位置:首页 > 蛋白库 > MEI2_SCHPO
MEI2_SCHPO
ID   MEI2_SCHPO              Reviewed;         750 AA.
AC   P08965;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=Meiosis protein mei2;
GN   Name=mei2; ORFNames=SPAC27D7.03c;
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].
RX   PubMed=2840284; DOI=10.1002/j.1460-2075.1988.tb02873.x;
RA   Watanabe Y., Iino Y., Furuhata K., Shimoda C., Yamamoto M.;
RT   "The S.pombe mei2 gene encoding a crucial molecule for commitment to
RT   meiosis is under the regulation of cAMP.";
RL   EMBO J. 7:761-767(1988).
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   INTERACTION WITH RAD24.
RX   PubMed=11818066; DOI=10.1016/s0960-9822(01)00654-6;
RA   Sato M., Watanabe Y., Akiyoshi Y., Yamamoto M.;
RT   "14-3-3 protein interferes with the binding of RNA to the phosphorylated
RT   form of fission yeast meiotic regulator Mei2p.";
RL   Curr. Biol. 12:141-145(2002).
CC   -!- FUNCTION: Crucial for commitment to meiosis but it is not sufficient
CC       itself for the commitment. May be a splicing regulator.
CC   -!- SUBUNIT: Binds rad24 when phosphorylated.
CC   -!- INDUCTION: By nitrogen starvation.
CC   -!- PTM: Inactivated by phosphorylation by ran1/pat1.
CC   -!- MISCELLANEOUS: The expression of mei2 protein is negatively controlled
CC       by cAMP.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X07180; CAA30165.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAA15822.1; -; Genomic_DNA.
DR   PIR; S00391; COZPME.
DR   RefSeq; NP_594609.1; NM_001020037.2.
DR   PDB; 6YYL; X-ray; 1.89 A; A/C=579-750.
DR   PDB; 6YYM; X-ray; 2.63 A; A=579-750.
DR   PDB; 7DUS; X-ray; 2.50 A; A=560-712.
DR   PDB; 7EIO; X-ray; 1.90 A; A/B=580-733.
DR   PDB; 7EIU; X-ray; 2.35 A; A/B=580-733.
DR   PDBsum; 6YYL; -.
DR   PDBsum; 6YYM; -.
DR   PDBsum; 7DUS; -.
DR   PDBsum; 7EIO; -.
DR   PDBsum; 7EIU; -.
DR   AlphaFoldDB; P08965; -.
DR   SMR; P08965; -.
DR   BioGRID; 278557; 41.
DR   IntAct; P08965; 1.
DR   STRING; 4896.SPAC27D7.03c.1; -.
DR   iPTMnet; P08965; -.
DR   MaxQB; P08965; -.
DR   PaxDb; P08965; -.
DR   PRIDE; P08965; -.
DR   EnsemblFungi; SPAC27D7.03c.1; SPAC27D7.03c.1:pep; SPAC27D7.03c.
DR   GeneID; 2542080; -.
DR   KEGG; spo:SPAC27D7.03c; -.
DR   PomBase; SPAC27D7.03c; mei2.
DR   VEuPathDB; FungiDB:SPAC27D7.03c; -.
DR   eggNOG; KOG4660; Eukaryota.
DR   HOGENOM; CLU_370943_0_0_1; -.
DR   InParanoid; P08965; -.
DR   OMA; ICDISYA; -.
DR   PhylomeDB; P08965; -.
DR   PRO; PR:P08965; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0033620; C:Mei2 nuclear dot complex; IDA:PomBase.
DR   GO; GO:0000228; C:nuclear chromosome; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR   GO; GO:0034064; C:Tor2-Mei2-Ste11 complex; IDA:PomBase.
DR   GO; GO:0140311; F:protein sequestering activity; EXP:PomBase.
DR   GO; GO:0003723; F:RNA binding; IPI:PomBase.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0140538; P:negative regulation of conjugation with zygote; IMP:PomBase.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IMP:PomBase.
DR   GO; GO:0051446; P:positive regulation of meiotic cell cycle; IMP:PomBase.
DR   GO; GO:1905191; P:positive regulation of metaphase/anaphase transition of meiosis II; IMP:PomBase.
DR   GO; GO:0110046; P:signal transduction involved in cell cycle switching, mitotic to meiotic cell cycle; IMP:PomBase.
