RLF2_YEAST
ID RLF2_YEAST Reviewed; 606 AA.
AC Q12495; D6W428;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Chromatin assembly factor 1 subunit p90;
DE AltName: Full=CAF-1 90 kDa subunit;
DE AltName: Full=RAP1 localization factor 2;
GN Name=RLF2; Synonyms=CAC1; OrderedLocusNames=YPR018W; ORFNames=YP9531.12;
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].
RX PubMed=9030688; DOI=10.1101/gad.11.3.358;
RA Enomoto S., McCune-Zierath P.D., Gerami-Nejad M., Sanders M.A., Berman J.;
RT "RLF2, a subunit of yeast chromatin assembly factor-I, is required for
RT telomeric chromatin function in vivo.";
RL Genes Dev. 11:358-370(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
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 PROTEIN SEQUENCE OF 237-247 AND 554-560, AND CHARACTERIZATION.
RX PubMed=9030687; DOI=10.1101/gad.11.3.345;
RA Kaufman P.D., Kobayashi R., Stillman B.;
RT "Ultraviolet radiation sensitivity and reduction of telomeric silencing in
RT Saccharomyces cerevisiae cells lacking chromatin assembly factor-I.";
RL Genes Dev. 11:345-357(1997).
RN [5]
RP INTERACTION WITH SAS2.
RX PubMed=11731480; DOI=10.1101/gad.929001;
RA Meijsing S.H., Ehrenhofer-Murray A.E.;
RT "The silencing complex SAS-I links histone acetylation to the assembly of
RT repressed chromatin by CAF-I and Asf1 in Saccharomyces cerevisiae.";
RL Genes Dev. 15:3169-3182(2001).
RN [6]
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).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-78; SER-94 AND THR-509, 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: Acts as a component of chromatin assembly factor 1 (CAF-1),
CC which assembles histone octamers onto replicating DNA in vitro. It
CC performs the first step of the nucleosome assembly process, bringing
CC newly synthesized histones H3 and H4 to replicating DNA; histones
CC H2A/H2B can bind to this chromatin precursor subsequent to DNA
CC replication to complete the histone octamer. p90 may facilitate the
CC efficient and timely assembly of histones into telomeric chromatin.
CC -!- SUBUNIT: Component of chromatin assembly factor 1 (CAF-1), which is
CC composed of MSI1/p50, CAC2/p60 and RLF2/CAC1/p90. RLF2 interacts with
CC SAS2. {ECO:0000269|PubMed:11731480}.
CC -!- INTERACTION:
CC Q12495; P13712: MSI1; NbExp=5; IntAct=EBI-3913, EBI-11391;
CC Q12495; P54790: ORC3; NbExp=3; IntAct=EBI-3913, EBI-12576;
CC Q12495; P15873: POL30; NbExp=3; IntAct=EBI-3913, EBI-12993;
CC Q12495; P40963: SAS2; NbExp=4; IntAct=EBI-3913, EBI-16476;
CC Q12495; Q04003: SAS4; NbExp=3; IntAct=EBI-3913, EBI-38500;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 1590 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RLF2 family. {ECO:0000305}.
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DR EMBL; Z49919; CAA90163.1; -; Genomic_DNA.
DR EMBL; Z71255; CAA95014.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11444.1; -; Genomic_DNA.
DR PIR; S57552; S57552.
DR RefSeq; NP_015343.1; NM_001184115.1.
DR PDB; 5EJO; X-ray; 2.75 A; A=519-606.
DR PDB; 5JBM; X-ray; 3.00 A; A=457-606.
DR PDBsum; 5EJO; -.
DR PDBsum; 5JBM; -.
DR AlphaFoldDB; Q12495; -.
DR SMR; Q12495; -.
DR BioGRID; 36195; 291.
DR ComplexPortal; CPX-568; Chromatin assembly factor 1 complex.
DR DIP; DIP-923N; -.
DR IntAct; Q12495; 147.
