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REC10_SCHPO
ID   REC10_SCHPO             Reviewed;         791 AA.
AC   Q09823;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=Linear element protein rec10 {ECO:0000305};
DE   AltName: Full=Meiotic recombination protein rec10;
GN   Name=rec10 {ECO:0000312|PomBase:SPAC25G10.04c};
GN   ORFNames=SPAC25G10.04c {ECO:0000312|PomBase:SPAC25G10.04c};
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 [GENOMIC DNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=7586030; DOI=10.1007/bf00311213;
RA   Lin Y., Smith G.R.;
RT   "Molecular cloning of the meiosis-induced rec10 gene of Schizosaccharomyces
RT   pombe.";
RL   Curr. Genet. 27:440-446(1995).
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   IDENTIFICATION IN THE LINEAR ELEMENT COMPLEX, SUBCELLULAR LOCATION, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=23395004; DOI=10.1016/j.molcel.2013.01.008;
RA   Fowler K.R., Gutierrez-Velasco S., Martin-Castellanos C., Smith G.R.;
RT   "Protein determinants of meiotic DNA break hot spots.";
RL   Mol. Cell 49:983-996(2013).
RN   [4]
RP   MUTAGENESIS OF 176-VAL--GLY-178; 184-ARG-ASP-185; GLU-271; ARG-434 AND
RP   GLY-727.
RX   PubMed=28469148; DOI=10.1038/s41598-017-00742-3;
RA   Ma L., Fowler K.R., Martin-Castellanos C., Smith G.R.;
RT   "Functional organization of protein determinants of meiotic DNA break
RT   hotspots.";
RL   Sci. Rep. 7:1393-1393(2017).
RN   [5]
RP   FUNCTION, INTERACTION WITH HOP1; REC15 AND REC25, SUBCELLULAR LOCATION,
RP   DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-309 AND 348-PRO-LYS-349.
RX   PubMed=31665745; DOI=10.1093/nar/gkz754;
RA   Kariyazono R., Oda A., Yamada T., Ohta K.;
RT   "Conserved HORMA domain-containing protein Hop1 stabilizes interaction
RT   between proteins of meiotic DNA break hotspots and chromosome axis.";
RL   Nucleic Acids Res. 47:10166-10180(2019).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=33825974; DOI=10.1007/s00412-021-00757-w;
RA   Ding D.Q., Matsuda A., Okamasa K., Hiraoka Y.;
RT   "Linear elements are stable structures along the chromosome axis in fission
RT   yeast meiosis.";
RL   Chromosoma 130:s00412.021.00757-s00412.021.00757(2021).
CC   -!- FUNCTION: Organizes linear element components on chromosomes and is
CC       thus required for meiotic DNA recombination.
CC       {ECO:0000269|PubMed:31665745, ECO:0000269|PubMed:33825974,
CC       ECO:0000269|PubMed:7586030}.
CC   -!- SUBUNIT: Component of linear elements (LinEs), which are similar to
CC       synaptonemal complexes, at least composed of rec27, rec25, rec10 and
CC       mug20 (PubMed:23395004). Interacts with rec25; the interaction is
CC       direct (PubMed:31665745). Interacts with hop1 (via N-terminus); the
CC       interaction is direct (PubMed:31665745). Interacts with rec15 (via C-
CC       terminus); the interaction is direct (PubMed:31665745).
CC       {ECO:0000269|PubMed:23395004, ECO:0000269|PubMed:31665745}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23395004,
CC       ECO:0000269|PubMed:31665745, ECO:0000269|PubMed:33825974}. Chromosome
CC       {ECO:0000269|PubMed:31665745}. Note=Localizes to DNA double-strand
CC       break (DSB) hotspots. {ECO:0000269|PubMed:31665745}.
CC   -!- DEVELOPMENTAL STAGE: Present from pre-meiotic DNA replication and
CC       disappears following meiotic prophase I. {ECO:0000269|PubMed:33825974,
CC       ECO:0000269|PubMed:7586030}.
CC   -!- DISRUPTION PHENOTYPE: Abnormal linear element formation
CC       (PubMed:33825974, PubMed:23395004). Abolishes localization of hop1 to
CC       meiotic chromosomal axis sites and DNA double-strand break (DSB)
CC       hotspots (PubMed:31665745). Severely decreases localization of rec15 to
CC       chromosomal axis sites (PubMed:31665745). Abnormal sporulation
CC       (PubMed:33825974). {ECO:0000269|PubMed:23395004,
CC       ECO:0000269|PubMed:31665745, ECO:0000269|PubMed:33825974}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA99538.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U09871; AAA99538.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CU329670; CAA94633.1; -; Genomic_DNA.
DR   PIR; S55725; S55725.
DR   PIR; T52489; T52489.
DR   RefSeq; NP_594524.1; NM_001019953.2.
DR   AlphaFoldDB; Q09823; -.
DR   BioGRID; 278184; 18.
DR   STRING; 4896.SPAC25G10.04c.1; -.
DR   PaxDb; Q09823; -.
DR   PRIDE; Q09823; -.
