RIF1_YEAST
ID RIF1_YEAST Reviewed; 1916 AA.
AC P29539; D6VQS1; P89507;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Telomere length regulator protein RIF1;
DE AltName: Full=RAP1-interacting factor 1;
GN Name=RIF1; OrderedLocusNames=YBR275C; ORFNames=YBR1743;
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], FUNCTION, AND INTERACTION WITH RAP1.
RC STRAIN=ATCC 204510 / AB320;
RX PubMed=1577274; DOI=10.1101/gad.6.5.801;
RA Hardy C.F.J., Sussel L., Shore D.;
RT "A RAP1-interacting protein involved in transcriptional silencing and
RT telomere length regulation.";
RL Genes Dev. 6:801-814(1992).
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, AND SEQUENCE REVISION TO 732.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1096.
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 [5]
RP FUNCTION.
RX PubMed=7867933; DOI=10.1101/gad.9.3.370;
RA Buck S.W., Shore D.;
RT "Action of a RAP1 carboxy-terminal silencing domain reveals an underlying
RT competition between HMR and telomeres in yeast.";
RL Genes Dev. 9:370-384(1995).
RN [6]
RP FUNCTION, AND INTERACTION WITH RAP1 AND RIF2.
RX PubMed=9087429; DOI=10.1101/gad.11.6.748;
RA Wotton D., Shore D.;
RT "A novel Rap1p-interacting factor, Rif2p, cooperates with Rif1p to regulate
RT telomere length in Saccharomyces cerevisiae.";
RL Genes Dev. 11:748-760(1997).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=9710643; DOI=10.1128/mcb.18.9.5600;
RA Bourns B.D., Alexander M.K., Smith A.M., Zakian V.A.;
RT "Sir proteins, Rif proteins, and Cdc13p bind Saccharomyces telomeres in
RT vivo.";
RL Mol. Cell. Biol. 18:5600-5608(1998).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10531008; DOI=10.1016/s0960-9822(99)80483-7;
RA Mishra K., Shore D.;
RT "Yeast Ku protein plays a direct role in telomeric silencing and
RT counteracts inhibition by rif proteins.";
RL Curr. Biol. 9:1123-1126(1999).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=12589054; DOI=10.1091/mbc.e02-08-0457;
RA Smith C.D., Smith D.L., DeRisi J.L., Blackburn E.H.;
RT "Telomeric protein distributions and remodeling through the cell cycle in
RT Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 14:556-570(2003).
RN [10]
RP FUNCTION.
RX PubMed=15572688; DOI=10.1128/mcb.24.24.10857-10867.2004;
RA Levy D.L., Blackburn E.H.;
RT "Counting of Rif1p and Rif2p on Saccharomyces cerevisiae telomeres
RT regulates telomere length.";
RL Mol. Cell. Biol. 24:10857-10867(2004).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1637, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1637, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97; SER-1637 AND SER-1795,
RP AND 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1637 AND SER-1852, AND
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Negatively regulates telomere length by preventing telomere
CC elongation or promoting degradation of the telomere ends. Recruited to
CC telomeres by interaction with the C-terminus of RAP1, which binds
CC directly to telomeric repeat DNA. This may create a negative feedback
CC loop in which the addition of new telomere repeats creates binding
CC sites for inhibitors of telomere length extension. May also influence
CC the balance of transcriptional silencing at telomeres and the silent
CC mating type locus HMR, which is mediated by SIR (Silent Information
CC Regulator) proteins including SIR3 and SIR4. RIF1 competes with SIR
CC proteins for binding to the C-terminus of RAP1. In the absence of RIF1,
CC a limiting cellular pool of SIR proteins may preferentially associate
CC with RAP1 at sub-telomeric loci, causing enhanced telomeric silencing
CC and attenuated silencing of the HMR locus.
CC {ECO:0000269|PubMed:10531008, ECO:0000269|PubMed:15572688,
CC ECO:0000269|PubMed:1577274, ECO:0000269|PubMed:7867933,
CC ECO:0000269|PubMed:9087429}.
CC -!- SUBUNIT: Interacts with RIF2 and RAP1. {ECO:0000269|PubMed:1577274,
CC ECO:0000269|PubMed:9087429}.
CC -!- INTERACTION:
CC P29539; P11938: RAP1; NbExp=3; IntAct=EBI-2083307, EBI-14821;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, telomere. Note=Localizes to
CC telomeres. Telomere association begins in G1/S, attains a peak during
CC late G2/S phase of the cell cycle, and is lost during telophase.
