BDF1_YEAST
ID BDF1_YEAST Reviewed; 686 AA.
AC P35817; D6VZ34; Q06048;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 3.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Bromodomain-containing factor 1;
GN Name=BDF1; OrderedLocusNames=YLR399C; ORFNames=L8084.18;
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], AND FUNCTION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7816623; DOI=10.1093/nar/22.24.5332;
RA Lygerou Z., Conesa C., Lesage P., Swanson R.N., Ruet A., Carlson M.,
RA Sentenac A., Seraphin B.;
RT "The yeast BDF1 gene encodes a transcription factor involved in the
RT expression of a broad class of genes including snRNAs.";
RL Nucleic Acids Res. 22:5332-5340(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=7791775; DOI=10.1128/mcb.15.7.3685;
RA Chua P., Roeder G.S.;
RT "Bdf1, a yeast chromosomal protein required for sporulation.";
RL Mol. Cell. Biol. 15:3685-3696(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 [MRNA] OF 471-686.
RX PubMed=8321235; DOI=10.1128/mcb.13.7.4331-4341.1993;
RA Widner W.R., Wickner R.B.;
RT "Evidence that the SKI antiviral system of Saccharomyces cerevisiae acts by
RT blocking expression of viral mRNA.";
RL Mol. Cell. Biol. 13:4331-4341(1993).
RN [6]
RP DOMAIN BROMODOMAIN.
RX PubMed=9175470; DOI=10.1016/s0968-0004(97)01042-6;
RA Jeanmougin F., Wurtz J.-M., Le Douarin B., Chambon P., Losson R.;
RT "The bromodomain revisited.";
RL Trends Biochem. Sci. 22:151-153(1997).
RN [7]
RP FUNCTION, AND INTERACTION WITH TAF7.
RX PubMed=10783167;
RA Matangkasombut O., Buratowski R.M., Swilling N.W., Buratowski S.;
RT "Bromodomain factor 1 corresponds to a missing piece of yeast TFIID.";
RL Genes Dev. 14:951-962(2000).
RN [8]
RP INTERACTION WITH HISTONES H3 AND H4.
RX PubMed=11343701; DOI=10.1016/s0014-5793(01)02397-3;
RA Pamblanco M., Poveda A., Sendra R., Rodriguez-Navarro S., Perez-Ortin J.E.,
RA Tordera V.;
RT "Bromodomain factor 1 (Bdf1) protein interacts with histones.";
RL FEBS Lett. 496:31-35(2001).
RN [9]
RP FUNCTION.
RX PubMed=12482937; DOI=10.1073/pnas.262669299;
RA Chang M., Bellaoui M., Boone C., Brown G.W.;
RT "A genome-wide screen for methyl methanesulfonate-sensitive mutants reveals
RT genes required for S phase progression in the presence of DNA damage.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16934-16939(2002).
RN [10]
RP FUNCTION, AND INTERACTION WITH HISTONES H3 AND H4.
RX PubMed=12620224; DOI=10.1016/s1097-2765(03)00033-9;
RA Matangkasombut O., Buratowski S.;
RT "Different sensitivities of bromodomain factors 1 and 2 to histone H4
RT acetylation.";
RL Mol. Cell 11:353-363(2003).
RN [11]
RP FUNCTION, INTERACTION WITH ACETYLATED HISTONES H3 AND H4, AND MUTAGENESIS
RP OF TYR-187 AND TYR-354.
RX PubMed=12620225; DOI=10.1016/s1097-2765(03)00035-2;
RA Ladurner A.G., Inouye C., Jain R., Tjian R.;
RT "Bromodomains mediate an acetyl-histone encoded antisilencing function at
RT heterochromatin boundaries.";
RL Mol. Cell 11:365-376(2003).
RN [12]
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 [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=15225549; DOI=10.1016/j.molcel.2004.05.022;
RA Martinez-Campa C., Politis P., Moreau J.-L., Kent N., Goodall J.,
RA Mellor J., Goding C.R.;
RT "Precise nucleosome positioning and the TATA box dictate requirements for
RT the histone H4 tail and the bromodomain factor Bdf1.";
RL Mol. Cell 15:69-81(2004).
RN [15]
RP PHOSPHORYLATION BY THE CK2 PROTEIN KINASE COMPLEX.
RX PubMed=15143168; DOI=10.1128/mcb.24.11.4734-4742.2004;
RA Sawa C., Nedea E., Krogan N., Wada T., Handa H., Greenblatt J.,
RA Buratowski S.;
RT "Bromodomain factor 1 (Bdf1) is phosphorylated by protein kinase CK2.";
RL Mol. Cell. Biol. 24:4734-4742(2004).
RN [16]
RP FUNCTION.