DR   EnsemblFungi; SPAC25G10.04c.1; SPAC25G10.04c.1:pep; SPAC25G10.04c.
DR   GeneID; 2541688; -.
DR   KEGG; spo:SPAC25G10.04c; -.
DR   PomBase; SPAC25G10.04c; rec10.
DR   VEuPathDB; FungiDB:SPAC25G10.04c; -.
DR   HOGENOM; CLU_354176_0_0_1; -.
DR   OMA; HRDFACR; -.
DR   PRO; PR:Q09823; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0000785; C:chromatin; IDA:PomBase.
DR   GO; GO:0030998; C:linear element; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0042138; P:meiotic DNA double-strand break formation; IMP:PomBase.
DR   GO; GO:0007131; P:reciprocal meiotic recombination; IMP:PomBase.
DR   InterPro; IPR012491; Red1/Rec10.
DR   Pfam; PF07964; Red1; 1.
PE   1: Evidence at protein level;
KW   Chromosome; Meiosis; Nucleus; Reference proteome.
FT   CHAIN           1..791
FT                   /note="Linear element protein rec10"
FT                   /id="PRO_0000097220"
FT   REGION          462..523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          644..672
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           485..492
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT   COMPBIAS        462..481
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        502..516
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         176..178
FT                   /note="VIG->IID: Decreases meiotic gene conversion at ade6
FT                   and leads to abnormal localization of rec25 within the
FT                   nucleus."
FT                   /evidence="ECO:0000269|PubMed:28469148"
FT   MUTAGEN         184..185
FT                   /note="RD->FT: Decreases meiotic gene conversion at ade6,
FT                   crossing-over between ade6 and arg1, and leads to abnormal
FT                   localization of rec25 to the nucleus."
FT                   /evidence="ECO:0000269|PubMed:28469148"
FT   MUTAGEN         271
FT                   /note="E->K: Decreases meiotic gene conversion at ade6;
FT                   when associated with H-434."
FT                   /evidence="ECO:0000269|PubMed:28469148"
FT   MUTAGEN         309
FT                   /note="E->A: Decreases interaction with rec15. Decreases
FT                   meiotic gene conversion at ade6. Decreases spore
FT                   viability."
FT                   /evidence="ECO:0000269|PubMed:31665745"
FT   MUTAGEN         348..349
FT                   /note="PK->GG: Decreases interaction with hop1. Decreases
FT                   meiotic gene conversion at ade6."
FT                   /evidence="ECO:0000269|PubMed:31665745"
FT   MUTAGEN         434
FT                   /note="R->H: Decreases meiotic gene conversion at ade6;
FT                   when associated with K-271."
FT                   /evidence="ECO:0000269|PubMed:28469148"
FT   MUTAGEN         727
FT                   /note="G->E: Abnormal localization of rec25 within the
FT                   nucleus."
FT                   /evidence="ECO:0000269|PubMed:28469148"
FT   CONFLICT        202
FT                   /note="S -> F (in Ref. 1; AAA99538)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        257
FT                   /note="S -> A (in Ref. 1; AAA99538)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   791 AA;  89876 MW;  682DFA66B5FFA7B9 CRC64;
     MDIFSEFLNC LSSDGTLNES SIYKTYQILE SLNPKDVDTK ENYIKLSNTF STLGSGVGFQ
     DNLLIEMFKI LTVLFFKTRS TDLGDLLIES FTSLEIEKLM RVKKTIGSIV LTKGIQELQE
     IELPKVGFNC MTYDESIFQG ISLERLILQL MSIFIAKCEE NKLWLVNNRK DLDLRVIGQR
     LLHRDFACRF LSGLFISRFS VSGDTDESKH QNGIRLQLFI DFSKFETRLT MQILKADRIF
     STCVANTVHA YEGLFSSGSN IDSTIATLVL EPRDLIVYRK GFALLQIPWT SVTTIDKIKK
     VKSLKIITEV SSLDEFVFQC KDGDKFDELF STSEEIMNKL LPAIIVSPKL TLRNRSIIQI
     KEGESKLPNT SKQASQNLPH LDDELAYQRF EDQVIDKSVC DDECTNTENT PSSNIPADVK
     DSLSADDYAY DTKRKTQIED LEEDQNKSKI ASKDGTNLKE INSVPEFSDE NVINQTGPAK
     KTPVQRRKDG KFAKSTKRKK QKSLKPDTEN QESSVKNKKA KSNVNLQYSP KTPICKINDE
     TLKPPTIANI AGHKQMNHLT SENIETPVPV PNGNWYNGVK HETATDIFTT CHDGNNSLKS
     SVWKELLKEK HWKQESKPQL TGNSRQIDLS TFVKQANTPN ITSLLDGTCS SPPNNECFND
     KEPDSSSSTL ISDRQELEYR NPNAETVKLE EIPYNKFFKT VEKNEAYNPS SKSATIDGLQ
     RYTSMIGNQI YEGILQNEKE LRSKLEAYHI NCNKVIKEFS KRQTARYKII EKELAQIEVN
     LVSQIDSLMF K
 
 
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