CC Localization to telomeres may be increased by telomere uncapping caused
CC by expression of a mutant telomerase RNA subunit (TLC1).
CC -!- SIMILARITY: Belongs to the RIF1 family. {ECO:0000305}.
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DR EMBL; X66501; CAA47121.1; -; Genomic_DNA.
DR EMBL; Z36144; CAA85238.1; -; Genomic_DNA.
DR EMBL; Z36145; CAA85240.1; -; Genomic_DNA.
DR EMBL; X76053; CAA53638.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07391.2; -; Genomic_DNA.
DR PIR; S46157; S46157.
DR RefSeq; NP_009834.4; NM_001178623.4.
DR PDB; 4BJS; X-ray; 1.94 A; A/B/C/D=1857-1916.
DR PDB; 4BJT; X-ray; 1.61 A; D/E/F=1752-1771.
DR PDB; 5NVR; X-ray; 3.95 A; A=177-1282.
DR PDB; 5NW5; X-ray; 6.50 A; A/B=100-1321.
DR PDBsum; 4BJS; -.
DR PDBsum; 4BJT; -.
DR PDBsum; 5NVR; -.
DR PDBsum; 5NW5; -.
DR AlphaFoldDB; P29539; -.
DR SMR; P29539; -.
DR BioGRID; 32970; 127.
DR ComplexPortal; CPX-2112; Telosome.
DR DIP; DIP-801N; -.
DR IntAct; P29539; 8.
DR MINT; P29539; -.
DR STRING; 4932.YBR275C; -.
DR iPTMnet; P29539; -.
DR SwissPalm; P29539; -.
DR MaxQB; P29539; -.
DR PaxDb; P29539; -.
DR PRIDE; P29539; -.
DR EnsemblFungi; YBR275C_mRNA; YBR275C; YBR275C.
DR GeneID; 852578; -.
DR KEGG; sce:YBR275C; -.
DR SGD; S000000479; RIF1.
DR VEuPathDB; FungiDB:YBR275C; -.
DR eggNOG; ENOG502QPT7; Eukaryota.
DR HOGENOM; CLU_002800_0_0_1; -.
DR InParanoid; P29539; -.
DR OMA; CDARRIN; -.
DR BioCyc; YEAST:G3O-29196-MON; -.
DR PRO; PR:P29539; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P29539; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0070187; C:shelterin complex; IPI:SGD.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:SGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000729; P:DNA double-strand break processing; IMP:SGD.
DR GO; GO:0006270; P:DNA replication initiation; IGI:SGD.
DR GO; GO:0032297; P:negative regulation of DNA-templated DNA replication initiation; IMP:SGD.
DR GO; GO:0101018; P:negative regulation of mitotic DNA replication initiation from late origin; IMP:SGD.
DR GO; GO:0070198; P:protein localization to chromosome, telomeric region; IMP:SGD.
DR GO; GO:0097752; P:regulation of DNA stability; IMP:SGD.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IMP:SGD.
DR GO; GO:0016233; P:telomere capping; IMP:SGD.
DR GO; GO:0000723; P:telomere maintenance; IMP:SGD.
DR DisProt; DP01607; -.
DR IDEAL; IID50206; -.
DR InterPro; IPR028566; Rif1.
DR InterPro; IPR022031; Rif1_N.
DR PANTHER; PTHR22928; PTHR22928; 1.
DR Pfam; PF12231; Rif1_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Chromosome; Nucleus; Phosphoprotein;
KW Reference proteome; Telomere.
