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RDS3_YEAST
ID   RDS3_YEAST              Reviewed;         107 AA.
AC   Q06835; D6W493;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 170.
DE   RecName: Full=Pre-mRNA-splicing factor RDS3;
DE   AltName: Full=Regulator of drug sensitivity 3;
GN   Name=RDS3; OrderedLocusNames=YPR094W; ORFNames=P9513.2;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
RP   FUNCTION.
RX   PubMed=11943786; DOI=10.1074/jbc.m202566200;
RA   Akache B., Turcotte B.;
RT   "New regulators of drug sensitivity in the family of yeast zinc cluster
RT   proteins.";
RL   J. Biol. Chem. 277:21254-21260(2002).
RN   [5]
RP   FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=14517302; DOI=10.1128/mcb.23.20.7339-7349.2003;
RA   Wang Q., Rymond B.C.;
RT   "Rds3p is required for stable U2 snRNP recruitment to the splicing
RT   apparatus.";
RL   Mol. Cell. Biol. 23:7339-7349(2003).
CC   -!- FUNCTION: Required for pre-mRNA splicing. Involved in regulation of
CC       drug sensitivity and may play a role in multidrug resistance.
CC       {ECO:0000269|PubMed:11943786, ECO:0000269|PubMed:14517302}.
CC   -!- SUBUNIT: Component of the spliceosome where it interacts with CUS1,
CC       HSH49, HSH155, IST3 and RSE1. Also interacts with YRA1.
CC       {ECO:0000269|PubMed:14517302}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14517302}.
CC   -!- SIMILARITY: Belongs to the PHF5 family. {ECO:0000305}.
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DR   EMBL; U51033; AAB68140.1; -; Genomic_DNA.
DR   EMBL; AY693180; AAT93199.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11509.1; -; Genomic_DNA.
DR   PIR; S69077; S69077.
DR   RefSeq; NP_015419.1; NM_001184191.1.
DR   PDB; 2K0A; NMR; -; A=2-107.
DR   PDB; 5GM6; EM; 3.50 A; J=1-107.
DR   PDB; 5LQW; EM; 5.80 A; Y=1-107.
DR   PDB; 5NRL; EM; 7.20 A; S=1-107.
DR   PDB; 5ZWM; EM; 3.40 A; 5=1-107.
DR   PDB; 5ZWO; EM; 3.90 A; 5=1-107.
DR   PDB; 6G90; EM; 4.00 A; S=1-107.
DR   PDB; 7OQB; EM; 9.00 A; S=1-107.
DR   PDB; 7OQE; EM; 5.90 A; S=1-107.
DR   PDBsum; 2K0A; -.
DR   PDBsum; 5GM6; -.
DR   PDBsum; 5LQW; -.
DR   PDBsum; 5NRL; -.
DR   PDBsum; 5ZWM; -.
DR   PDBsum; 5ZWO; -.
DR   PDBsum; 6G90; -.
DR   PDBsum; 7OQB; -.
DR   PDBsum; 7OQE; -.
DR   AlphaFoldDB; Q06835; -.
DR   BMRB; Q06835; -.
DR   SMR; Q06835; -.
DR   BioGRID; 36262; 227.
DR   ComplexPortal; CPX-1647; SF3B complex.
DR   ComplexPortal; CPX-26; U2 small nuclear ribonucleoprotein complex.
DR   DIP; DIP-3822N; -.
DR   IntAct; Q06835; 10.
DR   STRING; 4932.YPR094W; -.
DR   MaxQB; Q06835; -.
DR   PaxDb; Q06835; -.
DR   PRIDE; Q06835; -.
DR   EnsemblFungi; YPR094W_mRNA; YPR094W; YPR094W.
DR   GeneID; 856209; -.
DR   KEGG; sce:YPR094W; -.
DR   SGD; S000006298; RDS3.
DR   VEuPathDB; FungiDB:YPR094W; -.
DR   eggNOG; KOG1705; Eukaryota.
DR   GeneTree; ENSGT00390000018518; -.
DR   HOGENOM; CLU_110369_1_1_1; -.
DR   InParanoid; Q06835; -.
DR   OMA; AYYCWEC; -.
DR   BioCyc; YEAST:G3O-34235-MON; -.
DR   EvolutionaryTrace; Q06835; -.
DR   PRO; PR:Q06835; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; Q06835; protein.
DR   GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR   GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
DR   GO; GO:0005681; C:spliceosomal complex; IC:ComplexPortal.
DR   GO; GO:0005686; C:U2 snRNP; IDA:SGD.
DR   GO; GO:0005684; C:U2-type spliceosomal complex; IPI:ComplexPortal.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:SGD.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IMP:SGD.
DR   GO; GO:0000245; P:spliceosomal complex assembly; IDA:SGD.
DR   GO; GO:1903241; P:U2-type prespliceosome assembly; IC:ComplexPortal.
DR   InterPro; IPR005345; PHF5.
DR   PANTHER; PTHR13120; PTHR13120; 1.
DR   Pfam; PF03660; PHF5; 1.
DR   PIRSF; PIRSF016468; PHF5; 1.
PE   1: Evidence at protein level;
KW   3D-structure; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW   Spliceosome.
FT   CHAIN           1..107
FT                   /note="Pre-mRNA-splicing factor RDS3"
FT                   /id="PRO_0000218722"
FT   STRAND          15..19
FT                   /evidence="ECO:0007829|PDB:2K0A"
FT   HELIX           24..26
FT                   /evidence="ECO:0007829|PDB:2K0A"
FT   TURN            31..33
FT                   /evidence="ECO:0007829|PDB:2K0A"
FT   STRAND          44..46
FT                   /evidence="ECO:0007829|PDB:2K0A"
FT   HELIX           47..50
FT                   /evidence="ECO:0007829|PDB:2K0A"
FT   TURN            59..61
FT                   /evidence="ECO:0007829|PDB:2K0A"
FT   STRAND          62..65
FT                   /evidence="ECO:0007829|PDB:2K0A"
FT   HELIX           74..79
FT                   /evidence="ECO:0007829|PDB:2K0A"
SQ   SEQUENCE   107 AA;  12260 MW;  F0E4737CA4FE8D24 CRC64;
     MSRHQFDLIM CLKQPGVQTG LLCEKCDGKC PICDSYVRPK RKVRVCENCS FGKQAKNCII
     CNLNVGVNDA FYCWECCRLG KDKDGCPRIL NLGSNRLDRH FEKKKKV
 
 
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