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   02-SEP-2026, entry version 191.
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=3; IntAct=EBI-21172, EBI-2197;
CC       P38352; Q12018: CDC53; NbExp=8; IntAct=EBI-21172, EBI-4321;
CC       P38352; Q08273: HRT1; NbExp=2; IntAct=EBI-21172, EBI-31686;
CC       P38352; P52286: SKP1; NbExp=5; 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; 39.
DR   ComplexPortal; CPX-3254; SCF-Saf1 ubiquitin ligase complex.
DR   DIP; DIP-6307N; -.
DR   FunCoup; P38352; 158.
DR   IntAct; P38352; 8.
DR   MINT; P38352; -.
DR   STRING; 4932.YBR280C; -.
DR   GlyGen; P38352; 7 sites, 1 O-linked glycan (7 sites).
DR   iPTMnet; P38352; -.
DR   PaxDb; 4932-YBR280C; -.
DR   PeptideAtlas; P38352; -.
DR   EnsemblFungi; YBR280C_mRNA; YBR280C; YBR280C.
DR   GeneID; 852583; -.
DR   KEGG; sce:YBR280C; -.
DR   AGR; SGD:S000000484; -.
DR   SGD; S000000484; SAF1.
DR   VEuPathDB; FungiDB:YBR280C; -.
DR   eggNOG; ENOG502QUVE; Eukaryota.
DR   HOGENOM; CLU_460835_0_0_1; -.
DR   InParanoid; P38352; -.
DR   OMA; MGDYHYL; -.
DR   OrthoDB; 61110at2759; -.
DR   BioCyc; YEAST:G3O-29200-MONOMER; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 852583; 0 hits in 10 CRISPR screens.
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:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
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   FunFam; 2.130.10.30:FF:000055; SCF-associated factor 1; 1.
DR   FunFam; 2.130.10.30:FF:000075; SCF-associated factor 1; 1.
DR   Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 3.
DR   InterPro; IPR036047; F-box-like_dom_sf.
DR   InterPro; IPR051553; Ran_GTPase-activating.
DR   InterPro; IPR009091; RCC1/BLIP-II.
DR   InterPro; IPR000408; Reg_chr_condens.
DR   PANTHER; PTHR45982; REGULATOR OF CHROMOSOME CONDENSATION; 1.
DR   PANTHER; PTHR45982:SF6; SCF-ASSOCIATED FACTOR 1; 1.
DR   Pfam; PF13540; RCC1_2; 1.
DR   SUPFAM; SSF81383; F-box domain; 1.
DR   SUPFAM; SSF50985; RCC1/BLIP-II; 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        244..260
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..305
FT                   /note="Low complexity"
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
//