HAS1_YEAST
ID HAS1_YEAST Reviewed; 505 AA.
AC Q03532; D6W0B7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=ATP-dependent RNA helicase HAS1;
DE EC=3.6.4.13;
DE AltName: Full=Helicase associated with SET1 protein 1;
GN Name=HAS1; OrderedLocusNames=YMR290C;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 SET1 DEPENDENT EXPRESSION.
RX PubMed=9398665; DOI=10.1091/mbc.8.12.2421;
RA Nislow C., Ray E., Pillus L.;
RT "SET1, a yeast member of the Trithorax family, functions in transcriptional
RT silencing and diverse cellular processes.";
RL Mol. Biol. Cell 8:2421-2436(1997).
RN [4]
RP SUBCELLULAR LOCATION, AND ASSOCIATION WITH NUCLEAR PORE.
RX PubMed=10684247; DOI=10.1083/jcb.148.4.635;
RA Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y., Chait B.T.;
RT "The yeast nuclear pore complex: composition, architecture, and transport
RT mechanism.";
RL J. Cell Biol. 148:635-651(2000).
RN [5]
RP PHOSPHORYLATION.
RX PubMed=14574415; DOI=10.1038/nature02062;
RA Ubersax J.A., Woodbury E.L., Quang P.N., Paraz M., Blethrow J.D., Shah K.,
RA Shokat K.M., Morgan D.O.;
RT "Targets of the cyclin-dependent kinase Cdk1.";
RL Nature 425:859-864(2003).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-92; HIS-105; PRO-315
RP AND PHE-393.
RX PubMed=15049817; DOI=10.1111/j.1365-2958.2003.03973.x;
RA Emery B., de la Cruz J., Rocak S., Deloche O., Linder P.;
RT "Has1p, a member of the DEAD-box family, is required for 40S ribosomal
RT subunit biogenesis in Saccharomyces cerevisiae.";
RL Mol. Microbiol. 52:141-158(2004).
RN [7]
RP FUNCTION.
RX PubMed=15242642; DOI=10.1016/j.cell.2004.06.013;
RA Mnaimneh S., Davierwala A.P., Haynes J., Moffat J., Peng W.-T., Zhang W.,
RA Yang X., Pootoolal J., Chua G., Lopez A., Trochesset M., Morse D.,
RA Krogan N.J., Hiley S.L., Li Z., Morris Q., Grigull J., Mitsakakis N.,
RA Roberts C.J., Greenblatt J.F., Boone C., Kaiser C.A., Andrews B.J.,
RA Hughes T.R.;
RT "Exploration of essential gene functions via titratable promoter alleles.";
RL Cell 118:31-44(2004).
RN [8]
RP INTERACTION WITH RRP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15100437; DOI=10.1261/rna.5255804;
RA Horsey E.W., Jakovljevic J., Miles T.D., Harnpicharnchai P.,
RA Woolford J.L. Jr.;
RT "Role of the yeast Rrp1 protein in the dynamics of pre-ribosome
RT maturation.";
RL RNA 10:813-827(2004).
RN [9]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF LYS-92;
RP SER-228; THR-230; HIS-375; ARG-376 AND LYS-389.
RX PubMed=15718299; DOI=10.1093/nar/gki244;
RA Rocak S., Emery B., Tanner N.K., Linder P.;
RT "Characterization of the ATPase and unwinding activities of the yeast DEAD-
RT box protein Has1p and the analysis of the roles of the conserved motifs.";
RL Nucleic Acids Res. 33:999-1009(2005).
RN [10]
RP INTERACTION WITH RRP15, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15769876; DOI=10.1261/rna.7200205;
RA De Marchis M.L., Giorgi A., Schinina M.E., Bozzoni I., Fatica A.;
RT "Rrp15p, a novel component of pre-ribosomal particles required for 60S
RT ribosome subunit maturation.";
RL RNA 11:495-502(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, 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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION BY
RP 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: ATP-dependent RNA helicase involved in 40S ribosomal subunit
CC biogenesis. Required for the processing and cleavage of 35S pre-rRNA at
CC sites A0, A1, and A2, leading to mature 18S rRNA.
