SFI1_YEAST
ID SFI1_YEAST Reviewed; 946 AA.
AC Q12369; D6VY00;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Protein SFI1;
DE AltName: Full=Suppressor of fermentation induced loss of stress resistance protein 1;
GN Name=SFI1; OrderedLocusNames=YLL003W; ORFNames=L1373;
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 90840 / EAY235 / FY23;
RX PubMed=8810043;
RX DOI=10.1002/(sici)1097-0061(19960615)12:7<693::aid-yea956>3.0.co;2-g;
RA Miosga T., Zimmermann F.K.;
RT "Sequence analysis of the CEN12 region of Saccharomyces cerevisiae on a
RT 43.7 kb fragment of chromosome XII including an open reading frame
RT homologous to the human cystic fibrosis transmembrane conductance regulator
RT protein CFTR.";
RL Yeast 12:693-708(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=10455233;
RX DOI=10.1002/(sici)1097-0061(199908)15:11<1097::aid-yea437>3.0.co;2-b;
RA Ma P., Winderickx J., Nauwelaers D., Dumortier F., De Doncker A.,
RA Thevelein J.M., Van Dijck P.;
RT "Deletion of SFI1, a novel suppressor of partial Ras-cAMP pathway
RT deficiency in the yeast Saccharomyces cerevisiae, causes G(2) arrest.";
RL Yeast 15:1097-1109(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [4]
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CDC31 AND SPC110.
RX PubMed=14504268; DOI=10.1083/jcb.200307064;
RA Kilmartin J.V.;
RT "Sfi1p has conserved centrin-binding sites and an essential function in
RT budding yeast spindle pole body duplication.";
RL J. Cell Biol. 162:1211-1221(2003).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-855, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, 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 [10]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 218-306 AND 643-710 IN COMPLEX
RP WITH CDC31, AND FUNCTION.
RX PubMed=16785321; DOI=10.1083/jcb.200603153;
RA Li S., Sandercock A.M., Conduit P., Robinson C.V., Williams R.L.,
RA Kilmartin J.V.;
RT "Structural role of Sfi1p-centrin filaments in budding yeast spindle pole
RT body duplication.";
RL J. Cell Biol. 173:867-877(2006).
CC -!- FUNCTION: Component of the spindle pole body (SPB) half-bridge involved
CC in the initial steps of SPB duplication. {ECO:0000269|PubMed:10455233,
CC ECO:0000269|PubMed:14504268, ECO:0000269|PubMed:16785321}.
CC -!- SUBUNIT: Forms a complex with CDC31 and interacts with SPC110.
CC Associates with the spindle pole body half bridge.
CC {ECO:0000269|PubMed:14504268, ECO:0000269|PubMed:16785321}.
CC -!- INTERACTION:
CC Q12369; P06704: CDC31; NbExp=2; IntAct=EBI-2213082, EBI-4259;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:14504268, ECO:0000269|PubMed:14562095}.
CC Note=Spindle pole, half bridge. {ECO:0000269|PubMed:14504268}.
CC -!- SIMILARITY: Belongs to the SFI1 family. {ECO:0000305}.
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DR EMBL; X91488; CAA62767.1; -; Genomic_DNA.
DR EMBL; X95569; CAA64815.1; -; Genomic_DNA.
DR EMBL; Z73108; CAA97446.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09316.1; -; Genomic_DNA.
DR PIR; S64745; S64745.
DR RefSeq; NP_013098.1; NM_001181823.1.
DR PDB; 2DOQ; X-ray; 3.00 A; D=218-306.
DR PDB; 2GV5; X-ray; 3.00 A; C/F=643-710.
DR PDBsum; 2DOQ; -.
DR PDBsum; 2GV5; -.
DR AlphaFoldDB; Q12369; -.
DR SMR; Q12369; -.
DR BioGRID; 31248; 98.
DR DIP; DIP-8950N; -.
DR IntAct; Q12369; 8.
DR MINT; Q12369; -.
DR STRING; 4932.YLL003W; -.
DR iPTMnet; Q12369; -.
DR PaxDb; Q12369; -.
DR PRIDE; Q12369; -.
