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   02-SEP-2026, entry version 189.
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, AND INTERACTION WITH RAP1.
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 RAP1 (via C-terminus) (PubMed:1577274,
CC       PubMed:7867933, PubMed:9087429). Interacts with RIF2 (PubMed:7867933,
CC       PubMed:9087429). {ECO:0000269|PubMed:1577274,
CC       ECO:0000269|PubMed:7867933, 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   AlphaFoldDB; P29539; -.
DR   SMR; P29539; -.
DR   BioGRID; 32970; 151.
DR   ComplexPortal; CPX-2112; Telosome complex.
DR   DIP; DIP-801N; -.
DR   FunCoup; P29539; 146.
DR   IntAct; P29539; 16.
DR   MINT; P29539; -.
DR   STRING; 4932.YBR275C; -.
DR   GlyGen; P29539; 1 site.
DR   iPTMnet; P29539; -.
DR   SwissPalm; P29539; -.
DR   PaxDb; 4932-YBR275C; -.
DR   PeptideAtlas; P29539; -.
DR   EnsemblFungi; YBR275C_mRNA; YBR275C; YBR275C.
DR   GeneID; 852578; -.
DR   KEGG; sce:YBR275C; -.
DR   AGR; SGD:S000000479; -.
DR   SGD; S000000479; RIF1.
DR   VEuPathDB; FungiDB:YBR275C; -.
DR   eggNOG; ENOG502QPT7; Eukaryota.
DR   HOGENOM; CLU_002800_0_0_1; -.
DR   InParanoid; P29539; -.
DR   OMA; HERIYQC; -.
DR   OrthoDB; 4070686at2759; -.
DR   BioCyc; YEAST:G3O-29196-MONOMER; -.
DR   BioGRID-ORCS; 852578; 0 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P29539; -.
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:0140445; C:chromosome, telomeric repeat region; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0070187; C:shelterin complex; IPI:ComplexPortal.
DR   GO; GO:0019237; F:centromeric DNA binding; IDA:SGD.
DR   GO; GO:0003688; F:DNA replication origin binding; IDA:SGD.
DR   GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:SGD.
DR   GO; GO:0042162; F:telomeric repeat DNA binding; IDA:SGD.
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 formation; IMP:SGD.
DR   GO; GO:0016233; P:telomere capping; IMP:SGD.
DR   GO; GO:0000723; P:telomere maintenance; IMP:SGD.
DR   CDD; cd14267; Rif1_CTD_C-II_like; 1.
DR   DisProt; DP01607; -.
DR   Gene3D; 6.10.140.1760; -; 1.
DR   IDEAL; IID50206; -.
DR   InterPro; IPR022031; Rif1_N.
DR   PANTHER; PTHR22928; TELOMERE-ASSOCIATED PROTEIN RIF1; 1.
DR   PANTHER; PTHR22928:SF3; TELOMERE-ASSOCIATED PROTEIN RIF1; 1.
DR   Pfam; PF12231; Rif1_N; 1.
DR   PDBsum; 4BJS; -.
DR   PDBsum; 4BJT; -.
DR   PDBsum; 5NVR; -.
DR   PDBsum; 5NW5; -.
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..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1324..1334
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1342..1355
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1615..1625
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1626..1635
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1800..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
//