DR MINT; Q12495; -.
DR STRING; 4932.YPR018W; -.
DR iPTMnet; Q12495; -.
DR MaxQB; Q12495; -.
DR PaxDb; Q12495; -.
DR PRIDE; Q12495; -.
DR EnsemblFungi; YPR018W_mRNA; YPR018W; YPR018W.
DR GeneID; 856129; -.
DR KEGG; sce:YPR018W; -.
DR SGD; S000006222; RLF2.
DR VEuPathDB; FungiDB:YPR018W; -.
DR eggNOG; KOG4363; Eukaryota.
DR HOGENOM; CLU_028547_0_0_1; -.
DR InParanoid; Q12495; -.
DR OMA; YQGTFTK; -.
DR BioCyc; YEAST:G3O-34178-MON; -.
DR PRO; PR:Q12495; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12495; protein.
DR GO; GO:0033186; C:CAF-1 complex; IDA:SGD.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:SGD.
DR GO; GO:0000786; C:nucleosome; IDA:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0031497; P:chromatin assembly; IDA:ComplexPortal.
DR GO; GO:0006281; P:DNA repair; IC:ComplexPortal.
DR GO; GO:0006260; P:DNA replication; IC:ComplexPortal.
DR GO; GO:0006335; P:DNA replication-dependent chromatin assembly; IDA:SGD.
DR GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
DR InterPro; IPR022043; CAF1A.
DR Pfam; PF12253; CAF1A; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Direct protein sequencing; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..606
FT /note="Chromatin assembly factor 1 subunit p90"
FT /id="PRO_0000089272"
FT REGION 116..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 128..240
FT /evidence="ECO:0000255"
FT COMPBIAS 116..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..431
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 78
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 509
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT HELIX 527..537
FT /evidence="ECO:0007829|PDB:5EJO"
FT HELIX 544..554
FT /evidence="ECO:0007829|PDB:5EJO"
FT HELIX 560..570
FT /evidence="ECO:0007829|PDB:5EJO"
FT STRAND 571..573
FT /evidence="ECO:0007829|PDB:5EJO"
FT STRAND 577..580
FT /evidence="ECO:0007829|PDB:5JBM"
FT STRAND 584..587
FT /evidence="ECO:0007829|PDB:5EJO"
FT HELIX 589..598
FT /evidence="ECO:0007829|PDB:5EJO"
SQ SEQUENCE 606 AA; 70210 MW; C593E6E4FE5FD778 CRC64;
MEQHLKSIPL QDDTKKKGIL SFFQNTTTVK SNKFLTKEKD VITLDDPKED VSGPMIETVK
QETMKSINKE CADEMKTTPK KANAEDKLLC YKNSPIQSTK YDRNTNKQVP NGNIIAIETK
SRSSSPCSKR ELSSSKKEEA KREKELKKQQ RAEEKHRKEL LRQEEKKKKE LKVEEERQRR
AELKKQKEEE KRRKEEARLE AKRRKEEERL KKEEEIRLKE EAKERAQSRI GNFFKKLSDS
NTPVVEKSDY EKFFLPFYAK DGVRVSNKWK LTKVELEGSK RKIDDELLNS KDKTSSDDLL
NWLQSRRLPR GHKIKRKAVD VLQQMPLKEK TDDELQSLLA QVPHKYIKFY ENVRPPFIGT
YSMDFTLPPN DPFSTKGTGF NYDYDSDVEW VNEEEEGEVD NLESGEEEEE EEDDEDVPSE
GEFDGFLDSE ENSDLDGLPC AKRKFVGPLI PTICLKSNFE NLSEENKRYL QQLKAEVIIE
TDGPIDPFKE PKTSSLPSKR SNSDLQAQTA SQSQSPEKKQ KAMITDPMDL LRLFDGVQDS
TFSLGTVTEI AQKNLPQYNK QTIKNTIKEY AIRSSGKGDL PRKWVIKDAQ NWENLRANAN
MPTPSL
