ID TOF1_YEAST Reviewed; 1238 AA. AC P53840; D6W0S1; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 04-NOV-2026, entry version 186. DE RecName: Full=Topoisomerase 1-associated factor 1; GN Name=TOF1; OrderedLocusNames=YNL273W; ORFNames=N0636; 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=9169873; DOI=10.1038/387s093; RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F., RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its RT evolutionary implications."; RL Nature 387:93-98(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 IDENTIFICATION. RX PubMed=10028183; RX DOI=10.1002/(sici)1097-0061(19990115)15:1<35::aid-yea340>3.0.co;2-r; RA Park H., Sternglanz R.; RT "Identification and characterization of the genes for two topoisomerase I- RT interacting proteins from Saccharomyces cerevisiae."; RL Yeast 15:35-41(1999). RN [4] RP FUNCTION. RX PubMed=11156979; DOI=10.1093/genetics/157.2.567; RA Foss E.J.; RT "Tof1p regulates DNA damage responses during S phase in Saccharomyces RT cerevisiae."; RL Genetics 157:567-577(2001). RN [5] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=12944972; DOI=10.1038/nature01900; RA Katou Y., Kanoh Y., Bando M., Noguchi H., Tanaka H., Ashikari T., RA Sugimoto K., Shirahige K.; RT "S-phase checkpoint proteins Tof1 and Mrc1 form a stable replication- RT pausing complex."; RL Nature 424:1078-1083(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 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 [8] RP FUNCTION, AND INTERACTION WITH CSM3. RX PubMed=14742714; DOI=10.1091/mbc.e03-08-0619; RA Mayer M.L., Pot I., Chang M., Xu H., Aneliunas V., Kwok T., Newitt R., RA Aebersold R., Boone C., Brown G.W., Hieter P.; RT "Identification of protein complexes required for efficient sister RT chromatid cohesion."; RL Mol. Biol. Cell 15:1736-1745(2004). RN [9] RP FUNCTION, AND INTERACTION WITH WSS1. RX PubMed=15598824; DOI=10.1093/nar/gkh994; RA O'Neill B.M., Hanway D., Winzeler E.A., Romesberg F.E.; RT "Coordinated functions of WSS1, PSY2 and TOF1 in the DNA damage response."; RL Nucleic Acids Res. 32:6519-6530(2004). RN [10] RP FUNCTION, IDENTIFICATION IN THE FPC COMPLEX, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=15755447; DOI=10.1016/j.jmb.2005.01.041; RA Nedelcheva M.N., Roguev A., Dolapchiev L.B., Shevchenko A., Taskov H.B., RA Shevchenko A., Stewart A.F., Stoynov S.S.; RT "Uncoupling of unwinding from DNA synthesis implies regulation of MCM RT helicase by Tof1/Mrc1/Csm3 checkpoint complex."; RL J. Mol. Biol. 347:509-521(2005). RN [11] RP FUNCTION. RX PubMed=16137625; DOI=10.1016/j.molcel.2005.07.028; RA Tourriere H., Versini G., Cordon-Preciado V., Alabert C., Pasero P.; RT "Mrc1 and Tof1 promote replication fork progression and recovery RT independently of Rad53."; RL Mol. Cell 19:699-706(2005). RN [12] RP FUNCTION. RX PubMed=16024805; DOI=10.1128/mcb.25.15.6707-6721.2005; RA Archambault V., Ikui A.E., Drapkin B.J., Cross F.R.; RT "Disruption of mechanisms that prevent rereplication triggers a DNA damage RT response."; RL Mol. Cell. Biol. 25:6707-6721(2005). RN [13] RP INTERACTION WITH ESC4. RX PubMed=16569515; DOI=10.1016/j.dnarep.2006.02.005; RA Chin J.K., Bashkirov V.I., Heyer W.-D., Romesberg F.E.; RT "Esc4/Rtt107 and the control of recombination during replication."; RL DNA Repair 5:618-628(2006). RN [14] RP FUNCTION OF THE FPC COMPLEX. RX PubMed=16219777; DOI=10.1534/genetics.105.046128; RA Redon C., Pilch D.R., Bonner W.M.; RT "Genetic analysis of Saccharomyces cerevisiae H2A serine 129 mutant RT suggests a functional relationship between H2A and the sister-chromatid RT cohesion partners Csm3-Tof1 for the repair of topoisomerase I-induced DNA RT damage."; RL Genetics 172:67-76(2006). RN [15] RP FUNCTION OF THE FPC COMPLEX. RX PubMed=16418273; DOI=10.1073/pnas.0506540103; RA Mohanty B.K., Bairwa N.K., Bastia D.; RT "The Tof1p-Csm3p protein complex counteracts the Rrm3p helicase to control RT replication termination of Saccharomyces cerevisiae."; RL Proc. Natl. Acad. Sci. U.S.A. 103:897-902(2006). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1213, 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626; SER-654 AND SER-1213, 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1056; SER-1058 AND SER-1213, RP AND 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: Forms a fork protection complex (FPC) with CSM3 and which is CC required for chromosome segregation during meiosis and DNA damage CC repair. FPC coordinates leading and lagging strand synthesis and moves CC with the replication fork. FPC stabilizes replication forks in a CC configuration that is recognized by replication checkpoint sensors and CC protects stalled replication forks against the fork-releasing activity CC of RRM3 helicase. {ECO:0000269|PubMed:11156979, CC ECO:0000269|PubMed:12944972, ECO:0000269|PubMed:14742714, CC ECO:0000269|PubMed:15598824, ECO:0000269|PubMed:15755447, CC ECO:0000269|PubMed:16024805, ECO:0000269|PubMed:16137625, CC ECO:0000269|PubMed:16219777, ECO:0000269|PubMed:16418273}. CC -!- SUBUNIT: Component of the fork protection complex (FPC) consisting of CC TOF1 and CSM3. Interacts with WSS1 and ESC4. CC {ECO:0000269|PubMed:14742714, ECO:0000269|PubMed:15598824, CC ECO:0000269|PubMed:15755447, ECO:0000269|PubMed:16569515}. CC -!- INTERACTION: CC P53840; Q08032: CDC45; NbExp=3; IntAct=EBI-28257, EBI-4292; CC P53840; Q04659: CSM3; NbExp=7; IntAct=EBI-28257, EBI-28093; CC P53840; P25588: MRC1; NbExp=4; IntAct=EBI-28257, EBI-412442; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12944972, CC ECO:0000269|PubMed:14562095}. Note=Associated with chromatin during S CC phase. CC -!- MISCELLANEOUS: Present with 952 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the timeless family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z71549; CAA96181.1; -; Genomic_DNA. DR EMBL; BK006947; DAA10287.1; -; Genomic_DNA. DR PIR; S63247; S63247. DR RefSeq; NP_014126.1; NM_001183111.1. DR PDB; 6SKL; EM; 3.70 A; X=1-1238. DR PDB; 7PMK; EM; 3.20 A; X=1-1238. DR PDB; 7PMN; EM; 3.20 A; X=1-1238. DR PDB; 8B9A; EM; 3.50 A; X=1-1238. DR PDB; 8B9B; EM; 3.50 A; X=1-1238. DR PDB; 8B9C; EM; 4.60 A; X=1-1238. DR PDB; 8KG6; EM; 3.07 A; K=1-1238. DR PDB; 8XGC; EM; 3.70 A; I=1-1238. DR PDB; 9E2W; EM; 3.30 A; X=1-1238. DR PDB; 9E2X; EM; 3.50 A; X=1-1238. DR PDB; 9E2Y; EM; 3.20 A; X=354-396. DR AlphaFoldDB; P53840; -. DR EMDB; EMD-10227; -. DR EMDB; EMD-13537; -. DR EMDB; EMD-13539; -. DR EMDB; EMD-15924; -. DR EMDB; EMD-37211; -. DR EMDB; EMD-38317; -. DR EMDB; EMD-47470; -. DR EMDB; EMD-47471; -. DR EMDB; EMD-47472; -. DR SMR; P53840; -. DR BioGRID; 35567; 337. DR ComplexPortal; CPX-1673; Replication fork protection complex. DR DIP; DIP-4272N; -. DR FunCoup; P53840; 83. DR IntAct; P53840; 12. DR STRING; 4932.YNL273W; -. DR iPTMnet; P53840; -. DR PaxDb; 4932-YNL273W; -. DR PeptideAtlas; P53840; -. DR EnsemblFungi; YNL273W_mRNA; YNL273W; YNL273W. DR GeneID; 855448; -. DR KEGG; sce:YNL273W; -. DR AGR; SGD:S000005217; -. DR SGD; S000005217; TOF1. DR VEuPathDB; FungiDB:YNL273W; -. DR eggNOG; KOG1974; Eukaryota. DR HOGENOM; CLU_008440_0_0_1; -. DR InParanoid; P53840; -. DR OMA; AAERMNN; -. DR OrthoDB; 310853at2759; -. DR BioCyc; YEAST:G3O-33267-MONOMER; -. DR BioGRID-ORCS; 855448; 2 hits in 10 CRISPR screens. DR PRO; PR:P53840; -. DR