HSF1_CAEEL
ID HSF1_CAEEL Reviewed; 671 AA.
AC G5EFT5; Q6Q4G5;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Heat shock transcription factor hsf-1 {ECO:0000303|PubMed:15611166};
GN Name=hsf-1 {ECO:0000312|WormBase:Y53C10A.12};
GN ORFNames=Y53C10A.12 {ECO:0000312|WormBase:Y53C10A.12};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:AAS72409.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, AND MUTAGENESIS OF
RP 585-TRP--VAL-671.
RX PubMed=15611166; DOI=10.1534/genetics.104.028423;
RA Hajdu-Cronin Y.M., Chen W.J., Sternberg P.W.;
RT "The L-type cyclin CYL-1 and the heat-shock-factor HSF-1 are required for
RT heat-shock-induced protein expression in Caenorhabditis elegans.";
RL Genetics 168:1937-1949(2004).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 585-TRP--VAL-671.
RX PubMed=16916933; DOI=10.1073/pnas.0604050103;
RA Singh V., Aballay A.;
RT "Heat-shock transcription factor (HSF)-1 pathway required for
RT Caenorhabditis elegans immunity.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:13092-13097(2006).
RN [4] {ECO:0000305}
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 585-TRP--VAL-671.
RX PubMed=18331616; DOI=10.1111/j.1474-9726.2008.00385.x;
RA Steinkraus K.A., Smith E.D., Davis C., Carr D., Pendergrass W.R.,
RA Sutphin G.L., Kennedy B.K., Kaeberlein M.;
RT "Dietary restriction suppresses proteotoxicity and enhances longevity by an
RT hsf-1-dependent mechanism in Caenorhabditis elegans.";
RL Aging Cell 7:394-404(2008).
RN [5] {ECO:0000305}
RP FUNCTION, SUBUNIT, IDENTIFICATION IN THE DHIC COMPLEX, INTERACTION WITH
RP DDL-1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND PHOSPHORYLATION.
RX PubMed=22265419; DOI=10.1016/j.cell.2011.12.019;
RA Chiang W.C., Ching T.T., Lee H.C., Mousigian C., Hsu A.L.;
RT "HSF-1 regulators DDL-1/2 link insulin-like signaling to heat-shock
RT responses and modulation of longevity.";
RL Cell 148:322-334(2012).
RN [6] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-145.
RX PubMed=23107491; DOI=10.1111/acel.12024;
RA Morton E.A., Lamitina T.;
RT "Caenorhabditis elegans HSF-1 is an essential nuclear protein that forms
RT stress granule-like structures following heat shock.";
RL Aging Cell 12:112-120(2013).
RN [7] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF 585-TRP--VAL-671.
RX PubMed=26759377; DOI=10.1042/bj20150938;
RA Joo H.J., Park S., Kim K.Y., Kim M.Y., Kim H., Park D., Paik Y.K.;
RT "HSF-1 is involved in regulation of ascaroside pheromone biosynthesis by
RT heat stress in Caenorhabditis elegans.";
RL Biochem. J. 473:789-796(2016).
RN [8] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF ARG-145 AND 585-TRP--VAL-671.
RX PubMed=26952214; DOI=10.7554/elife.12821;
RA Kinet M.J., Malin J.A., Abraham M.C., Blum E.S., Silverman M.R., Lu Y.,
RA Shaham S.;
RT "HSF-1 activates the ubiquitin proteasome system to promote non-apoptotic
RT developmental cell death in C. elegans.";
RL Elife 5:0-0(2016).
RN [9] {ECO:0000305}
RP FUNCTION.
RX PubMed=27688402; DOI=10.1101/gad.283317.116;
RA Li J., Chauve L., Phelps G., Brielmann R.M., Morimoto R.I.;
RT "E2F coregulates an essential HSF developmental program that is distinct
RT from the heat-shock response.";
RL Genes Dev. 30:2062-2075(2016).