FT CHAIN 1..1916
FT /note="Telomere length regulator protein RIF1"
FT /id="PRO_0000097336"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1314..1372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1441..1476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1606..1678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1789..1811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1829..1854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1314..1357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1441..1461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1462..1476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1627..1647
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1650..1668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1797..1811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 1637
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1795
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 1852
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 580
FT /note="C -> S (in Ref. 1; CAA47121)"
FT /evidence="ECO:0000305"
FT CONFLICT 732
FT /note="A -> T (in Ref. 2; CAA85238 and 4; CAA53638)"
FT /evidence="ECO:0000305"
FT HELIX 1859..1861
FT /evidence="ECO:0007829|PDB:4BJS"
FT HELIX 1866..1876
FT /evidence="ECO:0007829|PDB:4BJS"
FT HELIX 1880..1885
FT /evidence="ECO:0007829|PDB:4BJS"
FT HELIX 1888..1907
FT /evidence="ECO:0007829|PDB:4BJS"
SQ SEQUENCE 1916 AA; 217931 MW; 07070AF02361D96F CRC64;
MSKDFSDKKK HTIDRIDQHI LRRSQHDNYS NGSSPWMKTN LPPPSPQAHM HIQSDLSPTP
KRRKLASSSD CENKQFDLSA INKNLYPEDT GSRLMQSLPE LSASNSDNVS PVTKSVAFSD
RIESSPIYRI PGSSPKPSPS SKPGKSILRN RLPSVRTVSD LSYNKLQYTQ HKLHNGNIFT
SPYKETRVNP RALEYWVSGE IHGLVDNESV SEFKEIIEGG LGILRQESED YVARRFEVYA
TFNNIIPILT TKNVNEVDQK FNILIVNIES IIEICIPHLQ IAQDTLLSSS EKKNPFVIRL
YVQIVRFFSA IMSNFKIVKW LTKRPDLVNK LKVIYRWTTG ALRNENSNKI IITAQVSFLR
DEKFGTFFLS NEEIKPIIST FTEIMEINSH NLIYEKLLLI RGFLSKYPKL MIETVTSWLP
GEVLPRIIIG DEIYSMKILI TSIVVLLELL KKCLDFVDEH ERIYQCIMLS PVCETIPEKF
LSKLPLNSYD SANLDKVTIG HLLTQQIKNY IVVKNDNKIA MDLWLSMTGL LYDSGKRVYD
LTSESNKVWF DLNNLCFINN HPKTRLMSIK VWRIITYCIC TKISQKNQEG NKSLLSLLRT
PFQMTLPYVN DPSAREGIIY HLLGVVYTAF TSNKNLSTDM FELFWDHLIT PIYEDYVFKY
DSIHLQNVLF TVLHLLIGGK NADVALERKY KKHIHPMSVI ASEGVKLKDI SSLPPQIIKR
EYDKIMKVVF QAVEVAISNV NLAHDLILTS LKHLPEDRKD QTHLESFSSL ILKVTQNNKD
TPIFRDFFGA VTSSFVYTFL DLFLRKNDSS LVNFNIQISK VGISQGNMTL DLLKDVIRKA
RNETSEFLII EKFLELDDKK TEVYAQNWVG STLLPPNISF REFQSLANIV NKVPNENSIE
NFLDLCLKLS FPVNLFTLLH VSMWSNNNFI YFIQSYVSKN ENKLNVDLIT LLKTSLPGNP
ELFSGLLPFL RRNKFMDILE YCIHSNPNLL NSIPDLNSDL LLKLLPRSRA SYFAANIKLF
KCSEQLTLVR WLLKGQQLEQ LNQNFSEIEN VLQNASDSEL EKSEIIRELL HLAMANPIEP
LFSGLLNFCI KNNMADHLDE FCGNMTSEVL FKISPELLLK LLTYKEKPNG KLLAAVIEKI
ENGDDDYILE LLEKIIIQKE IQILEKLKEP LLVFFLNPVS SNMQKHKKST NMLRELVLLY
LTKPLSRSAA KKFFSMLISI LPPNPNYQTI DMVNLLIDLI KSHNRKFKDK RTYNATLKTI
GKWIQESGVV HQGDSSKEIE AIPDTKSMYI PCEGSENKLS NLQRKVDSQD IQVPATQGMK
EPPSSIQISS QISAKDSDSI SLKNTAIMNS SQQESHANRS RSIDDETLEE VDNESIREID
QQMKSTQLDK NVANHSNICS TKSDEVDVTE LHESIDTQSS EVNAYQPIEV LTSELKAVTN
RSIKTNPDHN VVNSDNPLKR PSKETPTSEN KRSKGHETMV DVLVSEEQAV SPSSDVICTN
IKSIANEESS LALRNSIKVE TNCNENSLNV TLDLDQQTIT KEDGKGQVEH VQRQENQESM
NKINSKSFTQ DNIAQYKSVK KARPNNEGEN NDYACNVEQA SPVRNEVPGD GIQIPSGTIL
LNSSKQTEKS KVDDLRSDED EHGTVAQEKH QVGAINSRNK NNDRMDSTPI QGTEEESREV
VMTEEGINVR LEDSGTCELN KNLKGPLKGD KDANINDDFV PVEENVRDEG FLKSMEHAVS
KETGLEEQPE VADISVLPEI RIPIFNSLKM QGSKSQIKEK LKKRLQRNEL MPPDSPPRMT
ENTNINAQNG LDTVPKTIGG KEKHHEIQLG QAHTEADGEP LLGGDGNEDA TSREATPSLK
VHFFSKKSRR LVARLRGFTP GDLNGISVEE RRNLRIELLD FMMRLEYYSN RDNDMN