RX PubMed=15255905; DOI=10.1111/j.1365-2958.2004.04184.x;
RA Bianchi M.M., Costanzo G., Chelstowska A., Grabowska D., Mazzoni C.,
RA Piccinni E., Cavalli A., Ciceroni F., Rytka J., Slonimski P.P.,
RA Frontali L., Negri R.;
RT "The bromodomain-containing protein Bdf1p acts as a phenotypic and
RT transcriptional multicopy suppressor of YAF9 deletion in yeast.";
RL Mol. Microbiol. 53:953-968(2004).
RN [17]
RP DISRUPTION PHENOTYPE.
RX PubMed=16079223; DOI=10.1534/genetics.105.046938;
RA Jambunathan N., Martinez A.W., Robert E.C., Agochukwu N.B., Ibos M.E.,
RA Dugas S.L., Donze D.;
RT "Multiple bromodomain genes are involved in restricting the spread of
RT heterochromatic silencing at the Saccharomyces cerevisiae HMR-tRNA
RT boundary.";
RL Genetics 171:913-922(2005).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270 AND SER-429, AND
RP IDENTIFICATION BY 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 [20]
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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-615 AND SER-659, 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270; SER-429 AND SER-615, 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: Transcription factor involved in the expression of a broad
CC class of genes including snRNAs. Required for sporulation and DNA-
CC damage repair. Prevents the spreading of SIR silencing at telomeres and
CC protects histone H4, but not H3, from deacetylation.
CC {ECO:0000269|PubMed:10783167, ECO:0000269|PubMed:12482937,
CC ECO:0000269|PubMed:12620224, ECO:0000269|PubMed:12620225,
CC ECO:0000269|PubMed:15225549, ECO:0000269|PubMed:15255905,
CC ECO:0000269|PubMed:7791775, ECO:0000269|PubMed:7816623}.
CC -!- SUBUNIT: Interacts with the TFIID subunit TAF7 and with acetylated
CC histones H3 and H4. {ECO:0000269|PubMed:10783167,
CC ECO:0000269|PubMed:11343701, ECO:0000269|PubMed:12620224,
CC ECO:0000269|PubMed:12620225}.
CC -!- INTERACTION:
CC P35817; Q07442: BDF2; NbExp=5; IntAct=EBI-3493, EBI-37620;
CC P35817; P61830: HHT2; NbExp=2; IntAct=EBI-3493, EBI-8098;
CC P35817; Q12692: HTZ1; NbExp=5; IntAct=EBI-3493, EBI-8080;
CC P35817; Q05471: SWR1; NbExp=3; IntAct=EBI-3493, EBI-22102;
CC P35817; P46677: TAF1; NbExp=3; IntAct=EBI-3493, EBI-18855;
CC P35817; Q03761: TAF12; NbExp=2; IntAct=EBI-3493, EBI-35097;
CC P35817; P53040: TAF6; NbExp=2; IntAct=EBI-3493, EBI-18876;
CC P35817; Q05021: TAF7; NbExp=5; IntAct=EBI-3493, EBI-27490;
CC P35817; Q03433: VPS71; NbExp=2; IntAct=EBI-3493, EBI-27814;
CC P35817; P53930: YAF9; NbExp=3; IntAct=EBI-3493, EBI-28841;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:7791775}.
CC -!- PTM: Phosphorylated by the casein kinase CK2 complex.
CC {ECO:0000269|PubMed:15143168}.
CC -!- DISRUPTION PHENOTYPE: Heterochromatin spreading downstream of the
CC silent mating-type locus HMR. {ECO:0000269|PubMed:16079223}.
CC -!- MISCELLANEOUS: Present with 8100 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z18944; CAA79377.1; -; Genomic_DNA.
DR EMBL; U18116; AAA89115.1; -; Genomic_DNA.
DR EMBL; U19729; AAB82357.1; -; Genomic_DNA.
DR EMBL; L13469; AAA35048.1; -; mRNA.
DR EMBL; BK006945; DAA09700.1; -; Genomic_DNA.
DR PIR; S55955; S55955.
DR RefSeq; NP_013503.1; NM_001182287.1.
DR AlphaFoldDB; P35817; -.
DR SMR; P35817; -.
DR BioGRID; 31658; 368.
DR ComplexPortal; CPX-2122; Swr1 chromatin remodelling complex.
DR DIP; DIP-1624N; -.
DR IntAct; P35817; 30.
DR MINT; P35817; -.
DR STRING; 4932.YLR399C; -.
DR iPTMnet; P35817; -.
DR MaxQB; P35817; -.
DR PaxDb; P35817; -.
DR PRIDE; P35817; -.
DR EnsemblFungi; YLR399C_mRNA; YLR399C; YLR399C.
DR GeneID; 851115; -.
DR KEGG; sce:YLR399C; -.
DR SGD; S000004391; BDF1.
