SAF1_YEAST
ID SAF1_YEAST Reviewed; 637 AA.
AC P38352; D6VQS5;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=SCF-associated factor 1;
GN Name=SAF1; OrderedLocusNames=YBR280C; ORFNames=YBR2017;
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 204508 / S288c;
RX PubMed=8091861; DOI=10.1002/yea.320100007;
RA Holmstroem K., Brandt T., Kallesoe T.;
RT "The sequence of a 32,420 bp segment located on the right arm of chromosome
RT II from Saccharomyces cerevisiae.";
RL Yeast 10:S47-S62(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
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 INTERACTION WITH CDC53 AND SKP1, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP DOMAIN F-BOX.
RX PubMed=11283612; DOI=10.1038/35070067;
RA Seol J.H., Shevchenko A., Shevchenko A., Deshaies R.J.;
RT "Skp1 forms multiple protein complexes, including RAVE, a regulator of V-
RT ATPase assembly.";
RL Nat. Cell Biol. 3:384-391(2001).
RN [5]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [6]
RP FUNCTION.
RX PubMed=16677311; DOI=10.1111/j.1365-2958.2006.05153.x;
RA Escusa S., Camblong J., Galan J.M., Pinson B., Daignan-Fornier B.;
RT "Proteasome- and SCF-dependent degradation of yeast adenine deaminase upon
RT transition from proliferation to quiescence requires a new F-box protein
RT named Saf1p.";
RL Mol. Microbiol. 60:1014-1025(2006).
RN [7]
RP FUNCTION, INTERACTION WITH SKP1 AND AAH1, AND MUTAGENESIS OF LEU-24;
RP LEU-35; ARG-263; ARG-264; GLY-372; SER-387 AND LEU-580.
RX PubMed=17517885; DOI=10.1074/jbc.m702425200;
RA Escusa S., Laporte D., Massoni A., Boucherie H., Dautant A.,
RA Daignan-Fornier B.;
RT "Skp1-Cullin-F-box-dependent degradation of Aah1p requires its interaction
RT with the F-box protein Saf1p.";
RL J. Biol. Chem. 282:20097-20103(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-266, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [11]
RP IDENTIFICATION IN THE SCF(SAF1) 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. Targets AAH1 adenine deaminase for proteasome-dependent
CC degradation upon entry into quiescence. Targets also URA7.
CC {ECO:0000269|PubMed:16677311, ECO:0000269|PubMed:17517885}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with AAH1, SKP1 and CDC53. Component of the
CC SCF(SAF1) complex containing CDC53, SKP1, HRT1 and SAF1.
CC {ECO:0000269|PubMed:11283612, ECO:0000269|PubMed:17517885,
CC ECO:0000269|PubMed:19882662}.
CC -!- INTERACTION:
CC P38352; P53909: AAH1; NbExp=2; IntAct=EBI-21172, EBI-2197;
CC P38352; Q12018: CDC53; NbExp=7; IntAct=EBI-21172, EBI-4321;
CC P38352; Q08273: HRT1; NbExp=2; IntAct=EBI-21172, EBI-31686;
CC P38352; P52286: SKP1; NbExp=4; IntAct=EBI-21172, EBI-4090;
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA53643.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA85244.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X76053; CAA53643.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z36149; CAA85244.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006936; DAA07395.1; -; Genomic_DNA.
DR PIR; S44542; S44542.
DR RefSeq; NP_009839.4; NM_001178628.3.
DR AlphaFoldDB; P38352; -.
DR SMR; P38352; -.
DR BioGRID; 32974; 33.
DR ComplexPortal; CPX-3254; SCF-Saf1 ubiquitin ligase complex.
DR DIP; DIP-6307N; -.
DR IntAct; P38352; 7.
DR MINT; P38352; -.
DR STRING; 4932.YBR280C; -.
DR iPTMnet; P38352; -.
DR MaxQB; P38352; -.
DR PaxDb; P38352; -.
DR PRIDE; P38352; -.
