FKH2_YEAST
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 03-AUG-2022, entry version 188.
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 interactin with
CC 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}.
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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; 200.
DR DIP; DIP-5944N; -.
DR IntAct; P41813; 6.
DR MINT; P41813; -.
DR STRING; 4932.YNL068C; -.
DR iPTMnet; P41813; -.
DR MaxQB; P41813; -.
DR PaxDb; P41813; -.
DR PRIDE; P41813; -.
DR EnsemblFungi; YNL068C_mRNA; YNL068C; YNL068C.
DR GeneID; 855656; -.
DR KEGG; sce:YNL068C; -.
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 BioCyc; YEAST:G3O-33098-MON; -.
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 assembly; IMP:SGD.
DR GO; GO:0071930; P:negative regulation of transcription involved in G1/S transition of mitotic cell cycle; IGI:SGD.
DR GO; GO:0090419; P:negative regulation of transcription involved in G2/M transition of mitotic cell cycle; 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:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IMP:SGD.
DR GO; GO:0090282; P:positive regulation of transcription involved in G2/M transition of mitotic cell cycle; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00059; FH; 1.
DR CDD; cd00060; FHA; 1.
DR Gene3D; 1.10.10.10; -; 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 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; SSF46785; SSF46785; 1.
DR SUPFAM; SSF49879; SSF49879; 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