CC {ECO:0000269|PubMed:15049817, ECO:0000269|PubMed:15242642,
CC ECO:0000269|PubMed:15718299}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=450 uM for ATP {ECO:0000269|PubMed:15718299};
CC pH dependence:
CC Optimum pH is 6.5. Active from pH 5 to 8.
CC {ECO:0000269|PubMed:15718299};
CC -!- SUBUNIT: Interacts with RRP1. Associates in the nucleolus with the 60S
CC and pre-60S ribosomal subunits. It has also been isolated with the
CC nuclear pore complex. {ECO:0000269|PubMed:15100437,
CC ECO:0000269|PubMed:15769876}.
CC -!- INTERACTION:
CC Q03532; Q12389: DBP10; NbExp=4; IntAct=EBI-8170, EBI-5644;
CC Q03532; Q04660: ERB1; NbExp=5; IntAct=EBI-8170, EBI-28098;
CC Q03532; P53743: ESF2; NbExp=2; IntAct=EBI-8170, EBI-28537;
CC Q03532; Q03532: HAS1; NbExp=3; IntAct=EBI-8170, EBI-8170;
CC Q03532; P20448: HCA4; NbExp=3; IntAct=EBI-8170, EBI-5612;
CC Q03532; P43586: LOC1; NbExp=5; IntAct=EBI-8170, EBI-22906;
CC Q03532; Q12176: MAK21; NbExp=3; IntAct=EBI-8170, EBI-10944;
CC Q03532; P38112: MAK5; NbExp=4; IntAct=EBI-8170, EBI-10394;
CC Q03532; P47083: MPP10; NbExp=3; IntAct=EBI-8170, EBI-11168;
CC Q03532; P39744: NOC2; NbExp=3; IntAct=EBI-8170, EBI-29259;
CC Q03532; Q02892: NOG1; NbExp=2; IntAct=EBI-8170, EBI-12105;
CC Q03532; P53927: NOP15; NbExp=4; IntAct=EBI-8170, EBI-28853;
CC Q03532; P37838: NOP4; NbExp=4; IntAct=EBI-8170, EBI-12122;
CC Q03532; P40078: NSA2; NbExp=3; IntAct=EBI-8170, EBI-22681;
CC Q03532; P40693: RLP7; NbExp=3; IntAct=EBI-8170, EBI-15415;
CC Q03532; Q12481: RRP36; NbExp=2; IntAct=EBI-8170, EBI-31770;
CC Q03532; Q12136: SAS10; NbExp=2; IntAct=EBI-8170, EBI-36084;
CC Q03532; P53866: SQS1; NbExp=3; IntAct=EBI-8170, EBI-29168;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10684247,
CC ECO:0000269|PubMed:15049817}.
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC -!- PTM: Phosphorylated by CDK1. {ECO:0000305|PubMed:14574415}.
CC -!- MISCELLANEOUS: Transcription depends partially on SET1.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX18/HAS1
CC subfamily. {ECO:0000305}.
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DR EMBL; X80836; CAA56799.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10191.1; -; Genomic_DNA.
DR PIR; S47451; S47451.
DR RefSeq; NP_014017.1; NM_001182797.1.
DR PDB; 5Z3G; EM; 3.65 A; Y=1-505.
DR PDB; 6C0F; EM; 3.70 A; p=1-505.
DR PDB; 6CB1; EM; 4.60 A; p=1-505.
DR PDB; 6ELZ; EM; 3.30 A; D=1-505.
DR PDB; 6EM1; EM; 3.60 A; D=1-505.
DR PDB; 6EM3; EM; 3.20 A; D=1-505.
DR PDB; 6EM4; EM; 4.10 A; D=1-505.
DR PDB; 6EM5; EM; 4.30 A; D=1-505.
DR PDB; 7OHP; EM; 3.90 A; D=1-505.
DR PDB; 7OHR; EM; 4.72 A; D=1-505.
DR PDB; 7OHS; EM; 4.38 A; D=1-505.
DR PDB; 7OHV; EM; 3.90 A; D=1-505.
DR PDB; 7OHW; EM; 3.50 A; D=1-505.
