RIF2_YEAST
ID RIF2_YEAST Reviewed; 395 AA.
AC Q06208; D6VZ87; E9P8Y1;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Protein RIF2;
DE AltName: Full=RAP1-interacting factor 2;
GN Name=RIF2; OrderedLocusNames=YLR453C;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION, AND SUBUNIT.
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 [5]
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).
CC -!- FUNCTION: Involved in transcriptional silencing and telomere length
CC regulation. Its role in telomere length regulation results from either
CC a block in elongation or promoting degradation of the telomere ends.
CC Loss of RIF1 function results in derepression of an HMR silencer, whose
CC ARS consensus element has been deleted, and in the elongation of
CC telomeres. RAP1 may target the binding of RIF1 to silencers and
CC telomeres. {ECO:0000269|PubMed:9087429}.
CC -!- SUBUNIT: Interacts with RIF1 and RAP1 C-terminus.
CC {ECO:0000269|PubMed:9087429}.
CC -!- INTERACTION:
CC Q06208; P11938: RAP1; NbExp=5; IntAct=EBI-15199, EBI-14821;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, telomere
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 589 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U22382; AAB67535.1; -; Genomic_DNA.
DR EMBL; AY692860; AAT92879.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09753.1; -; Genomic_DNA.
DR PIR; S55975; S55975.
DR RefSeq; NP_013558.3; NM_001182341.3.
DR PDB; 4BJ1; X-ray; 2.94 A; A=65-380.
DR PDB; 4BJ5; X-ray; 3.29 A; A/B=1-395, D/F=36-48.
DR PDB; 4BJ6; X-ray; 3.26 A; A/B=35-395, D/F=36-48.
DR PDBsum; 4BJ1; -.
DR PDBsum; 4BJ5; -.
DR PDBsum; 4BJ6; -.
DR AlphaFoldDB; Q06208; -.
DR SMR; Q06208; -.
DR BioGRID; 31711; 116.
DR ComplexPortal; CPX-2112; Telosome.
DR DIP; DIP-4290N; -.
DR IntAct; Q06208; 2.
DR STRING; 4932.YLR453C; -.
DR MoonDB; Q06208; Predicted.
DR MaxQB; Q06208; -.
DR PaxDb; Q06208; -.
DR PRIDE; Q06208; -.
DR EnsemblFungi; YLR453C_mRNA; YLR453C; YLR453C.
DR GeneID; 851174; -.
DR KEGG; sce:YLR453C; -.
DR SGD; S000004445; RIF2.
DR VEuPathDB; FungiDB:YLR453C; -.
DR HOGENOM; CLU_058672_0_0_1; -.
DR OMA; IDHIVYF; -.
DR BioCyc; YEAST:G3O-32506-MON; -.
DR PRO; PR:Q06208; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06208; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:SGD.
DR GO; GO:0070187; C:shelterin complex; IPI:SGD.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:SGD.
DR GO; GO:0016233; P:telomere capping; IMP:SGD.
DR GO; GO:0000723; P:telomere maintenance; IC:ComplexPortal.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IMP:SGD.
DR DisProt; DP01606; -.
DR IDEAL; IID50224; -.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Nucleus; Reference proteome; Telomere.
FT CHAIN 1..395
FT /note="Protein RIF2"
FT /id="PRO_0000097337"
FT CONFLICT 387
FT /note="K -> R (in Ref. 3; AAT92879)"
FT /evidence="ECO:0000305"
FT HELIX 37..41
FT /evidence="ECO:0007829|PDB:4BJ6"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:4BJ6"
FT HELIX 71..87
FT /evidence="ECO:0007829|PDB:4BJ1"
FT HELIX 93..103
FT /evidence="ECO:0007829|PDB:4BJ1"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:4BJ1"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:4BJ1"
FT HELIX 119..135
FT /evidence="ECO:0007829|PDB:4BJ1"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:4BJ1"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:4BJ1"
FT HELIX 189..198
FT /evidence="ECO:0007829|PDB:4BJ1"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:4BJ6"
FT STRAND 204..214
FT /evidence="ECO:0007829|PDB:4BJ1"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:4BJ5"
FT HELIX 226..241
FT /evidence="ECO:0007829|PDB:4BJ1"
FT STRAND 245..253
FT /evidence="ECO:0007829|PDB:4BJ1"
FT HELIX 260..269
FT /evidence="ECO:0007829|PDB:4BJ1"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:4BJ1"
FT HELIX 284..294
FT /evidence="ECO:0007829|PDB:4BJ1"
FT HELIX 304..318
FT /evidence="ECO:0007829|PDB:4BJ1"
FT HELIX 323..333
FT /evidence="ECO:0007829|PDB:4BJ1"
FT HELIX 337..351
FT /evidence="ECO:0007829|PDB:4BJ1"
FT HELIX 355..364
FT /evidence="ECO:0007829|PDB:4BJ1"
FT TURN 368..370
FT /evidence="ECO:0007829|PDB:4BJ1"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:4BJ6"
SQ SEQUENCE 395 AA; 45643 MW; FF6E3A22C8805DE9 CRC64;
MEHVDSDFAP IRRSKKVVDS DKIVKAISDD LEQKNFTVLR KLNLVPIKKS VSSPKVCKPS
PVKERVDHVF YQKFKSMALQ ELGTNYLSIS YVPSLSKFLS KNLRSMKNCI VFFDKVEHIH
QYAGIDRAVS ETLSLVDINV VIIEMNDYLM KEGIQSSKSK ECIESMGQAS YSGQLDFEAS
EKPSNHTSDL MMMVMRKINN DESIDHIVYF KFEQLDKLST STIIEPSKLT EFINVLSVLE
KSNNIAFKVL IYSNNVSISS LLSTSLKKKL NTKYTVFEMP ILTCAQEQEY LKKMIKFTFD
SGSKLLQSYN SLVTCQLNNK ESNLAIFFEF LKVFPHPFTY LFNAYTEIIV QSRTFDELLD
KIRNRLTIKN YPHSAYNFKK NQRLPLKLTR KVHDR