DR   CDD; cd12528; RRM2_MEI2_fungi; 1.
DR   CDD; cd12532; RRM3_MEI2_fungi; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR034863; Fungal_Mei2-like_RRM2.
DR   InterPro; IPR034862; Fungal_Mei2-like_RRM3.
DR   InterPro; IPR007201; Mei2-like_Rrm_C.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   Pfam; PF00076; RRM_1; 1.
DR   Pfam; PF04059; RRM_2; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; SSF54928; 2.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Meiosis; Phosphoprotein; Reference proteome; Repeat;
KW   RNA-binding; Stress response.
FT   CHAIN           1..750
FT                   /note="Meiosis protein mei2"
FT                   /id="PRO_0000081626"
FT   DOMAIN          195..270
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          293..361
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           586..590
FT                   /evidence="ECO:0007829|PDB:6YYL"
FT   STRAND          598..602
FT                   /evidence="ECO:0007829|PDB:6YYL"
FT   HELIX           610..621
FT                   /evidence="ECO:0007829|PDB:6YYL"
FT   STRAND          624..633
FT                   /evidence="ECO:0007829|PDB:6YYL"
FT   TURN            634..637
FT                   /evidence="ECO:0007829|PDB:6YYL"
FT   STRAND          638..649
FT                   /evidence="ECO:0007829|PDB:6YYL"
FT   HELIX           651..660
FT                   /evidence="ECO:0007829|PDB:6YYL"
FT   STRAND          663..666
FT                   /evidence="ECO:0007829|PDB:7DUS"
FT   TURN            667..669
FT                   /evidence="ECO:0007829|PDB:7DUS"
FT   STRAND          670..673
FT                   /evidence="ECO:0007829|PDB:7DUS"
FT   STRAND          675..678
FT                   /evidence="ECO:0007829|PDB:6YYL"
FT   HELIX           684..691
FT                   /evidence="ECO:0007829|PDB:6YYL"
FT   HELIX           695..698
FT                   /evidence="ECO:0007829|PDB:6YYL"
FT   HELIX           701..703
FT                   /evidence="ECO:0007829|PDB:6YYL"
FT   STRAND          706..708
FT                   /evidence="ECO:0007829|PDB:6YYL"
FT   TURN            713..716
FT                   /evidence="ECO:0007829|PDB:6YYL"
SQ   SEQUENCE   750 AA;  82677 MW;  A13D9E75F48D09DC CRC64;
     MIMETESPLS ITSPSPSDST FQVDMEKTMH ALPSSLLDSP LLSTNEHYPP KSTLLLSGPS
     PIRNIQLSAT KSSESNSIDY LTDTQNIFPN FVNNENNYQF STAPLNPIDA CRVGERKVFT
     TGNVLLSADR QPLSTWQQNI SVLSESPPQN GIQSYISSSE QAAQALTRKP SVTGFRSSSL
     NSNSDDIDIF SHASRYLFVT NLPRIVPYAT LLELFSKLGD VKGIDTSSLS TDGICIVAFF
     DIRQAIQAAK SLRSQRFFND RLLYFQFCQR SSIQKMINQG ATIQFLDDNE GQLLLNMQGG
     SVLSILQLQS ILQTFGPLLI MKPLRSQNVS QIICEFYDTR DASFALDELD GRIIHNCCLQ
     VAYYDAMADS VSTSSASSLS VPRGFSGMLN NNSEWNNSMT MSSNQETPTA ASCAVSRIGS
     SYGMSNNFGS VPLGRTESSP AWGTSGYYDV SSTSPVAPSD RNPSRQYNSI RYGLDVNPIA
     PPNSSRLKQR NSDLLNGINP QWSPFSSNTG KVFDSPTGSL GMRRSLTVGA NASCSNPTNL
     SFASLTLHDS KADSTLSASS LNPDLNLQRY TPTVEKHASD RNSVDYAQIA SGIDTRTTVM
     IKNIPNKFTQ QMLRDYIDVT NKGTYDFLYL RIDFVNKCNV GYAFINFIEP QSIITFGKAR
     VGTQWNVFHS EKICDISYAN IQGKDRLIEK FRNSCVMDEN PAYRPKIFVS HGPNRGMEEP
     FPAPNNARRK LRSIASAQQI GLFPPTASKC
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024