DR PDB; 7OHX; EM; 3.30 A; D=1-505.
DR PDBsum; 5Z3G; -.
DR PDBsum; 6C0F; -.
DR PDBsum; 6CB1; -.
DR PDBsum; 6ELZ; -.
DR PDBsum; 6EM1; -.
DR PDBsum; 6EM3; -.
DR PDBsum; 6EM4; -.
DR PDBsum; 6EM5; -.
DR PDBsum; 7OHP; -.
DR PDBsum; 7OHR; -.
DR PDBsum; 7OHS; -.
DR PDBsum; 7OHV; -.
DR PDBsum; 7OHW; -.
DR PDBsum; 7OHX; -.
DR AlphaFoldDB; Q03532; -.
DR SMR; Q03532; -.
DR BioGRID; 35470; 379.
DR ComplexPortal; CPX-1604; Small ribosomal subunit processome, variant 1.
DR ComplexPortal; CPX-1607; Small ribosomal subunit processome, variant 2.
DR ComplexPortal; CPX-1608; Small ribosomal subunit processome, variant 3.
DR DIP; DIP-4396N; -.
DR IntAct; Q03532; 68.
DR MINT; Q03532; -.
DR STRING; 4932.YMR290C; -.
DR iPTMnet; Q03532; -.
DR MaxQB; Q03532; -.
DR PaxDb; Q03532; -.
DR PRIDE; Q03532; -.
DR EnsemblFungi; YMR290C_mRNA; YMR290C; YMR290C.
DR GeneID; 855335; -.
DR KEGG; sce:YMR290C; -.
DR SGD; S000004903; HAS1.
DR VEuPathDB; FungiDB:YMR290C; -.
DR eggNOG; KOG0342; Eukaryota.
DR GeneTree; ENSGT00680000100037; -.
DR HOGENOM; CLU_003041_26_5_1; -.
DR InParanoid; Q03532; -.
DR OMA; EYEFPAN; -.
DR BioCyc; YEAST:G3O-32960-MON; -.
DR SABIO-RK; Q03532; -.
DR PRO; PR:Q03532; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03532; protein.
DR GO; GO:0030686; C:90S preribosome; HDA:SGD.
DR GO; GO:0005635; C:nuclear envelope; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IDA:SGD.
DR GO; GO:0032040; C:small-subunit processome; IPI:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008186; F:ATP-dependent activity, acting on RNA; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0003724; F:RNA helicase activity; IDA:SGD.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IC:ComplexPortal.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:SGD.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:SGD.
DR GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR GO; GO:1990417; P:snoRNA release from pre-rRNA; IMP:SGD.
DR CDD; cd17942; DEADc_DDX18; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR044773; DDX18/Has1_DEADc.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR025313; DUF4217.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF13959; DUF4217; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01178; DUF4217; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Helicase; Hydrolase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Ribosome biogenesis;
KW RNA-binding; rRNA processing.
FT CHAIN 1..505
FT /note="ATP-dependent RNA helicase HAS1"
FT /id="PRO_0000055046"
FT DOMAIN 73..249
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 263..433
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 42..70
FT /note="Q motif"
FT MOTIF 196..199
FT /note="DEAD box"
FT MOTIF 275..291
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000305"
FT COMPBIAS 9..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 86..93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 92
FT /note="K->A: Lethal in vivo and impairs ATPase with 2-5% of
FT wild-type ATPase activity, a 20-fold higher KM for ATP and
FT unables RNA/DNA heteroduplexes unwinding activity in vitro.
FT Leads to 13% of wild-type ATPase activity and higher
FT RNA/DNA heteroduplexes unwinding activity in vitro; when
FT associated with A-389."
FT /evidence="ECO:0000269|PubMed:15049817,
FT ECO:0000269|PubMed:15718299"
FT MUTAGEN 105
FT /note="H->Y: Decreases the amount of 40S ribosomal subunits
FT at 37 degrees Celsius; when associated with S-315 and S-
FT 393."