RN [10] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28198373; DOI=10.1038/ncomms14337;
RA Kumsta C., Chang J.T., Schmalz J., Hansen M.;
RT "Hormetic heat stress and HSF-1 induce autophagy to improve survival and
RT proteostasis in C. elegans.";
RL Nat. Commun. 8:14337-14337(2017).
RN [11] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND SUMOYLATION.
RX PubMed=29036198; DOI=10.1371/journal.pgen.1007038;
RA Das R., Melo J.A., Thondamal M., Morton E.A., Cornwell A.B., Crick B.,
RA Kim J.H., Swartz E.W., Lamitina T., Douglas P.M., Samuelson A.V.;
RT "The homeodomain-interacting protein kinase HPK-1 preserves protein
RT homeostasis and longevity through master regulatory control of the HSF-1
RT chaperone network and TORC1-restricted autophagy in Caenorhabditis
RT elegans.";
RL PLoS Genet. 13:E1007038-E1007038(2017).
RN [12] {ECO:0000305}
RP FUNCTION.
RX PubMed=28837599; DOI=10.1371/journal.pone.0183445;
RA Brunquell J., Snyder A., Cheng F., Westerheide S.D.;
RT "HSF-1 is a regulator of miRNA expression in Caenorhabditis elegans.";
RL PLoS ONE 12:e0183445-e0183445(2017).
RN [13] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INDUCTION, PHOSPHORYLATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=29042483; DOI=10.1126/scisignal.aan4893;
RA Ooi F.K., Prahlad V.;
RT "Olfactory experience primes the heat shock transcription factor HSF-1 to
RT enhance the expression of molecular chaperones in C. elegans.";
RL Sci. Signal. 10:0-0(2017).
CC -!- FUNCTION: Functions as a stress-inducible and DNA-binding transcription
CC factor, playing a central role in the transcriptional activation of the
CC heat shock response (HSR), leading to the expression of a large class
CC of molecular chaperones, heat shock proteins (HSPs), that protect cells
CC from cellular insults' damage (PubMed:29042483, PubMed:15611166,
CC PubMed:22265419). Upon exposure to heat and other stress stimuli,
CC activates gene transcription through binding to site-specific heat
CC shock elements (HSEs) present in the promoter regions of target genes,
CC such as the HSPs (PubMed:29042483, PubMed:27688402, PubMed:15611166,
CC PubMed:22265419). Binds to inverted 5'-NGAAN-3' pentamer DNA sequences
CC in HSEs (PubMed:29042483, PubMed:27688402). Involved in positive
CC modulation of expression of heat shock protein hsp-16.2 in response to
CC heat shock; may act in concert with homeodomain-interacting protein
CC kinase hpk-1 (PubMed:15611166, PubMed:28198373, PubMed:29036198). In
CC response to heat shock or starvation, required for the modulation of
CC lifespan, and protection against aberrant protein aggregation
CC proteotoxicity; may act in parallel with the Insulin/IGF-1-like
CC signaling (IIS) mediated pathway (PubMed:15611166, PubMed:18331616,
CC PubMed:28198373, PubMed:29036198). Plays a role in modulating
CC autophagy, in response to a moderate and short-term heat shock, also
CC known as a hormetic heat shock (PubMed:28198373). Involved in positive
CC modulation of ascaroside pheromone biosynthesis in response to heat
CC shock, perhaps by directly activating transcription of peroxisomal
CC fatty acid beta-oxidation genes (PubMed:26759377). Required in
CC modulating the response to infection by either Gram-negative or Gram-
CC positive bacteria, perhaps acting via regulation of expression of
CC Hsp90/daf-21 and members of the small heat shock protein (HSP20) family
CC (PubMed:16916933, PubMed:29042483). May play a role downstream of the
CC daf-16/FOXO and daf-2 signaling pathway in response to bacterial
CC pathogens (PubMed:16916933). Modulates expression of multiple microRNA
CC genes, in both heat shock-dependent and -independent manner
CC (PubMed:28837599). Independent of heat shock, required to modulate
CC expression of genes involved in larval development, mainly distinct
CC from HSPs; acts in concert with putative transcription factor efl-
CC 1/E2F, which may form part of a multiprotein DRM complex
CC (PubMed:15611166, PubMed:27688402). Independent of heat shock, involved
CC in promoting death of the linker cell, a male-specific cell which
CC guides the elongation of the gonad; perhaps acting by modulating
CC expression of ubiquitin-conjugating enzyme let-70 (PubMed:26952214).
