ID FKH2_YEAST Reviewed; 862 AA. AC P41813; D6W1B1; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 196. DE RecName: Full=Fork head protein homolog 2 {ECO:0000303|PubMed:10747051}; GN Name=FKH2 {ECO:0000303|PubMed:10747051}; OrderedLocusNames=YNL068C; GN ORFNames=N2403, YNL2403C; 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]. RC STRAIN=ATCC 204508 / S288c; RA Zhu G., Davis T.N.; RT "Two fork head homologs in S. cerevisiae."; RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX PubMed=8701611; RX DOI=10.1002/(sici)1097-0061(19960330)12:4<391::aid-yea921>3.0.co;2-n; RA Poehlmann R., Philippsen P.; RT "Sequencing a cosmid clone of Saccharomyces cerevisiae chromosome XIV RT reveals 12 new open reading frames (ORFs) and an ancient duplication of six RT ORFs."; RL Yeast 12:391-402(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169873; 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 [4] 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 [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-440. RC STRAIN=S288c / FY1676; RX PubMed=8533472; DOI=10.1002/yea.320111008; RA Bergez P., Doignon F., Crouzet M.; RT "The sequence of a 44 420 bp fragment located on the left arm of chromosome RT XIV from Saccharomyces cerevisiae."; RL Yeast 11:967-974(1995). RN [6] RP ERRATUM OF PUBMED:8533472. RX PubMed=8904343; RX DOI=10.1002/(sici)1097-0061(19960315)12:3<297::aid-yea940>3.0.co;2-d; RA Bergez P., Doignon F., Crouzet M.; RL Yeast 12:297-297(1996). RN [7] RP FUNCTION, INTERACTION WITH MCM1, DNA-BINDING, AND DISRUPTION PHENOTYPE. RX PubMed=10959837; DOI=10.1016/s0960-9822(00)00618-7; RA Kumar R., Reynolds D.M., Shevchenko A., Shevchenko A., Goldstone S.D., RA Dalton S.; RT "Forkhead transcription factors, Fkh1p and Fkh2p, collaborate with Mcm1p to RT control transcription required for M-phase."; RL Curr. Biol. 10:896-906(2000). RN [8] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=10747051; DOI=10.1093/genetics/154.4.1533; RA Hollenhorst P.C., Bose M.E., Mielke M.R., Mueller U., Fox C.A.; RT "Forkhead genes in transcriptional silencing, cell morphology and the cell RT cycle. Overlapping and distinct functions for FKH1 and FKH2 in RT Saccharomyces cerevisiae."; RL Genetics 154:1533-1548(2000). RN [9] RP FUNCTION. RX PubMed=10894548; DOI=10.1038/35017581; RA Zhu G., Spellman P.T., Volpe T., Brown P.O., Botstein D., Davis T.N., RA Futcher B.; RT "Two yeast forkhead genes regulate the cell cycle and pseudohyphal RT growth."; RL Nature 406:90-94(2000). RN [10] RP FUNCTION. RX PubMed=10894549; DOI=10.1038/35017589; RA Koranda M., Schleiffer A., Endler L., Ammerer G.; RT "Forkhead-like transcription factors recruit Ndd1 to the chromatin of G2/M- RT specific promoters."; RL Nature 406:94-98(2000). RN [11] RP FUNCTION, AND DNA-BINDING. RX PubMed=11562353; DOI=10.1101/gad.906201; RA Hollenhorst P.C., Pietz G., Fox C.A.; RT "Mechanisms controlling differential promoter-occupancy by the yeast RT forkhead proteins Fkh1p and Fkh2p: implications for regulating the cell RT cycle and differentiation."; RL Genes Dev. 15:2445-2456(2001). RN [12] RP DOMAIN, AND INTERACTION WITH NDD1. RX PubMed=12865300; DOI=10.1101/gad.1074103; RA Reynolds D., Shi B.J., McLean C., Katsis F., Kemp B., Dalton S.; RT "Recruitment of Thr 319-phosphorylated Ndd1p to the FHA domain of Fkh2p RT requires Clb kinase activity: a mechanism for CLB cluster gene RT activation."; RL Genes Dev. 17:1789-1802(2003). RN [13] 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 [14] RP FUNCTION. RX PubMed=12702877; DOI=10.1126/science.1081379; RA Morillon