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SPO11_SCHPO
ID   SPO11_SCHPO             Reviewed;         345 AA.
AC   P40384;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Meiotic recombination protein rec12 {ECO:0000303|PubMed:8005432};
DE   AltName: Full=SPO11 protein homolog {ECO:0000303|PubMed:12437782};
GN   Name=rec12 {ECO:0000303|PubMed:8005432};
GN   ORFNames=SPAC17A5.11 {ECO:0000312|PomBase:SPAC17A5.11};
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF TYR-98.
RX   PubMed=12437782; DOI=10.1186/1475-9268-1-1;
RA   Sharif W.D., Glick G.G., Davidson M.K., Wahls W.P.;
RT   "Distinct functions of S. pombe Rec12 (Spo11) protein and Rec12-dependent
RT   crossover recombination (chiasmata) in meiosis I; and a requirement for
RT   Rec12 in meiosis II.";
RL   Cell Chromosome 1:1-1(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 207-335, AND DEVELOPMENTAL STAGE.
RX   PubMed=8005432; DOI=10.1093/genetics/136.3.769;
RA   Lin Y., Smith G.R.;
RT   "Transient, meiosis-induced expression of the rec6 and rec12 genes of
RT   Schizosaccharomyces pombe.";
RL   Genetics 136:769-779(1994).
RN   [4]
RP   FUNCTION.
RX   PubMed=10882124; DOI=10.1016/s1097-2765(00)80328-7;
RA   Cervantes M.D., Farah J.A., Smith G.R.;
RT   "Meiotic DNA breaks associated with recombination in S. pombe.";
RL   Mol. Cell 5:883-888(2000).
RN   [5]
RP   FUNCTION IN MEIOSIS.
RX   PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA   Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA   Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA   Smith G.R., Moreno S.;
RT   "A large-scale screen in S. pombe identifies seven novel genes required for
RT   critical meiotic events.";
RL   Curr. Biol. 15:2056-2062(2005).
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [7]
RP   IDENTIFICATION IN DSBC COMPLEX.
RX   PubMed=22841486; DOI=10.1016/j.molcel.2012.06.023;
RA   Miyoshi T., Ito M., Kugou K., Yamada S., Furuichi M., Oda A., Yamada T.,
RA   Hirota K., Masai H., Ohta K.;
RT   "A central coupler for recombination initiation linking chromosome
RT   architecture to S phase checkpoint.";
RL   Mol. Cell 47:722-733(2012).
CC   -!- FUNCTION: Required for formation of the double-strand breaks (DSBs)
CC       that initiate meiotic recombination (PubMed:10882124). Required for
CC       crossover recombination and chiasmatic segregation of chromosomes
CC       during meiosis I. Also involved in the faithful equational segregation
CC       of chromosomes during meiosis II (PubMed:12437782, PubMed:16303567).
CC       {ECO:0000269|PubMed:10882124, ECO:0000269|PubMed:12437782,
CC       ECO:0000269|PubMed:16303567}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q57815};
CC   -!- SUBUNIT: Component of the DSB catalytic core (DSBC) complex, composed
CC       of at least rec12, rec6 and rec14. The complex interacts with mde2.
CC       {ECO:0000269|PubMed:22841486}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- DEVELOPMENTAL STAGE: Most abundant at 2 hours after induction of
CC       meiosis, at the time of premeiotic DNA synthesis. Found at much lower
CC       levels before and after this time. {ECO:0000269|PubMed:8005432}.
CC   -!- SIMILARITY: Belongs to the TOP6A family. {ECO:0000305}.
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DR   EMBL; AF195027; AAF06017.1; -; mRNA.
DR   EMBL; CU329670; CAB11511.1; -; Genomic_DNA.
DR   EMBL; L14774; AAA35332.1; -; Genomic_DNA.
DR   PIR; T37826; T37826.
DR   RefSeq; NP_593479.1; NM_001018912.1.
DR   AlphaFoldDB; P40384; -.
DR   SMR; P40384; -.
DR   BioGRID; 278626; 56.
DR   STRING; 4896.SPAC17A5.11.1; -.
DR   PaxDb; P40384; -.
DR   EnsemblFungi; SPAC17A5.11.1; SPAC17A5.11.1:pep; SPAC17A5.11.
DR   GeneID; 2542150; -.
DR   KEGG; spo:SPAC17A5.11; -.
DR   PomBase; SPAC17A5.11; rec12.
DR   VEuPathDB; FungiDB:SPAC17A5.11; -.
DR   eggNOG; KOG2795; Eukaryota.
DR   HOGENOM; CLU_037229_0_1_1; -.
DR   InParanoid; P40384; -.
DR   OMA; NWGEARF; -.
DR   PhylomeDB; P40384; -.
DR   PRO; PR:P40384; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000228; C:nuclear chromosome; ISO:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0045027; F:DNA end binding; IDA:PomBase.
DR   GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0031619; P:homologous chromosome orientation involved in meiotic metaphase I plate congression; IMP:PomBase.
DR   GO; GO:0042138; P:meiotic DNA double-strand break formation; IMP:PomBase.
DR   GO; GO:0000706; P:meiotic DNA double-strand break processing; IBA:GO_Central.
DR   GO; GO:0007131; P:reciprocal meiotic recombination; IMP:PomBase.
DR   CDD; cd00223; TOPRIM_TopoIIB_SPO; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR002815; Spo11/TopoVI_A.
DR   InterPro; IPR013049; Spo11/TopoVI_A_N.
DR   InterPro; IPR036078; Spo11/TopoVI_A_sf.
DR   InterPro; IPR034136; TOPRIM_Topo6A/Spo11.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR10848; PTHR10848; 1.
DR   Pfam; PF04406; TP6A_N; 1.
DR   PRINTS; PR01550; TOP6AFAMILY.
DR   SUPFAM; SSF56726; SSF56726; 1.
PE   1: Evidence at protein level;
KW   Chromosome partition; Cytoplasm; Magnesium; Meiosis; Metal-binding;
KW   Nucleus; Reference proteome.
FT   CHAIN           1..345
FT                   /note="Meiotic recombination protein rec12"
FT                   /id="PRO_0000145477"
FT   ACT_SITE        98
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000305|PubMed:12437782"
FT   BINDING         179
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q57815"
FT   BINDING         229
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q57815"
FT   MUTAGEN         98
FT                   /note="Y->F: Errors in meiosis II segregation."
FT                   /evidence="ECO:0000269|PubMed:12437782"
SQ   SEQUENCE   345 AA;  39399 MW;  056257FAAE7A2781 CRC64;
     MNSNDKKKVV RSWIEQFVHD FVEQLSKPTK DSVNVALKRR KHNSWNGSLD SKANERQKVK
     VFSFPRNETT IAQLFRVLDC VHEAVISDTV ITKRDIYYRD VDLFKRQTVV DELLGDISNT
     IGCSRSDLNV EASAKGLVFG SIHIALENGT VITATKPLLI SHHRISSITS TAKWVLVIEK
     EAVFQTLTEE ALADTIIVTA KGFPDLMTRK FLVKLAKALP DAKFFGIFDW DPHGLCIYSC
     FKYGSNAYSH EPHSQLRNLQ LLGPLYEDIF NKNQEFSLKL NKRDIKMITT LLQFEGFQKE
     PVVREQLQRM LFIQKKAEIQ AILEFPSWIK GKLADADKSG KHSVR
 
 
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