CC Plays a role in egg-laying (PubMed:15611166).
CC {ECO:0000269|PubMed:15611166, ECO:0000269|PubMed:16916933,
CC ECO:0000269|PubMed:18331616, ECO:0000269|PubMed:22265419,
CC ECO:0000269|PubMed:26759377, ECO:0000269|PubMed:26952214,
CC ECO:0000269|PubMed:27688402, ECO:0000269|PubMed:28198373,
CC ECO:0000269|PubMed:28837599, ECO:0000269|PubMed:29036198,
CC ECO:0000269|PubMed:29042483}.
CC -!- SUBUNIT: Forms homodimers and homotrimers (PubMed:29042483,
CC PubMed:22265419). Component of the DHIC (ddl-1-containing hsf-1
CC inhibitory complex), which contains at least ddl-1, ddl-2, hsb-1 and
CC hsf-1 (PubMed:22265419). Within the complex, interacts with ddl-1
CC (PubMed:22265419). Formation of the DHIC may be dependent upon the
CC Insulin/IGF-1-like signaling (IIS) mediated pathway (PubMed:22265419).
CC {ECO:0000269|PubMed:22265419, ECO:0000269|PubMed:29042483}.
CC -!- INTERACTION:
CC G5EFT5; O01901: ddl-1; NbExp=3; IntAct=EBI-2916699, EBI-323542;
CC G5EFT5; G5EFT5: hsf-1; NbExp=2; IntAct=EBI-2916699, EBI-2916699;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23107491}. Cytoplasm
CC {ECO:0000269|PubMed:22265419}. Note=Localizes constitutively to the
CC nucleus (PubMed:23107491, PubMed:29042483). Localization to the nucleus
CC enhanced by heat shock (PubMed:22265419). Localization to nucleus
CC inhibited by the Insulin/IGF-1-like signaling (IIS) mediated pathway
CC (PubMed:22265419). In response to heat shock, forms nuclear stress
CC granules (PubMed:23107491, PubMed:29036198). These structures are
CC dependent upon either heat shock, or can be induced by treatment with
CC sodium azide, which may act by inhibiting ATP production
CC (PubMed:23107491). DNA binding may promote localization to stress
CC granules (PubMed:23107491). Localization to stress granules partially
CC overlaps with sites of active transcription (PubMed:23107491). Other
CC stressors such as osmotic stress, heavy metals, or ethanol do not
CC induce localization to nuclear stress granules (PubMed:23107491).
CC {ECO:0000269|PubMed:22265419, ECO:0000269|PubMed:23107491,
CC ECO:0000269|PubMed:29036198, ECO:0000269|PubMed:29042483}.
CC -!- TISSUE SPECIFICITY: Expressed in intestinal cells, body wall muscle
CC cells, and hypodermal cells, as well as many neurons in the head and
CC tail. {ECO:0000269|PubMed:22265419}.
CC -!- INDUCTION: Induced by heat shock. {ECO:0000269|PubMed:15611166,
CC ECO:0000269|PubMed:29042483}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:22265419,
CC ECO:0000269|PubMed:29036198, ECO:0000269|PubMed:29042483}.
CC -!- PTM: Sumoylated (PubMed:29036198). Sumoylation may inhibit
CC transcriptional activity in response to heat shock (PubMed:29036198).