FT /evidence="ECO:0000269|PubMed:15049817"
FT MUTAGEN 228
FT /note="S->A: Slow growth at 18 and 16 degrees Celsius, no
FT growth at 14 degrees Celsius and drastic decrease of the
FT amount of 40S ribosomal subunits at 30 degrees Celsius in
FT vivo. Leads to 70-80% of wild-type ATPase activity, a 2-
FT fold lower KM for ATP and a slightly reduced RNA/DNA
FT heteroduplexes unwinding activity in vitro."
FT /evidence="ECO:0000269|PubMed:15718299"
FT MUTAGEN 230
FT /note="T->A: Lethal in vivo and leads to 70-80% of wild-
FT type ATPase activity, a 2-fold lower KM for ATP and a
FT reduced RNA/DNA heteroduplexes unwinding activity in
FT vitro."
FT /evidence="ECO:0000269|PubMed:15718299"
FT MUTAGEN 315
FT /note="P->S: Decreases the amount of 40S ribosomal subunits
FT at 37 degrees Celsius; when associated with Y-105 and S-
FT 393."
FT /evidence="ECO:0000269|PubMed:15049817"
FT MUTAGEN 375
FT /note="H->E: Lethal in vivo and leads to 70-80% of wild-
FT type ATPase activity, a 2-fold lower KM for ATP and a
FT reduced RNA/DNA heteroduplexes unwinding activity in
FT vitro."
FT /evidence="ECO:0000269|PubMed:15718299"
FT MUTAGEN 376
FT /note="R->A: Lethal in vivo and leads to less than 30% of
FT wild-type ATPase activity and a 2-fold lower KM for ATP in
FT vitro."
FT /evidence="ECO:0000269|PubMed:15718299"
FT MUTAGEN 389
FT /note="K->A: Increases 3-fold the ATPase activity and a
FT higher RNA/DNA heteroduplexes unwinding activity in vitro.
FT Leads to 13% of wild-type ATPase activity and lower RNA/DNA
FT heteroduplexes unwinding activity in vitro; when associated
FT with A-92."
FT /evidence="ECO:0000269|PubMed:15718299"
FT MUTAGEN 393
FT /note="F->S: Decreases the amount of 40S ribosomal subunits
FT at 37 degrees Celsius; when associated with Y-105 and S-
FT 315."
FT /evidence="ECO:0000269|PubMed:15049817"
FT HELIX 276..286
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 292..297
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 301..309
FT /evidence="ECO:0007829|PDB:6EM3"
FT TURN 310..313
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 325..336
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 342..346
FT /evidence="ECO:0007829|PDB:6EM3"
FT TURN 347..352
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 360..363
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:6EM3"
FT TURN 371..377
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 426..432
FT /evidence="ECO:0007829|PDB:6EM3"
FT TURN 433..435
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 438..455
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 460..464
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 468..474
FT /evidence="ECO:0007829|PDB:6EM3"
SQ SEQUENCE 505 AA; 56717 MW; EE15D51A7F6BE1A2 CRC64;
MATPSNKRSR DSESTEEPVV DEKSTSKQNN AAPEGEQTTC VEKFEELKLS QPTLKAIEKM
GFTTMTSVQA RTIPPLLAGR DVLGAAKTGS GKTLAFLIPA IELLHSLKFK PRNGTGIIVI
TPTRELALQI FGVARELMEF HSQTFGIVIG GANRRQEAEK LMKGVNMLIA TPGRLLDHLQ
NTKGFVFKNL KALIIDEADR ILEIGFEDEM RQIIKILPNE DRQSMLFSAT QTTKVEDLAR
ISLRPGPLFI NVVPETDNST ADGLEQGYVV CDSDKRFLLL FSFLKRNQKK KIIVFLSSCN
SVKYYAELLN YIDLPVLELH GKQKQQKRTN TFFEFCNAER GILICTDVAA RGLDIPAVDW
IIQFDPPDDP RDYIHRVGRT ARGTKGKGKS LMFLTPNELG FLRYLKASKV PLNEYEFPEN
KIANVQSQLE KLIKSNYYLH QTAKDGYRSY LQAYASHSLK TVYQIDKLDL AKVAKSYGFP
VPPKVNITIG ASGKTPNTKR RKTHK
