DAF11_CAEEL
ID DAF11_CAEEL Reviewed; 1077 AA.
AC Q8I4N4;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Receptor-type guanylate cyclase daf-11 {ECO:0000305|PubMed:10790386};
DE EC=4.6.1.2 {ECO:0000269|PubMed:24015261};
DE AltName: Full=Abnormal dauer formation protein 11 {ECO:0000312|WormBase:B0240.3a};
DE Flags: Precursor;
GN Name=daf-11 {ECO:0000312|WormBase:B0240.3a};
GN ORFNames=B0240.3 {ECO:0000312|WormBase:B0240.3a};
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|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 [2] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF GLY-806 AND SER-866.
RX PubMed=1732156; DOI=10.1093/genetics/130.1.105;
RA Vowels J.J., Thomas J.H.;
RT "Genetic analysis of chemosensory control of dauer formation in
RT Caenorhabditis elegans.";
RL Genetics 130:105-123(1992).
RN [3] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF GLY-806 AND SER-866.
RX PubMed=7828815; DOI=10.1093/genetics/138.2.303;
RA Vowels J.J., Thomas J.H.;
RT "Multiple chemosensory defects in daf-11 and daf-21 mutants of
RT Caenorhabditis elegans.";
RL Genetics 138:303-316(1994).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=8893028; DOI=10.1016/s0896-6273(00)80203-2;
RA Schackwitz W.S., Inoue T., Thomas J.H.;
RT "Chemosensory neurons function in parallel to mediate a pheromone response
RT in C. elegans.";
RL Neuron 17:719-728(1996).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=9486798; DOI=10.1242/dev.125.2.249;
RA Coburn C.M., Mori I., Ohshima Y., Bargmann C.I.;
RT "A cyclic nucleotide-gated channel inhibits sensory axon outgrowth in
RT larval and adult Caenorhabditis elegans: a distinct pathway for maintenance
RT of sensory axon structure.";
RL Development 125:249-258(1998).
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=10571181; DOI=10.1016/s0092-8674(00)81525-1;
RA Troemel E.R., Sagasti A., Bargmann C.I.;
RT "Lateral signaling mediated by axon contact and calcium entry regulates
RT asymmetric odorant receptor expression in C. elegans.";
RL Cell 99:387-398(1999).
RN [7] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP GLY-806; SER-866 AND GLY-867.
RX PubMed=10790386; DOI=10.1093/genetics/155.1.85;
RA Birnby D.A., Link E.M., Vowels J.J., Tian H., Colacurcio P.L., Thomas J.H.;
RT "A transmembrane guanylyl cyclase (DAF-11) and Hsp90 (DAF-21) regulate a
RT common set of chemosensory behaviors in Caenorhabditis elegans.";
RL Genetics 155:85-104(2000).
RN [8] {ECO:0000305}
RP FUNCTION.
RX PubMed=11677050; DOI=10.1016/s0925-4773(01)00507-x;
RA Murakami M., Koga M., Ohshima Y.;
RT "DAF-7/TGF-beta expression required for the normal larval development in C.
RT elegans is controlled by a presumed guanylyl cyclase DAF-11.";
RL Mech. Dev. 109:27-35(2001).
RN [9] {ECO:0000305}
RP FUNCTION.
RX PubMed=18316030; DOI=10.1016/j.cmet.2008.01.005;
RA You Y.J., Kim J., Raizen D.M., Avery L.;
RT "Insulin, cGMP, and TGF-beta signals regulate food intake and quiescence in
RT C. elegans: a model for satiety.";
RL Cell Metab. 7:249-257(2008).
RN [10] {ECO:0000305}
RP FUNCTION.
RX PubMed=19489741; DOI=10.1111/j.1474-9726.2009.00495.x;
RA Hahm J.H., Kim S., Paik Y.K.;
RT "Endogenous cGMP regulates adult longevity via the insulin signaling
RT pathway in Caenorhabditis elegans.";
RL Aging Cell 8:473-483(2009).
RN [11] {ECO:0000305}
RP FUNCTION.
RX PubMed=20436480; DOI=10.1038/nn.2540;
RA Liu J., Ward A., Gao J., Dong Y., Nishio N., Inada H., Kang L., Yu Y.,
RA Ma D., Xu T., Mori I., Xie Z., Xu X.Z.;
RT "C. elegans phototransduction requires a G protein-dependent cGMP pathway
RT and a taste receptor homolog.";
RL Nat. Neurosci. 13:715-722(2010).
