STS1_YEAST
ID STS1_YEAST Reviewed; 319 AA.
AC P38637; D6VVU1; P35188;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Tethering factor for nuclear proteasome STS1;
DE AltName: Full=Dumbbell former protein 8;
DE AltName: Full=SEC23 suppressor 1;
GN Name=STS1; Synonyms=DBF8, SSM5; OrderedLocusNames=YIR011C; ORFNames=YIB11C;
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 [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8065366; DOI=10.1128/mcb.14.9.6350-6360.1994;
RA Houman F., Holm C.;
RT "DBF8, an essential gene required for efficient chromosome segregation in
RT Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 14:6350-6360(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=7925484;
RA Liang S., Lacroute F., Kepes F.;
RT "Multicopy STS1 restores both protein transport and ribosomal RNA stability
RT in a new yeast sec23 mutant allele.";
RL Eur. J. Cell Biol. 62:270-281(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7762303; DOI=10.1002/yea.320110109;
RA Voss H., Tamames J., Teodoru C., Valencia A., Sensen C., Wiemann S.,
RA Schwager C., Zimmermann J., Sander C., Ansorge W.;
RT "Nucleotide sequence and analysis of the centromeric region of yeast
RT chromosome IX.";
RL Yeast 11:61-78(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [5]
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 [6]
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 [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8914516; DOI=10.1007/bf02172401;
RA Amrani N., Dufour M.E., Bonneaud N., Lacroute F.;
RT "Mutations in STS1 suppress the defect in 3' mRNA processing caused by the
RT rna15-2 mutation in Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 252:552-562(1996).
RN [8]
RP FUNCTION, AND INTERACTION WITH SRP1.
RX PubMed=10913188; DOI=10.1128/mcb.20.16.6062-6073.2000;
RA Tabb M.M., Tongaonkar P., Vu L., Nomura M.;
RT "Evidence for separable functions of Srp1p, the yeast homolog of importin
RT alpha (Karyopherin alpha): role for Srp1p and Sts1p in protein
RT degradation.";
RL Mol. Cell. Biol. 20:6062-6073(2000).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP FUNCTION, AND PROTEASOME-BINDING.
RX PubMed=17916559; DOI=10.1074/jbc.m704857200;
RA Romero-Perez L., Chen L., Lambertson D., Madura K.;
RT "Sts1 can overcome the loss of Rad23 and Rpn10 and represents a novel
RT regulator of the ubiquitin/proteasome pathway.";
RL J. Biol. Chem. 282:35574-35582(2007).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RPN11 AND SRP1.
RX PubMed=21075847; DOI=10.1074/jbc.m110.135863;
RA Chen L., Romero L., Chuang S.M., Tournier V., Joshi K.K., Lee J.A.,
RA Kovvali G., Madura K.;
RT "Sts1 plays a key role in targeting proteasomes to the nucleus.";
RL J. Biol. Chem. 286:3104-3118(2011).
CC -!- FUNCTION: Involved in ubiquitin-mediated protein degradation.
CC Regulatory factor in the ubiquitin/proteasome pathway that controls the
CC turnover of proteasome substrates. Targets proteasomes to the nucleus
CC and facilitates the degradation of nuclear proteins. Required for
CC efficient chromosome segregation. Restores protein transport and
CC ribosomal RNA stability. {ECO:0000269|PubMed:10913188,
CC ECO:0000269|PubMed:17916559, ECO:0000269|PubMed:21075847,
CC ECO:0000269|PubMed:7925484, ECO:0000269|PubMed:8065366,
CC ECO:0000269|PubMed:8914516}.
CC -!- SUBUNIT: Binds the proteasome. Interacts with karyopherin SRP1 and
CC proteasome subunit RPN11. {ECO:0000269|PubMed:10913188,
CC ECO:0000269|PubMed:21075847}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- MISCELLANEOUS: Present with 2120 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cut8/STS1 family. {ECO:0000305}.
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DR EMBL; Z37996; CAA86081.1; -; Genomic_DNA.
DR EMBL; U12437; AAA21413.1; -; Genomic_DNA.
DR EMBL; X79743; CAB38099.1; -; Genomic_DNA.
DR EMBL; X75916; CAA53515.1; -; Genomic_DNA.
DR EMBL; AY557878; AAS56204.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08557.1; -; Genomic_DNA.
DR PIR; S48355; S48355.
DR RefSeq; NP_012276.1; NM_001179533.1.
DR AlphaFoldDB; P38637; -.
DR SMR; P38637; -.
DR BioGRID; 35003; 398.
DR DIP; DIP-7670N; -.
DR IntAct; P38637; 1.
DR STRING; 4932.YIR011C; -.
DR PaxDb; P38637; -.
DR PRIDE; P38637; -.
DR EnsemblFungi; YIR011C_mRNA; YIR011C; YIR011C.
DR GeneID; 854828; -.
DR KEGG; sce:YIR011C; -.
DR SGD; S000001450; STS1.
DR VEuPathDB; FungiDB:YIR011C; -.
DR eggNOG; ENOG502RNK4; Eukaryota.
DR HOGENOM; CLU_054606_1_0_1; -.
DR InParanoid; P38637; -.
DR OMA; SSLGWMH; -.
DR BioCyc; YEAST:G3O-31432-MON; -.
DR PRO; PR:P38637; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P38637; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0007059; P:chromosome segregation; IMP:SGD.
DR GO; GO:0071630; P:nuclear protein quality control by the ubiquitin-proteasome system; IMP:SGD.
DR GO; GO:0031144; P:proteasome localization; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.58.1590; -; 1.
DR InterPro; IPR013868; Cut8/Sts1_fam.
DR InterPro; IPR038422; Cut8/Sts1_sf.
DR PANTHER; PTHR28032; PTHR28032; 1.
DR Pfam; PF08559; Cut8; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Protein transport; Reference proteome; Transport.
FT CHAIN 1..319
FT /note="Tethering factor for nuclear proteasome STS1"
FT /id="PRO_0000079792"
FT REGION 33..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 231
FT /note="V -> I (in Ref. 2; CAA53515)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 319 AA; 36485 MW; 4C5608D50B6AD829 CRC64;
MMGFEWGFKP SSKITQSTVS SQGTGNVMIP TAGVKQKRRY ANEEQEEEEL PRNKNVMKYG
GVSKRRPQPG SLIRGQPLPL QRGMELMNKN QLQQLLVDLM TKHPEIQQSV HTRVIGLDFS
IQKCLDMLKQ KSEAVYQSIP YNRSYESNKL DDYAFVRMKP QILEFLNCLV DFILDNIPPR
LENLHASLKF LDICTELVIK LPRFELASNN YYYDKCIEQL SHVWCTLIEH VARDRIILLA
DNSSVWKSHM TRLQVYNEHS NGLLERPLQL FKSLDMGSPS AASSSTLSLQ ESIIYHHDTM
TANENNNNSG SAATDSPFN
