CNGB3_HUMAN
ID CNGB3_HUMAN Reviewed; 809 AA.
AC Q9NQW8; C9JA51; Q9NRE9;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Cyclic nucleotide-gated cation channel beta-3;
DE AltName: Full=Cone photoreceptor cGMP-gated channel subunit beta;
DE AltName: Full=Cyclic nucleotide-gated cation channel modulatory subunit;
DE AltName: Full=Cyclic nucleotide-gated channel beta-3;
DE Short=CNG channel beta-3;
GN Name=CNGB3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT ACHM3
RP PHE-435, AND VARIANTS TRP-234; PRO-298 AND GLY-755.
RX PubMed=10958649; DOI=10.1093/hmg/9.14.2107;
RA Kohl S., Baumann B., Broghammer M., Jaegle H., Sieving P., Kellner U.,
RA Spegal R., Anastasi M., Zrenner E., Sharpe L.T., Wissinger B.;
RT "Mutations in the CNGB3 gene encoding the beta-subunit of the cone
RT photoreceptor cGMP-gated channel are responsible for achromatopsia (ACHM3)
RT linked to chromosome 8Q21.";
RL Hum. Mol. Genet. 9:2107-2116(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 114-809 (ISOFORM 2), FUNCTION, SUBUNIT, AND
RP VARIANT ACHM3 PHE-435.
RC TISSUE=Retina;
RX PubMed=10888875; DOI=10.1038/77162;
RA Sundin O.H., Yang J.-M., Li Y., Zhu D., Hurd J.N., Mitchell T.N.,
RA Silva E.D., Maumenee I.H.;
RT "Genetic basis of total colourblindness among the Pingelapese islanders.";
RL Nat. Genet. 25:289-293(2000).
RN [4]
RP SUBUNIT.
RX PubMed=21878911; DOI=10.1038/ncomms1466;
RA Shuart N.G., Haitin Y., Camp S.S., Black K.D., Zagotta W.N.;
RT "Molecular mechanism for 3:1 subunit stoichiometry of rod cyclic
RT nucleotide-gated ion channels.";
RL Nat. Commun. 2:457-457(2011).
RN [5]
RP VARIANT ACHM3 GLU-148.
RX PubMed=12357335; DOI=10.1038/sj.ejhg.5200856;
RA Rojas C.V., Maria L.S., Santos J.L., Cortes F., Alliende M.A.;
RT "A frameshift insertion in the cone cyclic nucleotide gated cation channel
RT causes complete achromatopsia in a consanguineous family from a rural
RT isolate.";
RL Eur. J. Hum. Genet. 10:638-642(2002).
RN [6]
RP VARIANTS ACHM3 VAL-307 AND ASN-525.
RX PubMed=14757870; DOI=10.1136/jmg.2003.011437;
RA Johnson S., Michaelides M., Aligianis I.A., Ainsworth J.R., Mollon J.D.,
RA Maher E.R., Moore A.T., Hunt D.M.;
RT "Achromatopsia caused by novel mutations in both CNGA3 and CNGB3.";
RL J. Med. Genet. 41:E20-E20(2004).
RN [7]
RP VARIANTS ACHM3 PHE-156; LEU-309; PHE-435 AND 720-GLN--LYS-726 DEL.
RX PubMed=15657609; DOI=10.1038/sj.ejhg.5201269;
RA Kohl S., Varsanyi B., Antunes G.A., Baumann B., Hoyng C.B., Jaegle H.,
RA Rosenberg T., Kellner U., Lorenz B., Salati R., Jurklies B., Farkas A.,
RA Andreasson S., Weleber R.G., Jacobson S.G., Rudolph G., Castellan C.,
RA Dollfus H., Legius E., Anastasi M., Bitoun P., Lev D., Sieving P.A.,
RA Munier F.L., Zrenner E., Sharpe L.T., Cremers F.P.M., Wissinger B.;
RT "CNGB3 mutations account for 50% of all cases with autosomal recessive
RT achromatopsia.";
RL Eur. J. Hum. Genet. 13:302-308(2005).