RN [12] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=21124868; DOI=10.1371/journal.pgen.1001199;
RA Jensen V.L., Bialas N.J., Bishop-Hurley S.L., Molday L.L., Kida K.,
RA Nguyen P.A., Blacque O.E., Molday R.S., Leroux M.R., Riddle D.L.;
RT "Localization of a guanylyl cyclase to chemosensory cilia requires the
RT novel ciliary MYND domain protein DAF-25.";
RL PLoS Genet. 6:E1001199-E1001199(2010).
RN [13] {ECO:0000305}
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24015261; DOI=10.1371/journal.pone.0072569;
RA Beckert U., Aw W.Y., Burhenne H., Forsterling L., Kaever V., Timmons L.,
RA Seifert R.;
RT "The receptor-bound guanylyl cyclase DAF-11 is the mediator of hydrogen
RT peroxide-induced cGMP increase in Caenorhabditis elegans.";
RL PLoS ONE 8:E72569-E72569(2013).
RN [14] {ECO:0000305}
RP FUNCTION.
RX PubMed=25303524; DOI=10.1016/j.cell.2014.09.011;
RA Meisel J.D., Panda O., Mahanti P., Schroeder F.C., Kim D.H.;
RT "Chemosensation of bacterial secondary metabolites modulates neuroendocrine
RT signaling and behavior of C. elegans.";
RL Cell 159:267-280(2014).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25009271; DOI=10.1523/jneurosci.0012-14.2014;
RA Harris G., Shen Y., Ha H., Donato A., Wallis S., Zhang X., Zhang Y.;
RT "Dissecting the signaling mechanisms underlying recognition and preference
RT of food odors.";
RL J. Neurosci. 34:9389-9403(2014).
RN [16]
RP FUNCTION, AND MUTAGENESIS OF ASP-770.
RX PubMed=21304598; DOI=10.1371/journal.pone.0016561;
RA Fierro-Gonzalez J.C., Cornils A., Alcedo J., Miranda-Vizuete A.,
RA Swoboda P.;
RT "The thioredoxin TRX-1 modulates the function of the insulin-like
RT neuropeptide DAF-28 during dauer formation in Caenorhabditis elegans.";
RL PLoS ONE 6:E16561-E16561(2011).
RN [17]
RP FUNCTION, AND MUTAGENESIS OF 723-ARG--MET-739.
RX PubMed=30014846; DOI=10.7554/elife.36833;
RA Hao Y., Yang W., Ren J., Hall Q., Zhang Y., Kaplan J.M.;
RT "Thioredoxin shapes the C. elegans sensory response to Pseudomonas produced
RT nitric oxide.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: Guanylate cyclase involved in the production of the second
CC messenger cGMP (PubMed:24015261). In addition, regulates cGMP levels by
CC controlling the transcription of 3',5'-cyclic phosphodiesterase pde-1
CC and pde-5 mRNAs (PubMed:19489741, PubMed:24015261). Involved in the
CC olfactory, light and pheromone sensing pathways. Part of the
CC chemosensory mechanism of the ASJ sensory neuron that controls dauer
CC formation and dauer recovery (PubMed:1732156, PubMed:8893028,
CC PubMed:21304598). Promotes the calcium flux in ASJ sensory neurons in
CC response to onset and removal of a nitric oxide (NO) stimulus and is
CC thereby required for the behavioral avoidance response to NO-producing
CC organisms like P.aeruginosa (PubMed:30014846). In ASI and ASJ sensory
CC neurons, controls dauer formation and behavioral response to
CC P.aeruginosa by up-regulating the transcription of daf-7, a member of
CC the TGF-beta family (PubMed:11677050, PubMed:25303524). Required for
CC the chemotaxis responses to non-volatile and volatile attractants
CC mediated by the sensory neurons ASE and AWC respectively
CC (PubMed:7828815, PubMed:10790386). Required in ASJ neurons for
CC phototransduction downstream of G protein coupled-photoreceptor lite-1
CC (PubMed:20436480). Plays a role in the development of ASJ sensory
CC neuron axons during late larval stages and in the maintenance of normal
CC axon morphology in adults (PubMed:9486798). Required to maintain the
CC expression of putative olfactory receptor str-2 in one of the two AWC
CC neurons in adults (PubMed:10571181). Regulates, via the production of
CC cGMP, lifespan (in some environmental conditions), sensitivity to
CC oxidative stress and entry into quiescence triggered by satiety
CC (PubMed:18316030, PubMed:19489741, PubMed:24015261). In AWB and AWC
CC sensory neurons, mediates the recognition of food odors which
CC subsequently allows for the detection of preferred food sources
CC (PubMed:25009271). {ECO:0000269|PubMed:10571181,
CC ECO:0000269|PubMed:10790386, ECO:0000269|PubMed:11677050,
CC ECO:0000269|PubMed:1732156, ECO:0000269|PubMed:18316030,
CC ECO:0000269|PubMed:19489741, ECO:0000269|PubMed:20436480,
CC ECO:0000269|PubMed:21304598, ECO:0000269|PubMed:24015261,
CC ECO:0000269|PubMed:25009271, ECO:0000269|PubMed:25303524,
CC ECO:0000269|PubMed:30014846, ECO:0000269|PubMed:7828815,
CC ECO:0000269|PubMed:8893028, ECO:0000269|PubMed:9486798}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2;
CC Evidence={ECO:0000269|PubMed:24015261};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. Cell projection, dendrite
CC {ECO:0000269|PubMed:10790386}. Cell projection, cilium
CC {ECO:0000269|PubMed:10790386}. Perikaryon
CC {ECO:0000269|PubMed:10790386}. Note=Expressed preferentially in
CC ciliated endings of sensory neurons (PubMed:10790386). Cilium
CC localization is regulated by daf-25 (PubMed:21124868).
