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BRR6_SCHPO
ID   BRR6_SCHPO              Reviewed;         297 AA.
AC   Q9UT30;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Nucleus export protein brr6;
GN   Name=brr6; Synonyms=brl1; ORFNames=SPAC8F11.06;
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] {ECO:0000312|EMBL:CAB52167.1}
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   [2] {ECO:0000305}
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   [3]
RP   FUNCTION.
RX   PubMed=17993570; DOI=10.1128/ec.00321-07;
RA   Lo Presti L., Cockell M., Cerutti L., Simanis V., Hauser P.M.;
RT   "Functional characterization of Pneumocystis carinii brl1 by transspecies
RT   complementation analysis.";
RL   Eukaryot. Cell 6:2448-2452(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- FUNCTION: Involved in mRNA and protein export from nucleus.
CC       {ECO:0000250|UniProtKB:P38770, ECO:0000269|PubMed:17993570}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000250}; Multi-
CC       pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the BRL1/BRR6 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB52167.1; -; Genomic_DNA.
DR   PIR; T39181; T39181.
DR   RefSeq; NP_593955.1; NM_001019382.2.
DR   AlphaFoldDB; Q9UT30; -.
DR   BioGRID; 280011; 8.
DR   STRING; 4896.SPAC8F11.06.1; -.
DR   iPTMnet; Q9UT30; -.
DR   MaxQB; Q9UT30; -.
DR   PaxDb; Q9UT30; -.
DR   PRIDE; Q9UT30; -.
DR   EnsemblFungi; SPAC8F11.06.1; SPAC8F11.06.1:pep; SPAC8F11.06.
DR   GeneID; 2543596; -.
DR   KEGG; spo:SPAC8F11.06; -.
DR   PomBase; SPAC8F11.06; brr6.
DR   VEuPathDB; FungiDB:SPAC8F11.06; -.
DR   eggNOG; KOG4503; Eukaryota.
DR   HOGENOM; CLU_937376_0_0_1; -.
DR   InParanoid; Q9UT30; -.
DR   OMA; WVHVHRD; -.
DR   PhylomeDB; Q9UT30; -.
DR   PRO; PR:Q9UT30; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IC:PomBase.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR   GO; GO:0005635; C:nuclear envelope; IDA:PomBase.
DR   GO; GO:0031965; C:nuclear membrane; ISO:PomBase.
DR   GO; GO:1990578; C:perinuclear endoplasmic reticulum membrane; HDA:PomBase.
DR   GO; GO:0055088; P:lipid homeostasis; IEA:InterPro.
DR   GO; GO:0140480; P:mitotic spindle pole body insertion into the nuclear envelope; IMP:PomBase.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0006998; P:nuclear envelope organization; IMP:PomBase.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR040202; Brl1/Brr6.
DR   InterPro; IPR018767; Brl1/Brr6_dom.
DR   PANTHER; PTHR28136; PTHR28136; 1.
DR   Pfam; PF10104; Brr6_like_C_C; 1.
DR   SMART; SM01042; Brr6_like_C_C; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Membrane; mRNA transport; Nucleus; Phosphoprotein;
KW   Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..297
FT                   /note="Nucleus export protein brr6"
FT                   /id="PRO_0000317216"
FT   TRANSMEM        126..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        203..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        228..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..91
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         90
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   297 AA;  33574 MW;  631C314527ACB9D2 CRC64;
     MEMYVEDVPM PDIGPDSVLN TPIRPKYEIL KSKKKTQNEN DPEPMDISMS PDEKNLKKST
     VRRKLRKSKP NSSSNQVSSR TRALTKRSNS SNAIIKANNQ DSVYVSDWTN VHRDIPIVVS
     GYLQLMFNAC VASIFLYFLF KIVFGIQNDV RNRVEYHKIL QEEQAADCQR EYLSINCDSP
     GPAIFEVCQK LKQCKMESSN NVGSTKLAAL VFAEIIDAFI SHISYKTMVF SLILVFGSLL
     TSNYAFGLYR ARHSQNIHDY AANAIPAMIP SSRFLPSNLS DISNRNLIEA ASQEEEI
 
 
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