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MLO3_SCHPO
ID   MLO3_SCHPO              Reviewed;         199 AA.
AC   Q09330;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=mRNA export protein mlo3;
DE   AltName: Full=RNA-annealing protein mlo3;
GN   Name=mlo3; ORFNames=SPBC1D7.04;
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].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=8972853; DOI=10.1093/nar/24.23.4676;
RA   Javerzat J.-P., Cranston G., Allshire R.C.;
RT   "Fission yeast genes which disrupt mitotic chromosome segregation when
RT   overexpressed.";
RL   Nucleic Acids Res. 24:4676-4683(1996).
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   FUNCTION, INTERACTION WITH RPN15, MEX67 AND UAP56, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=15990877; DOI=10.1038/sj.emboj.7600713;
RA   Thakurta A.G., Gopal G., Yoon J.H., Kozak L., Dhar R.;
RT   "Homolog of BRCA2-interacting Dss1p and Uap56p link Mlo3p and Rae1p for
RT   mRNA export in fission yeast.";
RL   EMBO J. 24:2512-2523(2005).
RN   [4]
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).
CC   -!- FUNCTION: Has a role in the mRNA export process. Interferes with
CC       mitotic chromosome segregation when overexpressed.
CC       {ECO:0000269|PubMed:15990877}.
CC   -!- SUBUNIT: Interacts with rpn15/dss1, mex67 and uap56.
CC       {ECO:0000269|PubMed:15990877}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15990877,
CC       ECO:0000269|PubMed:16823372}.
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DR   EMBL; L42551; AAB41270.1; -; mRNA.
DR   EMBL; CU329671; CAB10980.1; -; Genomic_DNA.
DR   PIR; T39861; T39861.
DR   RefSeq; NP_595715.1; NM_001021613.2.
DR   AlphaFoldDB; Q09330; -.
DR   SMR; Q09330; -.
DR   BioGRID; 277092; 80.
DR   STRING; 4896.SPBC1D7.04.1; -.
DR   iPTMnet; Q09330; -.
DR   MaxQB; Q09330; -.
DR   PaxDb; Q09330; -.
DR   PRIDE; Q09330; -.
DR   EnsemblFungi; SPBC1D7.04.1; SPBC1D7.04.1:pep; SPBC1D7.04.
DR   GeneID; 2540565; -.
DR   KEGG; spo:SPBC1D7.04; -.
DR   PomBase; SPBC1D7.04; mlo3.
DR   VEuPathDB; FungiDB:SPBC1D7.04; -.
DR   eggNOG; KOG0533; Eukaryota.
DR   HOGENOM; CLU_052367_2_2_1; -.
DR   InParanoid; Q09330; -.
DR   OMA; GIARVWF; -.
DR   PhylomeDB; Q09330; -.
DR   PRO; PR:Q09330; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0000346; C:transcription export complex; ISO:PomBase.
DR   GO; GO:0062153; F:C5-methylcytidine-containing RNA binding; ISO:PomBase.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0006406; P:mRNA export from nucleus; IBA:GO_Central.
DR   GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:PomBase.
DR   CDD; cd12267; RRM_YRA1_MLO3; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR025715; FoP_C.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR034357; Yra1/Mlo3_RRM.
DR   Pfam; PF13865; FoP_duplication; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM01218; FoP_duplication; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   mRNA transport; Nucleus; Reference proteome; RNA-binding; Transport.
FT   CHAIN           1..199
FT                   /note="mRNA export protein mlo3"
FT                   /id="PRO_0000081634"
FT   DOMAIN          55..134
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          144..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..32
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..162
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..199
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   199 AA;  21791 MW;  E8544B8DC39A8EF6 CRC64;
     MSMELDQSLD AIIASKPKGG IRKRRARSNK PKPTKNAKPA VNTASALKSV ISEESKIIVS
     NLPTDVTEAQ VKELFVKSIG PCKRVSLAYG PNGRSKGIAT IIFSRPGDAT RAYEQYEGRL
     VDGTRKMKVE IILDPSRQLN SLAARVSPAS NASATASKNG AKSSKRKTTR RRRTPNRPKK
     SAEELDKEMD DYFGSNEKE
 
 
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