CC {ECO:0000269|PubMed:10790386, ECO:0000269|PubMed:21124868}.
CC -!- TISSUE SPECIFICITY: Expressed in sensory neurons including ASI, ASJ,
CC ASK, AWB and AWC. Expressed in ASJ neurons in the dauer stage.
CC {ECO:0000269|PubMed:10790386}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in AWB and AWC sensory
CC neurons results in a defective preference between different food odors.
CC {ECO:0000269|PubMed:25009271}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR EMBL; BX284605; CAD56284.3; -; Genomic_DNA.
DR RefSeq; NP_505960.3; NM_073559.5.
DR AlphaFoldDB; Q8I4N4; -.
DR SMR; Q8I4N4; -.
DR STRING; 6239.B0240.3; -.
DR PaxDb; Q8I4N4; -.
DR EnsemblMetazoa; B0240.3a.1; B0240.3a.1; WBGene00000907.
DR GeneID; 179605; -.
DR KEGG; cel:CELE_B0240.3; -.
DR UCSC; B0240.3; c. elegans.
DR CTD; 179605; -.
DR WormBase; B0240.3a; CE42996; WBGene00000907; daf-11.
DR eggNOG; KOG1023; Eukaryota.
DR HOGENOM; CLU_001072_1_3_1; -.
DR InParanoid; Q8I4N4; -.
DR OMA; DSHWIVK; -.
DR OrthoDB; 222371at2759; -.
DR PhylomeDB; Q8I4N4; -.
DR PRO; PR:Q8I4N4; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00000907; Expressed in pharyngeal muscle cell (C elegans) and 2 other tissues.
DR ExpressionAtlas; Q8I4N4; baseline and differential.
DR GO; GO:0030425; C:dendrite; IDA:WormBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0097730; C:non-motile cilium; IDA:WormBase.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004383; F:guanylate cyclase activity; ISS:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001653; F:peptide receptor activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0001306; P:age-dependent response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0071321; P:cellular response to cGMP; IMP:UniProtKB.
DR GO; GO:0006182; P:cGMP biosynthetic process; ISS:WormBase.
DR GO; GO:0006935; P:chemotaxis; IGI:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IGI:UniProtKB.
DR GO; GO:0040024; P:dauer larval development; IMP:WormBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0061067; P:negative regulation of dauer larval development; IMP:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0008355; P:olfactory learning; IMP:WormBase.
DR GO; GO:0007602; P:phototransduction; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IMP:WormBase.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; IMP:UniProtKB.
DR GO; GO:0030516; P:regulation of axon extension; IMP:WormBase.
DR GO; GO:0050920; P:regulation of chemotaxis; IMP:UniProtKB.
DR GO; GO:0061065; P:regulation of dauer larval development; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IGI:UniProtKB.
DR GO; GO:0042542; P:response to hydrogen peroxide; IMP:UniProtKB.
DR GO; GO:0019236; P:response to pheromone; IEA:UniProtKB-KW.
DR GO; GO:0009266; P:response to temperature stimulus; IMP:UniProtKB.
DR GO; GO:0007608; P:sensory perception of smell; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IMP:UniProtKB.
DR CDD; cd07302; CHD; 1.
DR Gene3D; 3.30.70.1230; -; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; cGMP biosynthesis; Chemotaxis; Coiled coil;
KW Glycoprotein; GTP-binding; Lyase; Magnesium; Membrane; Metal-binding;
KW Neurogenesis; Nucleotide-binding; Olfaction; Pheromone response;
KW Reference proteome; Sensory transduction; Signal; Transcription;
KW Transcription regulation; Transmembrane; Transmembrane helix.