A., O'Sullivan J., Azad A., Proudfoot N., Mellor J.; RT "Regulation of elongating RNA polymerase II by forkhead transcription RT factors in yeast."; RL Science 300:492-495(2003). RN [15] RP FUNCTION. RX PubMed=17283050; DOI=10.1128/mcb.01798-06; RA Sherriff J.A., Kent N.A., Mellor J.; RT "The Isw2 chromatin-remodeling ATPase cooperates with the Fkh2 RT transcription factor to repress transcription of the B-type cyclin gene RT CLB2."; RL Mol. Cell. Biol. 27:2848-2860(2007). RN [16] RP IDENTIFICATION BY 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-832 AND SER-833, AND RP 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-708; SER-832 AND SER-833, 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). RN [19] RP FUNCTION, AND INTERACTION WITH ORC. RX PubMed=22265405; DOI=10.1016/j.cell.2011.12.012; RA Knott S.R., Peace J.M., Ostrow A.Z., Gan Y., Rex A.E., Viggiani C.J., RA Tavare S., Aparicio O.M.; RT "Forkhead transcription factors establish origin timing and long-range RT clustering in S. cerevisiae."; RL Cell 148:99-111(2012). RN [20] RP SUBCELLULAR LOCATION. RX PubMed=22932476; DOI=10.1186/2045-3701-2-30; RA Dastidar R.G., Hooda J., Shah A., Cao T.M., Henke R.M., Zhang L.; RT "The nuclear localization of SWI/SNF proteins is subjected to oxygen RT regulation."; RL Cell Biosci. 2:30-30(2012). RN [21] RP FUNCTION. RX PubMed=22438832; DOI=10.1371/journal.pgen.1002583; RA Postnikoff S.D., Malo M.E., Wong B., Harkness T.A.; RT "The yeast forkhead transcription factors fkh1 and fkh2 regulate lifespan RT and stress response together with the anaphase-promoting complex."; RL PLoS Genet. 8:e1002583-e1002583(2012). RN [22] RP FUNCTION, AND DNA-BINDING. RX PubMed=24504085; DOI=10.1371/journal.pone.0087647; RA Ostrow A.Z., Nellimoottil T., Knott S.R., Fox C.A., Tavare S., RA Aparicio O.M.; RT "Fkh1 and Fkh2 bind multiple chromosomal elements in the S. cerevisiae RT genome with distinct specificities and cell cycle dynamics."; RL PLoS ONE 9:e87647-e87647(2014). RN [23] RP FUNCTION. RX PubMed=26728715; DOI=10.1101/gr.196857.115; RA Peace J.M., Villwock S.K., Zeytounian J.L., Gan Y., Aparicio O.M.; RT "Quantitative BrdU immunoprecipitation method demonstrates that Fkh1 and RT Fkh2 are rate-limiting activators of replication origins that reprogram RT replication timing in G1 phase."; RL Genome Res. 26:365-375(2016). CC -!- FUNCTION: Transcription factor that regulates the expression of the CC CLB2 cluster of genes during the G2/M phase of the mitotic cell cycle CC (PubMed:10959837, PubMed:10894548, PubMed:10894549, PubMed:11562353, CC PubMed:12702877, PubMed:17283050, PubMed:24504085). The CLB2 cluster of CC genes includes mitotic regulators such as CLB1, CLB2, CDC5 and CDC20 as CC well as SWI5 and ACE2, transcription factors required for the CC subsequent temporal wave of cell cycle regulated gene expression in the CC M/G1 phase interval (PubMed:10959837, PubMed:10894548, CC PubMed:11562353). Involved in HMRa silencing (PubMed:10747051). FKH1 CC and FKH2 associate with the coding regions of active genes and CC influence, in opposing ways, transcriptional elongation and CC termination, and coordinate early transcription elongation and pre-mRNA CC processing (PubMed:12702877). Both FKH1 and FKH2 play a role as CC regulators of lifespan in collaboration with the anaphase-promoting CC complex (APC), likely through combined regulation of stress response, CC genomic stability, and cell cycle regulation (PubMed:22438832). FKH1 CC and FKH2 function also in controlling yeast cell morphology by CC preventing preudohyphal growth (PubMed:10747051, PubMed:10894548). Acts CC as a rate-limiting replication origin activator via its interaction CC with the origin recognition complex (ORC) (PubMed:22265405, CC PubMed:26728715). {ECO:0000269|PubMed:10747051, CC ECO:0000269|PubMed:10894548, ECO:0000269|PubMed:10894549, CC ECO:0000269|PubMed:10959837, ECO:0000269|PubMed:11562353, CC ECO:0000269|PubMed:12702877, ECO:0000269|PubMed:17283050, CC ECO:0000269|PubMed:22265405, ECO:0000269|PubMed:22438832, CC ECO:0000269|PubMed:24504085, ECO:0000269|PubMed:26728715}. CC -!