DR EnsemblFungi; YLL003W_mRNA; YLL003W; YLL003W.
DR GeneID; 850657; -.
DR KEGG; sce:YLL003W; -.
DR SGD; S000003926; SFI1.
DR VEuPathDB; FungiDB:YLL003W; -.
DR eggNOG; KOG4775; Eukaryota.
DR HOGENOM; CLU_304658_0_0_1; -.
DR InParanoid; Q12369; -.
DR OMA; WDRATVR; -.
DR BioCyc; YEAST:G3O-32108-MON; -.
DR EvolutionaryTrace; Q12369; -.
DR PRO; PR:Q12369; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12369; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005825; C:half bridge of spindle pole body; IDA:SGD.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:SGD.
DR GO; GO:0051225; P:spindle assembly; IMP:SGD.
DR GO; GO:0030474; P:spindle pole body duplication; IMP:SGD.
DR InterPro; IPR013665; Sfi1_dom.
DR InterPro; IPR018907; Spindle_body_associated_C_dom.
DR Pfam; PF08457; Sfi1; 1.
DR Pfam; PF10638; Sfi1_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Mitosis;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..946
FT /note="Protein SFI1"
FT /id="PRO_0000269647"
FT REGION 846..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 855
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT HELIX 222..240
FT /evidence="ECO:0007829|PDB:2DOQ"
FT HELIX 241..245
FT /evidence="ECO:0007829|PDB:2DOQ"
FT HELIX 247..294
FT /evidence="ECO:0007829|PDB:2DOQ"
FT HELIX 643..675
FT /evidence="ECO:0007829|PDB:2GV5"
FT HELIX 677..706
FT /evidence="ECO:0007829|PDB:2GV5"
FT TURN 707..709
FT /evidence="ECO:0007829|PDB:2GV5"
SQ SEQUENCE 946 AA; 112979 MW; B58B966607801618 CRC64;
MGKFGTTNKS TENLLRDKFV PETSPTNIPT DVLIKQGQIT DSTESLIHGG AERYIVNALK
PIELNKTEGF FEDPPFHLPS PPVDSTNLEY EDVTDLPKNG LRYDLNDISV EVIEDLYRQI
EAFLVHFKLS RSFLQIFKNY VNILIQEGIN PLRDEYFTIL EDELKGFFTF NSVIEEILEI
FLIHPRNKFI ALSLAEYTYA KNKIRRHFNH WKTVCELNEE ANRFANQAKL RVQEAVFYIW
SDKTLKYSQM ANDEAESFRN TWLLFRSFQQ WITLTQTLKE QSRLADQAFL NKMFRKILKA
QEHWKHLETV NTDNIKKIFL RTTFHIWKLR HKEINYHGLE RRIFERIKQK VINYEYNKSI
AEKVRSFSLQ RKYLNKWEKK NIENEDKLGA LYELENKFIK QKFFRKLNRS FQHSQQEAIA
KSKLNQTLLR CVFEKMWLKR FEDHLHLYSI VSLKEANLVK RIFHSWKKLL YIDLKASDYS
RTNLLKSSLR SWKLEVKLKI FEQKCKKSIQ ASAYRTWRKR IQYGKISSEH VKTAFCAKYL
GVWKRRMLQM NSMNDEASKF YEEGLVNECL AIWKERLIKT KELEDRYNFL CKTHAILTVK
RTLMHIDNVH LLYTKLAPSM DRVKLSKAFL KWRKATRFKV RHKLNDILHV YEKSKERELQ
SQLFNAWRNR FCFYTEECNI QAISKRNYQL EKMVLKKFRE RLLEIVKSEE LADEVREEFV
LVKTFYIWKT HLDEIFYMST LLEQSEANKQ FIITSKFLKM WSLRFLKIKR NDETVEVFRH
RWDRATVRGL LLLWKNRSDS SPKRRKDFNL KHELKTPIRS DSQNASTIPG SERIKQHRME
AMKSHYSRAR RAIPSPVKSS SVLDSTAKKQ INLESTTGLN GSPTRGKPLR YSPRRTTRNM
PSKVDHIDFG RIPAVPFSLS ANSPKIDQDM DYIREHDKSP LSRKRQ