CC {ECO:0000269|PubMed:29036198}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown increases susceptibility
CC to Gram-negative bacterium P.aeruginosa in wild-type and in a daf-2
CC mutant background (PubMed:16916933). Abolishes both median and maximum
CC lifespan extension caused by starvation (PubMed:18331616). Fails to
CC prevent paralysis due to proteotoxicity under starvation conditions
CC (PubMed:18331616). Prevents the heat shock-induced increase in lgg-
CC 1/Atg8 punctae in body-wall muscles, nerve ring neurons and proximal
CC intestinal cells (PubMed:28198373). Accelerates death upon exposure to
CC the Gram-negative bacterium P.aeruginosa PA14 (PubMed:29042483).
CC {ECO:0000269|PubMed:16916933, ECO:0000269|PubMed:18331616,
CC ECO:0000269|PubMed:28198373, ECO:0000269|PubMed:29042483}.
CC -!- SIMILARITY: Belongs to the HSF 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; AY559747; AAS72409.1; -; mRNA.
DR EMBL; AY559748; AAS72410.1; -; mRNA.
DR EMBL; BX284601; CAA22146.1; -; Genomic_DNA.
DR PIR; T27125; T27125.
DR RefSeq; NP_493031.1; NM_060630.3.
DR AlphaFoldDB; G5EFT5; -.
DR SMR; G5EFT5; -.
DR ComplexPortal; CPX-4305; DHIC complex.
DR IntAct; G5EFT5; 2.
DR MINT; G5EFT5; -.
DR STRING; 6239.Y53C10A.12; -.
DR EPD; G5EFT5; -.
DR PaxDb; G5EFT5; -.
DR PeptideAtlas; G5EFT5; -.
DR EnsemblMetazoa; Y53C10A.12.1; Y53C10A.12.1; WBGene00002004.
DR EnsemblMetazoa; Y53C10A.12.2; Y53C10A.12.2; WBGene00002004.
DR GeneID; 173078; -.
DR KEGG; cel:CELE_Y53C10A.12; -.
DR CTD; 173078; -.
DR WormBase; Y53C10A.12; CE22380; WBGene00002004; hsf-1.
DR eggNOG; KOG0627; Eukaryota.
DR GeneTree; ENSGT00940000169930; -.
DR HOGENOM; CLU_026529_0_0_1; -.
DR InParanoid; G5EFT5; -.
DR OMA; SHPCFVQ; -.
DR OrthoDB; 1154048at2759; -.
DR Reactome; R-CEL-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-CEL-3371511; HSF1 activation.
DR Reactome; R-CEL-3371568; Attenuation phase.
DR Reactome; R-CEL-3371571; HSF1-dependent transactivation.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00002004; Expressed in embryo and 4 other tissues.
DR GO; GO:0000785; C:chromatin; IMP:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
DR GO; GO:0097165; C:nuclear stress granule; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0071203; C:WASH complex; IC:ComplexPortal.
DR GO; GO:0005516; F:calmodulin binding; IPI:WormBase.
DR GO; GO:0003682; F:chromatin binding; IMP:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:WormBase.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:WormBase.
DR GO; GO:1904070; P:ascaroside biosynthetic process; IMP:UniProtKB.
DR GO; GO:0040024; P:dauer larval development; IGI:WormBase.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
DR GO; GO:0045087; P:innate immune response; IMP:WormBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:1905911; P:positive regulation of dauer entry; IMP:UniProtKB.
DR GO; GO:0032000; P:positive regulation of fatty acid beta-oxidation; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0016239; P:positive regulation of macroautophagy; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0012501; P:programmed cell death; IGI:UniProtKB.
DR GO; GO:0010623; P:programmed cell death involved in cell development; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IMP:UniProtKB.
DR GO; GO:1990834; P:response to odorant; IMP:UniProtKB.
DR GO; GO:0035966; P:response to topologically incorrect protein; IMP:WormBase.