DR VEuPathDB; FungiDB:YLR399C; -.
DR eggNOG; KOG1474; Eukaryota.
DR GeneTree; ENSGT00940000176400; -.
DR HOGENOM; CLU_001499_4_0_1; -.
DR InParanoid; P35817; -.
DR OMA; CYAFNPD; -.
DR BioCyc; YEAST:G3O-32463-MON; -.
DR PRO; PR:P35817; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P35817; protein.
DR GO; GO:0000785; C:chromatin; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000812; C:Swr1 complex; IDA:SGD.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0070577; F:lysine-acetylated histone binding; IDA:SGD.
DR GO; GO:0001094; F:TFIID-class transcription factor complex binding; IDA:SGD.
DR GO; GO:0006338; P:chromatin remodeling; IPI:SGD.
DR GO; GO:0006281; P:DNA repair; IMP:SGD.
DR GO; GO:0031452; P:negative regulation of heterochromatin assembly; IMP:SGD.
DR GO; GO:1900051; P:positive regulation of histone exchange; IMP:SGD.
DR GO; GO:0090054; P:regulation of silent mating-type cassette heterochromatin assembly; IMP:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0009301; P:snRNA transcription; IMP:SGD.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1270.220; -; 1.
DR Gene3D; 1.20.920.10; -; 2.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR027353; NET_dom.
DR InterPro; IPR038336; NET_sf.
DR Pfam; PF17035; BET; 1.
DR Pfam; PF00439; Bromodomain; 2.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 2.
DR SUPFAM; SSF47370; SSF47370; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 2.
DR PROSITE; PS50014; BROMODOMAIN_2; 2.
DR PROSITE; PS51525; NET; 1.
PE 1: Evidence at protein level;
KW Bromodomain; Coiled coil; DNA damage; DNA repair; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Sporulation; Transcription;
KW Transcription regulation.
FT CHAIN 1..686
FT /note="Bromodomain-containing factor 1"
FT /id="PRO_0000211176"
FT DOMAIN 165..237
FT /note="Bromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 332..404
FT /note="Bromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 518..598
FT /note="NET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00857"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 460..499
FT /evidence="ECO:0000255"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..144
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..447
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..508
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 615
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 659
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 187
FT /note="Y->F: Impairs interaction with histones H3 and H4;
FT when associated with F-354."
FT /evidence="ECO:0000269|PubMed:12620225"
FT MUTAGEN 354
FT /note="Y->F: Impairs interaction with histones H3 and H4;
FT when associated with F-187."
FT /evidence="ECO:0000269|PubMed:12620225"
FT CONFLICT 8
FT /note="Q -> LC (in Ref. 1; CAA79377)"
FT /evidence="ECO:0000305"
FT CONFLICT 93..94
FT /note="GA -> R (in Ref. 2; AAA89115)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="A -> P (in Ref. 1; CAA79377)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="A -> P (in Ref. 1; CAA79377)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="D -> E (in Ref. 1; CAA79377)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="A -> R (in Ref. 5; AAA35048)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 686 AA; 76978 MW; 8CCD52F41F91D0DA CRC64;
MTDITPVQND VDVNGNNVND DVSSNLKRPI DQGDPSNGLA EEENPANNQL HLKKARLDGD
ALTSSPAGLA ENGIEGATLA ANGENGYNAT GSGAEDEQQG LKKEEGGQGT KQEDLDENSK
QELPMEVPKE PAPAPPPEPD MNNLPQNPIP KHQQKHALLA IKAVKRLKDA RPFLQPVDPV
KLDIPFYFNY IKRPMDLSTI ERKLNVGAYE VPEQITEDFN LMVNNSIKFN GPNAGISQMA
RNIQASFEKH MLNMPAKDAP PVIAKGRRSS AQEDAPIVIR RAQTHNGRPK RTIHPPKSKD
IYPYESKKPK SKRLQQAMKF CQSVLKELMA KKHASYNYPF LEPVDPVSMN LPTYFDYVKE
PMDLGTIAKK LNDWQYQTME DFERDVRLVF KNCYTFNPDG TIVNMMGHRL EEVFNSKWAD
RPNLDDYDSD EDSRTQGDYD DYESEYSESD IDETIITNPA IQYLEEQLAR MKVELQQLKK
QELEKIRKER RLARGSKKRG KRSKGRSGSK NASSKGRRDK KNKLKTVVTY DMKRIITERI
NDLPTSKLER AIDIIKKSMP NISEDDEVEL DLDTLDNHTI LTLYNTFFRQ YESSSGASNG
LDGTSGVTRD ASSLSPTSAG SRKRRSKALS QEEQSRQIEK IKNKLAILDS ASPLSQNGSP
GQIQSAAHNG FSSSSDDDVS SESEEE
