CC   -!- DEVELOPMENTAL STAGE: Detected only during early meiosis prophase I
CC       (early 4N-fraction containing leptotene, zygotene and few pachytenes
CC       spermatocytes) and not during later stages of meiosis (at protein
CC       level). {ECO:0000269|PubMed:24068956, ECO:0000269|PubMed:24240703}.
CC   -!- DISRUPTION PHENOTYPE: Mice develop and grow normally but show
CC       infertility in both sexes. Infertility is due to a meiotic arrest at a
CC       zygotene/pachytene-like stage. DNA double strand break repair and
CC       homologous chromosome synapsis are impaired in meiocytes.
CC       {ECO:0000269|PubMed:24068956, ECO:0000269|PubMed:24240703}.
CC   -!- SIMILARITY: Belongs to the MEIOB family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI19086.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAI19088.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB30034.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC166102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC119085; AAI19086.1; ALT_INIT; mRNA.
DR   EMBL; BC119087; AAI19088.1; ALT_INIT; mRNA.
DR   EMBL; AK015924; BAB30034.1; ALT_INIT; mRNA.
DR   CCDS; CCDS50020.1; -.
DR   RefSeq; NP_083473.1; NM_029197.1.
DR   RefSeq; XP_006525108.1; XM_006525045.3.
DR   RefSeq; XP_006525110.1; XM_006525047.3.
DR   RefSeq; XP_006525111.1; XM_006525048.3.
DR   AlphaFoldDB; Q9D513; -.
DR   SMR; Q9D513; -.
DR   CORUM; Q9D513; -.
DR   STRING; 10090.ENSMUSP00000024972; -.
DR   iPTMnet; Q9D513; -.
DR   PhosphoSitePlus; Q9D513; -.
DR   jPOST; Q9D513; -.
DR   PaxDb; Q9D513; -.
DR   PRIDE; Q9D513; -.
DR   ProteomicsDB; 292218; -.
DR   Antibodypedia; 42506; 40 antibodies from 13 providers.
DR   Ensembl; ENSMUST00000024972; ENSMUSP00000024972; ENSMUSG00000024155.
DR   GeneID; 75178; -.
DR   KEGG; mmu:75178; -.
DR   UCSC; uc008ayk.1; mouse.
DR   CTD; 254528; -.
DR   MGI; MGI:1922428; Meiob.
DR   VEuPathDB; HostDB:ENSMUSG00000024155; -.
DR   eggNOG; KOG0851; Eukaryota.
DR   GeneTree; ENSGT00390000001723; -.
DR   HOGENOM; CLU_042457_2_0_1; -.
DR   InParanoid; Q9D513; -.
DR   OMA; SCTLIYE; -.
DR   OrthoDB; 615895at2759; -.
DR   PhylomeDB; Q9D513; -.
DR   TreeFam; TF323670; -.
DR   BioGRID-ORCS; 75178; 4 hits in 107 CRISPR screens.
DR   PRO; PR:Q9D513; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q9D513; protein.
DR   Bgee; ENSMUSG00000024155; Expressed in spermatocyte and 27 other tissues.
DR   ExpressionAtlas; Q9D513; baseline and differential.
DR   Genevisible; Q9D513; MM.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR   GO; GO:0008310; F:single-stranded DNA 3'-5' exodeoxyribonuclease activity; IDA:UniProtKB.
DR   GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
DR   GO; GO:0007144; P:female meiosis I; IMP:UniProtKB.
DR   GO; GO:0009566; P:fertilization; IMP:UniProtKB.
DR   GO; GO:0007129; P:homologous chromosome pairing at meiosis; IMP:UniProtKB.
DR   GO; GO:0007141; P:male meiosis I; IMP:UniProtKB.
DR   GO; GO:0007140; P:male meiotic nuclear division; IEP:UniProtKB.
DR   GO; GO:0000712; P:resolution of meiotic recombination intermediates; IMP:UniProtKB.
DR   Gene3D; 2.40.50.140; -; 3.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   SUPFAM; SSF50249; SSF50249; 3.
PE   1: Evidence at protein level;
KW   Chromosome; Cytoplasm; DNA-binding; Exonuclease; Hydrolase; Meiosis;
KW   Nuclease; Nucleus; Reference proteome.
FT   CHAIN           1..470
FT                   /note="Meiosis-specific with OB domain-containing protein"
FT                   /id="PRO_0000337136"
FT   DNA_BIND        167..272
FT                   /note="OB"
FT   MUTAGEN         235
FT                   /note="R->A: Impaired DNA-binding and exonuclease
FT                   activities."
FT                   /evidence="ECO:0000269|PubMed:24240703"
FT   MUTAGEN         251
FT                   /note="S->A: Impaired exonuclease activity without
FT                   affecting much the DNA-binding activity."
FT                   /evidence="ECO:0000269|PubMed:24240703"
SQ   SEQUENCE   470 AA;  52975 MW;  DC24D41B07E6C9E9 CRC64;
     MAKFFALKNF TALSDLHPNM ANLKIIGIVI GKTDVKGFPD RKNIGSERYT FSFTIRDSPC
     HFVNVSSWGS EDYIRSLSES FRVAECVIIE NPLIQRKDTE REEKFSPATP SNYKLLLSEN
     HSMVKVCSPY EVDTKLLSLI HLPVKESRDY YSLADIVANG HSLDGRIINV LAAVRSVGEP
     KYFTTSDRRK GQRCEVKLFD ETEPSFTMTC WDNESILLAQ SWMARETVIF ASDVRINFNK
     FQNCMAATVI SKTIITVNPD TPEANILLNY IRENKETNVA DEIDSYLKES VNLNTIVDVY
     TVEQLKVKAL KSEGKADPFY GILYAYISTL NIDDETTKVV RNRCSSCGYI VNEASNTCTI
     CNQDSSRLKS FFLSFDVLVD LTDHTGTLHS CSLSGSIAEE TLGCTINEFL TMTSEQKTKL
     KWQLLLERSK IYLKLILSHR ARGGLKVTIL SCKLADPTEA SRNLARQGHT
 
 
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