DR EnsemblFungi; YBR280C_mRNA; YBR280C; YBR280C.
DR GeneID; 852583; -.
DR KEGG; sce:YBR280C; -.
DR SGD; S000000484; SAF1.
DR VEuPathDB; FungiDB:YBR280C; -.
DR eggNOG; ENOG502QUVE; Eukaryota.
DR HOGENOM; CLU_460835_0_0_1; -.
DR InParanoid; P38352; -.
DR OMA; GWDFNCV; -.
DR BioCyc; YEAST:G3O-29200-MON; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:P38352; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38352; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:SGD.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IMP:SGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:ComplexPortal.
DR Gene3D; 2.130.10.30; -; 3.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR SUPFAM; SSF50985; SSF50985; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS00626; RCC1_2; 1.
DR PROSITE; PS50012; RCC1_3; 2.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation pathway.
FT CHAIN 1..637
FT /note="SCF-associated factor 1"
FT /id="PRO_0000206658"
FT DOMAIN 14..63
FT /note="F-box"
FT REPEAT 109..202
FT /note="RCC1 1"
FT REPEAT 565..635
FT /note="RCC1 2"
FT REGION 242..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 24
FT /note="L->P: In saf1-5; impairs the interaction with SKP1."
FT /evidence="ECO:0000269|PubMed:17517885"
FT MUTAGEN 35
FT /note="L->P: In saf1-6; impairs the interaction with SKP1."
FT /evidence="ECO:0000269|PubMed:17517885"
FT MUTAGEN 263
FT /note="R->K: In saf1-4; impairs the protein stability; when
FT associated with K-264."
FT /evidence="ECO:0000269|PubMed:17517885"
FT MUTAGEN 264
FT /note="R->K: In saf1-4; impairs the protein stability; when
FT associated with K-263."
FT /evidence="ECO:0000269|PubMed:17517885"
FT MUTAGEN 372
FT /note="G->V: In saf1-1; impairs the protein stability."
FT /evidence="ECO:0000269|PubMed:17517885"
FT MUTAGEN 387
FT /note="S->F: In saf1-2; impairs the protein stability."
FT /evidence="ECO:0000269|PubMed:17517885"
FT MUTAGEN 580
FT /note="L->S: In saf1-3; impairs the protein stability."
FT /evidence="ECO:0000269|PubMed:17517885"
SQ SEQUENCE 637 AA; 70495 MW; 358D751C612744BE CRC64;
MSEVESREKE PDAGLSPDIV QATLPFLSSD DIKNLSQTNK YYNTLLDFDH SKILWHELFH
KAFGTLKTND EPFQGRNSAE FKTCTETILR EAFPTLSWQE VYQLRAYDAK FYSWGYLKHG
RLGYTASSNN ELVATSLNGP SPRFKYGVNT PTEVPWFNSR TTSRTSNFTP SEDPLSAIKK
DGDEIIAQVS SGGFSFQILT ESGNLYSSGS TFSGGLKGPG PSGSQHDYNP FREMIHNMER
SYPRITSRSN GSTVNTTGTF SGRRMSGSHP STAYEPGNAT TAQHITIDSG GAPAASPGGS
HSGVPRTTMP SMGPHENIYS QIEMLERSAN KAVPGNNHIR RMFARNSFPL YSGRDENLGS
FNDIQFVAVS SGRSHFLAMD TDNNIYSWDS TESDQGVKIE FANLPSRATN PILKIASGWN
FNCCYIYKVG LVAWKERDAI QKGESFAFAK YEIVPNTNDV NGDSRIVDFA CLQDNCVFFI
NNNGDKLWKY HNGLNQIVDL NIVGKLCKIN ACFASLVLFT DTHCYTLKVT NGDVDKDSLT
ELDINENVIS VASGDYHTVA LTERGHLYSW GIESQDCGCL GLGPSEKIVN ELHIGNWEGQ
RNIRVVKPTK IELPEDYICV SVTAGGWQTG ALIIKKH