- SUBUNIT: Interacts with MCM1 (PubMed:10959837). Interacts with NDD1 CC (PubMed:12865300). Interacts with the origin recognition complex (ORC) CC composed of ORC1 to ORC6 (PubMed:22265405). CC {ECO:0000269|PubMed:10959837, ECO:0000269|PubMed:12865300, CC ECO:0000269|PubMed:22265405}. CC -!- INTERACTION: CC P41813; P32562: CDC5; NbExp=2; IntAct=EBI-6973, EBI-4440; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22932476}. Cytoplasm, CC cytosol {ECO:0000269|PubMed:12702877}. Note=Relocalizes to the cytosol CC in response to hypoxia. {ECO:0000269|PubMed:12702877}. CC -!- DOMAIN: The FHA domain is necessary for the interaction with NDD1. CC {ECO:0000269|PubMed:12865300}. CC -!- DISRUPTION PHENOTYPE: Causes only a modest decline in CLB2 cluster CC genes expression, but this expression is abolished when both FKH1 and CC FKH2 are deleted (PubMed:10959837). Leads to a defect in silencing HMRa CC (PubMed:10747051). Causes a form of yeast pseudohyphal growth, when CC FKH2 is also deleted (PubMed:10747051). Affects cell-cycle progression CC and CLB2 mRNA expression (PubMed:10747051). CC {ECO:0000269|PubMed:10747051, ECO:0000269|PubMed:10959837}. CC -!- MISCELLANEOUS: Present with 656 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. 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; L38850; AAA60939.1; -; Genomic_DNA. DR EMBL; X86470; CAA60193.1; -; Genomic_DNA. DR EMBL; Z71343; CAA95941.1; -; Genomic_DNA. DR EMBL; Z71344; CAA95942.1; -; Genomic_DNA. DR EMBL; U12141; AAA99643.1; -; Genomic_DNA. DR EMBL; BK006947; DAA10477.1; -; Genomic_DNA. DR PIR; S53913; S53913. DR RefSeq; NP_014331.3; NM_001182906.3. DR AlphaFoldDB; P41813; -. DR SMR; P41813; -. DR BioGRID; 35755; 206. DR DIP; DIP-5944N; -. DR IntAct; P41813; 6. DR MINT; P41813; -. DR STRING; 4932.YNL068C; -. DR iPTMnet; P41813; -. DR MaxQB; P41813; -. DR PaxDb; 4932-YNL068C; -. DR PeptideAtlas; P41813; -. DR EnsemblFungi; YNL068C_mRNA; YNL068C; YNL068C. DR GeneID; 855656; -. DR KEGG; sce:YNL068C; -. DR AGR; SGD:S000005012; -. DR SGD; S000005012; FKH2. DR VEuPathDB; FungiDB:YNL068C; -. DR eggNOG; KOG2294; Eukaryota. DR GeneTree; ENSGT00940000173882; -. DR HOGENOM; CLU_007090_2_0_1; -. DR InParanoid; P41813; -. DR OMA; YYRFAKT; -. DR OrthoDB; 5385885at2759; -. DR BioCyc; YEAST:G3O-33098-MONOMER; -. DR BioGRID-ORCS; 855656; 2 hits in 13 CRISPR screens. DR PRO; PR:P41813; -. DR Proteomes; UP000002311; Chromosome XIV. DR RNAct; P41813; Protein. DR GO; GO:0005829; C:cytosol; IDA:SGD. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:0003682; F:chromatin binding; IDA:SGD. DR GO; GO:0003688; F:DNA replication origin binding; IDA:SGD. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IDA:SGD. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:SGD. DR GO; GO:0003713; F:transcription coactivator activity; IDA:SGD. DR GO; GO:0003712; F:transcription coregulator activity; IDA:SGD. DR GO; GO:0006338; P:chromatin remodeling; IMP:SGD. DR GO; GO:2000221; P:negative regulation of pseudohyphal growth; IMP:SGD. DR GO; GO:0061186; P:negative regulation of silent mating-type cassette heterochromatin formation; IMP:SGD. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:SGD. DR GO; GO:1903468; P:positive regulation of DNA replication initiation; IMP:SGD. DR GO; GO:0032298; P:positive regulation of DNA-templated DNA replication initiation; IMP:SGD. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD. DR GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IMP:SGD. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd00059; FH_FOX; 1. DR CDD; cd22701; FHA_FKH1-like; 1. DR Gene3D; 2.60.200.20; -; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR000253; FHA_dom. DR InterPro; IPR001766; Fork_head_dom. DR InterPro; IPR008984; SMAD_FHA_dom_sf. DR InterPro; IPR018122; TF_fork_head_CS_1. DR InterPro; IPR030456; TF_fork_head_CS_2. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR PANTHER; PTHR45881; CHECKPOINT SUPPRESSOR 1-LIKE, ISOFORM A-RELATED; 1. DR PANTHER; PTHR45881:SF1; FORK HEAD PROTEIN HOMOLOG 2; 1. DR Pfam; PF00498; FHA; 1. DR Pfam; PF00250; Forkhead; 1. DR PRINTS; PR00053; FORKHEAD. DR SMART; SM00339; FH; 1. DR SMART; SM00240; FHA; 1. DR SUPFAM; SSF49879; SMAD/FHA domain; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS50006; FHA_DOMAIN; 1. DR PROSITE; PS00657; FORK_HEAD_1; 1. DR PROSITE; PS00658; FORK_HEAD_2; 1. DR PROSITE; PS50039; FORK_HEAD_3; 1. PE 1: Evidence at protein level; KW Cytoplasm; DNA-binding; Nucleus; Phosphoprotein; Reference proteome; KW Transcription; Transcription regulation. FT CHAIN 1..862 FT /note="Fork head protein homolog 2" FT /id="PRO_0000091904" FT DOMAIN 83..152 FT /note="FHA" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086" FT DNA_BIND 339..430 FT /note="Fork-head" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089" FT REGION 498..528 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 611..663 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 698..731 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 750..846 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 500..528 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 706..731 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 750..792 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 808..824 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 825..845 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 708 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 832 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956, FT ECO:0007744|PubMed:19779198" FT MOD_RES 833 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956, FT ECO:0007744|PubMed:19779198" SQ SEQUENCE 862 AA; 94374 MW; 68A03F5EB7BB5CF3 CRC64; MSSSNFNEMN ELNMTQTNYG STKYTAQHHQ GVINAIISSL TAPDQPTTVS LQYSNDKNMA TEIQAYAKLS GPNWTYYVKD LEVSIGRNTD PLNSALQENS DGVKNSYRVN IDLGPAKVVS RKHAIIKYNM NIGGWELHIL GRNGAKVNFQ RTHNGPNNPP IRLSSGTLLD IGGTQMMFIL PDSDPVVAPI CIEHLMPNLI NMFGLEGNNN PLLRDIIKQS NYAKQRQLTS NQQIKGFKLY GSGGNAPFGS GANLGPSEQG IFNNNNNSKN KNGYFTSINP NYTASTTTSN TINPQAASPQ GPPNTIIAAN FVDSYKSSNA YPQALDFTSD LSHDENRNVK PPHSYATMIT QAILSSPEGV ISLADIYKYI SSNYAYYRFA KSGWQNSIRH NLSLNKAFEK VPRRPNEPGK GMKWRISESY QQEFLNKWNT GKVGKIRRGS SVARQLQLHM AKFNSLPMEM DYRLSLNMAQ PPKRQLQSHN VLEPSNNNII EGFVQHVPSK GNLPASQQSQ PPVSHQNQSQ QPPPQEQRQE IQFTFADTQN RNIALARPIK TPQLQAPNSN ANLNQNNMKE YKESLHPPAI SISQMNRQSP NNALVSFTNA CANSKIINNI SDSADKSTNN NGGTKMNLPA ISTSSLDENG NLEPTTTTSS GNSNSVPQTG TTTSSLAANS LRLSQPYDTL LRSPTKAFHI TAMEAYTPER GSANRARSPL HSNSNNTNNN GANNSNLQTS GMENKQTGLV LDSNVLKSME SNNDNRRLTP STSKSQNVKS SPGVWNLLQF SSTNNTPAAD SGGNKRGFSI NPDIKAKENE NATSEKDSDS NSNDLETKDI NSSPLKNQGG STANAKELIL DTDGAKISII NN //