Proteomes; UP000002311; Chromosome XIV. DR RNAct; P53840; protein. DR GO; GO:0005829; C:cytosol; IDA:SGD. DR GO; GO:0043596; C:nuclear replication fork; IDA:SGD. DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal. DR GO; GO:0031298; C:replication fork protection complex; IDA:SGD. DR GO; GO:0003677; F:DNA binding; IBA:GO_Central. DR GO; GO:0006281; P:DNA repair; IDA:ComplexPortal. DR GO; GO:0006260; P:DNA replication; IMP:SGD. DR GO; GO:0000076; P:DNA replication checkpoint signaling; IMP:SGD. DR GO; GO:0043570; P:maintenance of DNA repeat elements; IMP:SGD. DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:SGD. DR GO; GO:0043111; P:replication fork arrest; IMP:SGD. DR GO; GO:0031297; P:replication fork processing; IMP:SGD. DR InterPro; IPR044998; Timeless. DR InterPro; IPR006906; Timeless_N. DR InterPro; IPR007725; TIMELESS_PAB. DR InterPro; IPR060740; TOF-1-like_helical. DR PANTHER; PTHR22940:SF4; PROTEIN TIMELESS HOMOLOG; 1. DR PANTHER; PTHR22940; TIMEOUT/TIMELESS-2; 1. DR Pfam; PF04821; TIMELESS; 1. DR Pfam; PF05029; TIMELESS_C; 1. DR Pfam; PF27570; TOF-1-like_helical; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell cycle; DNA damage; DNA repair; KW DNA replication inhibitor; Meiosis; Nucleus; Phosphoprotein; KW Reference proteome. FT CHAIN 1..1238 FT /note="Topoisomerase 1-associated factor 1" FT /id="PRO_0000072620" FT REGION 1008..1051 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1159..1218 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1010..1023 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1038..1050 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1173..1194 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1195..1205 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1209..1218 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 626 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 654 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 1056 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 1058 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 1213 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198" FT HELIX 16..31 FT /evidence="ECO:0007829|PDB:8KG6" FT STRAND 32..34 FT /evidence="ECO:0007829|PDB:7PMK" FT STRAND 37..42 FT /evidence="ECO:0007829|PDB:9E2W" FT STRAND 45..47 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 51..63 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 64..68 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 74..80 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 84..88 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 89..105 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 118..136 FT /evidence="ECO:0007829|PDB:8KG6" FT STRAND 143..145 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 147..168 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 171..173 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 175..187 FT /evidence="ECO:0007829|PDB:8KG6" FT TURN 191..193 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 198..213 FT /evidence="ECO:0007829|PDB:8KG6" FT STRAND 220..223 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 245..248 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 250..259 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 262..271 FT /evidence="ECO:0007829|PDB:8KG6" FT TURN 273..276 FT /evidence="ECO:0007829|PDB:9E2W" FT TURN 281..283 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 284..289 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 292..294 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 300..302 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 330..349 FT /evidence="ECO:0007829|PDB:8KG6" FT TURN 350..352 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 358..360 FT /evidence="ECO:0007829|PDB:8KG6" FT STRAND 363..368 FT /evidence="ECO:0007829|PDB:8KG6" FT TURN 369..371 FT /evidence="ECO:0007829|PDB:8KG6" FT STRAND 372..377 FT /evidence="ECO:0007829|PDB:8KG6" FT TURN 379..383 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 385..394 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 409..412 FT /evidence="ECO:0007829|PDB:9E2W" FT STRAND 414..417 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 418..420 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 431..460 FT /evidence="ECO:0007829|PDB:8KG6" FT TURN 461..463 FT /evidence="ECO:0007829|PDB:8B9A" FT HELIX 464..466 FT /evidence="ECO:0007829|PDB:7PMK" FT HELIX 469..492 FT /evidence="ECO:0007829|PDB:8KG6" FT STRAND 494..496 FT /evidence="ECO:0007829|PDB:9E2W" FT HELIX 499..502 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 507..522 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 526..548 FT /evidence="ECO:0007829|PDB:8KG6" FT TURN 551..554 FT /evidence="ECO:0007829|PDB:9E2W" FT HELIX 557..561 FT /evidence="ECO:0007829|PDB:8KG6" FT STRAND 562..564 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 568..579 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 580..582 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 585..601 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 602..604 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 659..662 FT /evidence="ECO:0007829|PDB:8KG6" FT TURN 663..666 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 669..679 FT /evidence="ECO:0007829|PDB:8KG6" FT TURN 680..684 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 687..698 FT /evidence="ECO:0007829|PDB:8KG6" FT TURN 699..704 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 707..710 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 713..723 FT /evidence="ECO:0007829|PDB:8KG6" FT TURN 725..727 FT /evidence="ECO:0007829|PDB:9E2W" FT STRAND 730..734 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 735..754 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 759..762 FT /evidence="ECO:0007829|PDB:8KG6" FT HELIX 771..776 FT /evidence="ECO:0007829|PDB:8KG6" SQ SEQUENCE 1238 AA; 141120 MW; CF8FEC33EE0088E9 CRC64; MSADLQQGTT NAADFSLTVL RARIALLATA IGGPDYTSQI DPPPYKLGDD CLACLKDLKR WFKLVDDQQK RWDVAMAVAE YRILTDDLLP ILIDWENKCS LAAKLAKNNP DHEEFRNKAY YDKIALNCLQ LLVLMTWPLI VTEQSSSNQI TLYGELKKHQ LVYKKTILSM ESGKVLRAAI RLALDVIKID RLSRTPRDNM VLKLVLNFFR NVIAIEPGEF TINTKKSMPK KGITSIDTLP PNVSMDDISL NTVISSFHKN KVFGFLLTLT SSLSKEFDQD FINIPLLEIM FYFTKDVNQE LLFPRQFETG THSKVVNKNE SSSANNIVTS AGFELSKLLQ KEHQMRKNVI KHTSARHSRF GGLLSIQTPD KTRLTVSGSQ ALVDEKIALQ KLDDSKKWNK RIIKKHQSVA AEGLPNSLLN SQTGKAIFFT ESNGKHFKEF INNFIDSGFN ILLHSVTNYF TTEQDRMVTL EQVEYLLFFA WFVKYQLLRS KIDNSADIKQ VSEALKEVTF ILVSSLLRSA YDLKNWTVTH AGMIAFNELL NLVSRTKAAQ EEDSTDIEFI VSRLFSDERI QLLSNLPKIG SKYSLQFMKS CIELTHSVLK VLEQYSDDKT LVIEGKSRRQ KKFNISEGDI TKLIEEENVD RDEALDILTS SLRSIEVNFQ KVQANYMTEP VIETYINFLE RFRELEDDSI KKVFSFFHRV FVQAKEQALL FRFDLIILLR EMLSPDGLDR MSRSRKYVSQ FSDYFLARLK KRLKKSPAWF VGLLFPPLHN SEVGFYQRYG EYNVLNNESM YAAPASQFKP IPDEEALPPS ILLDMKYGVL VSTLLDDGKT ELLDQLLKHI THTLDIFKSW LTVNVNAGKE TVNPPNEYFT LTGVLNNDPI FKDKDYRALL LLIGYSIPRK INEPCFLPGT VEVSDLTVSC ELVKKYLSTP FETPNGLPSS SYLLRVRSEK DSFSHNEQDG WEGDDDYDYN DPYIVPDDQI LSKSDAAYFK DLDNNASDKL KGTKFSKGIA RSKKKDKRKR RKGEAKTNLP MFGDQDDERP QTVRERHGVF SKEFISDSED DEDLMNPIFF ENETYMRWLL DKNNGQLTED RYIQFAKFAA ERMNNGGVVT GDYTSLFGGS IPSIESIRAT ESSSFAPDKS LISLASHVAS EMSIFDVNNN NNNQLSDDDV NSESRNSLGS SQPSNSQNMF QSEVYSRKES TKRSLEASAA DESDEDEEAI RLFGKKSRVV LSQGDSDD //