DR GO; GO:0007210; P:serotonin receptor signaling pathway; IMP:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000232; HSF_DNA-bd.
DR InterPro; IPR027725; HSF_fam.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10015; PTHR10015; 1.
DR Pfam; PF00447; HSF_DNA-bind; 1.
DR PRINTS; PR00056; HSFDOMAIN.
DR SMART; SM00415; HSF; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Stress response; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..671
FT /note="Heat shock transcription factor hsf-1"
FT /id="PRO_0000453732"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..196
FT /note="DNA-binding domain"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT REGION 329..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 206..240
FT /evidence="ECO:0000255"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 145
FT /note="R->A: Reduces formation of nuclear stress granules,
FT in response to heat shock. May reduce sequence-specific DNA
FT binding. Restores normal male gonadal linker cell death on
FT either egl-20/Wnt or bar-1/beta-catenin mutant
FT backgrounds."
FT /evidence="ECO:0000269|PubMed:23107491,
FT ECO:0000269|PubMed:26952214"
FT MUTAGEN 585..671
FT /note="Missing: In sy441; Egg-laying defects. Eggs cultured
FT at 25 degrees Celsius arrest development at the larval L2-
FT L3 stages, are pale and vacuolated, but distinct from dauer
FT larvae. Reduced life-span. Drastic reduction in induction
FT of expression of heat shock protein hsp-16.2 in response to
FT heat shock. Increased susceptibility to Gram-negative
FT bacterium P.aeruginosa. Starvation increases maximum, but
FT not median, lifespan. Inappropriate survival of male
FT gonadal linker cell, exacerbated in a ubiquitin-conjugating
FT enzyme let-70 mutant background. Significantly reduced
FT expression of let-70 and ubiquitin ubq-1. Ascaroside
FT pheromone biosynthesis is inhibited and extracts from
FT mutants induce a significantly decreased dauer formation
FT rate in wild-type L1 larvae."
FT /evidence="ECO:0000269|PubMed:15611166,
FT ECO:0000269|PubMed:16916933, ECO:0000269|PubMed:18331616,
FT ECO:0000269|PubMed:26759377, ECO:0000269|PubMed:26952214"
SQ SEQUENCE 671 AA; 75012 MW; CEFC67160982ACB1 CRC64;
MQPTGNQIQQ NQQQQQQLIM RVPKQEVSVS GAARRYVQQA PPNRPPRQNH QNGAIGGKKS
SVTIQEVPNN AYLETLNKSG NNKVDDDKLP VFLIKLWNIV EDPNLQSIVH WDDSGASFHI
SDPYLFGRNV LPHFFKHNNM NSMVRQLNMY GFRKMTPLSQ GGLTRTESDQ DHLEFSHPCF
VQGRPELLSQ IKRKQSARTV EDKQVNEQTQ QNLEVVMAEM RAMREKAKNM EDKMNKLTKE
NRDMWTQMGS MRQQHARQQQ YFKKLLHFLV SVMQPGLSKR VAKRGVLEID FCAANGTAGP
NSKRARMNSE EGPYKDVCDL LESLQRETQE PFSRRFTNNE GPLISEVTDE FGNSPVGRGS
AQDLFGDTFG AQSSRYSDGG ATSSREQSPH PIISQPQSNS AGAHGANEQK PDDMYMGSGP
LTHENIHRGI SALKRDYQGA SPASGGPSTS SSAPSGAGAG ARMAQKRAAP YKNATRQMAQ
PQQDYSGGFV NNYSGFMPSD PSMIPYQPSH QYLQPHQKLM AIEDQHHPTT STSSTNADPH
QNLYSPTLGL SPSFDRQLSQ ELQEYFTGTD TSLESFRDLV SNHNWDDFGN NVPLDDDEEG
SEDPLRQLAL ENAPETSNYD GAEDLLFDNE QQYPENGFDV PDPNYLPLAD EEIFPHSPAL
RTPSPSDPNL V
