DAS1_YEAST
ID DAS1_YEAST Reviewed; 663 AA.
AC P47005; D6VW36;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=F-box protein DAS1;
DE AltName: Full=DST1-delta 6-azauracil sensitivity protein 1;
GN Name=DAS1; OrderedLocusNames=YJL149W; ORFNames=J0634;
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].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8813765;
RX DOI=10.1002/(sici)1097-0061(19960630)12:8<787::aid-yea954>3.0.co;2-4;
RA Katsoulou C., Tzermia M., Tavernarakis N., Alexandraki D.;
RT "Sequence analysis of a 40.7 kb segment from the left arm of yeast
RT chromosome X reveals 14 known genes and 13 new open reading frames
RT including homologues of genes clustered on the right arm of chromosome
RT XI.";
RL Yeast 12:787-797(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [3]
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 [4]
RP IDENTIFICATION IN SCF COMPLEX.
RX PubMed=10385629; DOI=10.1101/gad.13.12.1614;
RA Seol J.H., Feldman R.M.R., Zachariae W., Shevchenko A., Correll C.C.,
RA Lyapina S., Chi Y., Galova M., Claypool J., Sandmeyer S., Nasmyth K.,
RA Shevchenko A., Deshaies R.J.;
RT "Cdc53/cullin and the essential Hrt1 RING-H2 subunit of SCF define a
RT ubiquitin ligase module that activates the E2 enzyme Cdc34.";
RL Genes Dev. 13:1614-1626(1999).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN SCF COMPLEX.
RX PubMed=10582239; DOI=10.1098/rstb.1999.0497;
RA Willems A.R., Goh T., Taylor L., Chernushevich I., Shevchenko A., Tyers M.;
RT "SCF ubiquitin protein ligases and phosphorylation-dependent proteolysis.";
RL Philos. Trans. R. Soc. Lond., B, Biol. Sci. 354:1533-1550(1999).
RN [6]
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 [7]
RP INTERACTION WITH SKP1, AND RECONSTITUTION OF THE SCF(DAS1) COMPLEX.
RX PubMed=14747994; DOI=10.1002/prot.10620;
RA Kus B.M., Caldon C.E., Andorn-Broza R., Edwards A.M.;
RT "Functional interaction of 13 yeast SCF complexes with a set of yeast E2
RT enzymes in vitro.";
RL Proteins 54:455-467(2004).
RN [8]
RP IDENTIFICATION IN THE SCF(DAS1) COMPLEX.
RX PubMed=19882662; DOI=10.1002/pmic.200900497;
RA Kato M., Kito K., Ota K., Ito T.;
RT "Remodeling of the SCF complex-mediated ubiquitination system by
RT compositional alteration of incorporated F-box proteins.";
RL Proteomics 10:115-123(2010).
CC -!- FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box
CC protein) E3 ubiquitin-protein ligase complex which mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins. Probably recognizes and binds to phosphorylated target
CC proteins (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with SKP1. Component of the probable SCF(DAS1)
CC complex containing CDC53, SKP1, RBX1 and DAS1.
CC {ECO:0000269|PubMed:10385629, ECO:0000269|PubMed:10582239,
CC ECO:0000269|PubMed:14747994, ECO:0000269|PubMed:19882662}.
CC -!- INTERACTION:
CC P47005; P52286: SKP1; NbExp=4; IntAct=EBI-26114, EBI-4090;
CC -!- MISCELLANEOUS: Present with 195 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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; Z49425; CAA89445.1; -; Genomic_DNA.
DR EMBL; X87371; CAA60806.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08652.1; -; Genomic_DNA.
DR PIR; S55164; S55164.
DR RefSeq; NP_012386.1; NM_001181582.1.
DR AlphaFoldDB; P47005; -.
DR BioGRID; 33609; 82.
DR ComplexPortal; CPX-3244; SCF-Das1 ubiquitin ligase complex.
DR DIP; DIP-6404N; -.
DR IntAct; P47005; 5.
DR MINT; P47005; -.
DR STRING; 4932.YJL149W; -.
DR iPTMnet; P47005; -.
DR MaxQB; P47005; -.
DR PaxDb; P47005; -.
DR PRIDE; P47005; -.
DR TopDownProteomics; P47005; -.
DR EnsemblFungi; YJL149W_mRNA; YJL149W; YJL149W.
DR GeneID; 853292; -.
DR KEGG; sce:YJL149W; -.
DR SGD; S000003685; DAS1.
DR VEuPathDB; FungiDB:YJL149W; -.
DR eggNOG; ENOG502QRGQ; Eukaryota.
DR HOGENOM; CLU_020929_0_0_1; -.
DR InParanoid; P47005; -.
DR OMA; PSCNDII; -.
DR BioCyc; YEAST:G3O-31593-MON; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:P47005; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47005; protein.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:SGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISA:SGD.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0000409; P:regulation of transcription by galactose; IC:ComplexPortal.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; ISA:SGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:ComplexPortal.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR Pfam; PF12937; F-box-like; 1.
DR SMART; SM00256; FBOX; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..663
FT /note="F-box protein DAS1"
FT /id="PRO_0000119971"
FT DOMAIN 46..91
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
SQ SEQUENCE 663 AA; 77367 MW; C48B6CAB40920027 CRC64;
MPFQDYFQKK KAAFINRNNK SNADASALRD INDININFAA KSKNYVFPLT KLPDELMQEV
FSHLPQPDRL QLCLVNKRLN KIATKLLYRR IYLNDSNVVK SDFMHLAINW TLLNLPSSLK
EEESRDIANC KLKKLIETLQ NNIHITEVIQ WIRINWDLDS TLQRSILSIL CNQGKSLQRL
ENVTDPACND IISNGHFSRS NVSSFDMAPP NSLPEMVVPE NYIPNLTKYL SQRISSRLSH
MTLFIDPLKL FNYLYPLDIK LQIIDLKLHW RREFYNNDYF VKKIRPGNPL TKLSEVFDKR
TLKILTIISW NDTLLKRETE MLKDFKEFEN LEDLSLISIK QDVHILVDLF SSLTNLKRLK
MDFLEEYVPE PTNPHIFLSI LLACSKLQFI DLRYDGLIPQ IINIQENKFQ LNQQCNCTNC
QIVFSDILKG KIFMFPEDYY IHDLQDIAAK DIFKMMKYLS LLPYSKACDA YPSVRTQPMN
LTNFVTKMNR NLLEYRNSKS QLVPKIVNNP HQHSTVTSTS TAHMSEPEMI IIDDDDDDDE
INAAIPPSSD DTAATISTDL ELPHESLTKR DIIMCYHALI HHFKSIYVTF LKSFPHLRFL
MLNDIPTIVM EENNERIFEP VFYHYDYKSN LYGWSKESNK NLENDSNNNN NNSDTIARIA
TVM