FT SIGNAL 1..?
FT /evidence="ECO:0000305"
FT CHAIN ?..1077
FT /note="Receptor-type guanylate cyclase daf-11"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433297"
FT TOPO_DOM ?..334
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..1077
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 355..695
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 765..895
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 1048..1077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 983..1034
FT /evidence="ECO:0000255"
FT BINDING 770
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 770
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 771
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 814
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 814
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT CARBOHYD 14
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 723..739
FT /note="RTAELEKEQEKGDQLLM->EVGRI: In nu629; abolishes the
FT calcium flux to the cytoplasm in the ASJ sensory neurons in
FT response to the addition and removal of a nitric oxide
FT stimulus."
FT /evidence="ECO:0000269|PubMed:30014846"
FT MUTAGEN 770
FT /note="D->N: In ks67; constitutive dauer formation at 25
FT degrees Celsius."
FT /evidence="ECO:0000269|PubMed:21304598"
FT MUTAGEN 806
FT /note="G->E: In m84; constitutive dauer formation with mild
FT defect in dauer recovery. Mild inhibition of chemotaxis
FT responses to some volatile attractants."
FT /evidence="ECO:0000269|PubMed:10790386,
FT ECO:0000269|PubMed:1732156, ECO:0000269|PubMed:7828815"
FT MUTAGEN 866
FT /note="S->F: In m87; temperature sensitive constitutive
FT dauer formation with severe defect in dauer recovery. Loss
FT of chemotaxis responses to non-volatile and some volatile
FT attractants."
FT /evidence="ECO:0000269|PubMed:10790386,
FT ECO:0000269|PubMed:1732156, ECO:0000269|PubMed:7828815"
FT MUTAGEN 867
FT /note="G->R: In p169; temperature sensitive constitutive
FT dauer formation with severe defect in dauer recovery."
FT /evidence="ECO:0000269|PubMed:10790386"
SQ SEQUENCE 1077 AA; 121866 MW; 7DDD48C3F8101F37 CRC64;
MGPTCSSNFL RFANLTAEMQ SLEINILKGY PYEHPTMIDM VTRSPQNLAQ NLVSLLRGFE
WGQVGAVLCE ECYEGDELAS EIYFSTIEDI FENNNIALKE TVRIGKRENS VNISDAITIF
EPSARVILLF LGNKLNDYTE FMTAMSMNNY TTEEYTPVIV ISKNSLELTF PWKENDAIAE
LFDKAIIVYN NCYDKSKISS FLSSYSFSTI EETIISLQMY EGYHLLGYYL YTAITNTTLF
NYVQPEKAIS SMSIPGPFGE IFINSNGQRI AGYDVLVVDK SLNSNNFIMP LGTISTDKKC
PDQACLNFVL NSTSSFEPLK DVPLCGFHGE ICDQTGVIIA IAVIMGVLLM FIIILTTIRK
CCNGSKGRSI SNPWVIPFQD VRFIDLTNTE GSQHMSIQSL QRNMEEKQRL QSLARTKHIA
TVDQVYVLAD KYVMRDKLRY DKIDINLLYQ MKSHLQHDNL NSFVGITIDK ASHMYIIWNQ
CFRGSLHDHI FTKERQRGTA TRFEGLFLRD ILKGLEYIHA SAIDFHGNLT LHNCMLDSHW
IVKLSGFGVN RLLVKWKTSG QIFTEDHTPV IKSEELHYFD PAMKKIWKNY ADRNERALIT
PQFGKKCDMY SFGVILHEII LKKKFVEQLF DSPREEDDSV LIDDENDAIA SRFPLPIIIP
EGIEMHNDLI KMLENCFGSV RPDIALARKI IDTVLKMSGS LVDLMIKNLT AYTQGLNETV
KNRTAELEKE QEKGDQLLME LLPKSVANDL KNGIAVDPKV YENATILYSD IVGFTSLCSQ
SQPMEVVTLL SGMYQRFDLI ISQQGGYKME TIGDAYCVAA GLPVVMEKDH VKSICMIALL
QRDCLHHFEI PHRPGTFLNC RWGFNSGPVF AGVIGQKAPR YACFGEAVIL ASKMESSGVE
DRIQMTLASQ QLLEENFPQF VCSNRGGRTI EGIGRILTYW LEGVNAGEQV KVVEFQNDLN
DELSRIMKKD GELLAAATAL KPKDKMTLAK EKVIAERKNE EERLQRQQTL QEALEEHEEE
IEMNEVLVDE DEGEGKPKEV DLTSIVSTQM EELEDEPAGR TIGHGRLDSQ ASTIPDN