RN [8]
RP VARIANT MACULAR DEGENERATION GLN-403, VARIANT STGD1 ASP-469, VARIANTS ACHM3
RP ARG-107; LYS-199; THR-466; ASN-494; TYR-513; CYS-558; PHE-595 AND PRO-672,
RP AND VARIANTS HIS-25; SER-27; GLN-203; PRO-298; VAL-307 AND GLY-755.
RX PubMed=15712225; DOI=10.1002/humu.20142;
RA Nishiguchi K.M., Sandberg M.A., Gorji N., Berson E.L., Dryja T.P.;
RT "Cone cGMP-gated channel mutations and clinical findings in patients with
RT achromatopsia, macular degeneration, and other hereditary cone diseases.";
RL Hum. Mutat. 25:248-258(2005).
CC -!- FUNCTION: Visual signal transduction is mediated by a G-protein coupled
CC cascade using cGMP as second messenger. This protein can be activated
CC by cGMP which leads to an opening of the cation channel and thereby
CC causing a depolarization of rod photoreceptors. Induced a flickering
CC channel gating, weakened the outward rectification in the presence of
CC extracellular calcium, increased sensitivity for L-cis diltiazem and
CC enhanced the cAMP efficiency of the channel when coexpressed with CNGA3
CC (By similarity). Essential for the generation of light-evoked
CC electrical responses in the red-, green- and blue sensitive cones.
CC {ECO:0000250, ECO:0000269|PubMed:10888875}.
CC -!- SUBUNIT: Tetramer formed of three CNGA3 and one CNGB3 modulatory
CC subunits. {ECO:0000269|PubMed:10888875, ECO:0000269|PubMed:21878911}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NQW8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NQW8-2; Sequence=VSP_009742;
CC -!- TISSUE SPECIFICITY: Expressed specifically in the retina.
CC {ECO:0000269|PubMed:10958649}.
CC -!- DISEASE: Stargardt disease 1 (STGD1) [MIM:248200]: A common hereditary
CC macular degeneration. It is characterized by decreased central vision,
CC atrophy of the macula and underlying retinal pigment epithelium, and
CC frequent presence of prominent flecks in the posterior pole of the
CC retina. {ECO:0000269|PubMed:15712225}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Achromatopsia 3 (ACHM3) [MIM:262300]: An autosomal recessive,
CC ocular stationary disorder due to the absence of functioning cone
CC photoreceptors in the retina. It is characterized by total
CC colorblindness, low visual acuity, photophobia and nystagmus.
CC Achromatopsia type 3 patients manifest severe myopia.
CC {ECO:0000269|PubMed:10888875, ECO:0000269|PubMed:10958649,
CC ECO:0000269|PubMed:12357335, ECO:0000269|PubMed:14757870,
CC ECO:0000269|PubMed:15657609, ECO:0000269|PubMed:15712225}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel (TC
CC 1.A.1.5) family. CNGB3 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF80179.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF272900; AAF86274.1; -; mRNA.
DR EMBL; AC013751; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090572; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF228520; AAF80179.1; ALT_INIT; mRNA.
DR CCDS; CCDS6244.1; -. [Q9NQW8-1]
DR RefSeq; NP_061971.3; NM_019098.4. [Q9NQW8-1]
DR PDB; 7RHS; EM; 2.93 A; D=2-809.
DR PDBsum; 7RHS; -.
DR AlphaFoldDB; Q9NQW8; -.
DR SMR; Q9NQW8; -.
DR BioGRID; 120106; 4.
DR IntAct; Q9NQW8; 2.
DR MINT; Q9NQW8; -.
DR STRING; 9606.ENSP00000316605; -.
DR TCDB; 1.A.1.5.37; the voltage-gated ion channel (vic) superfamily.
DR GlyGen; Q9NQW8; 1 site.
DR iPTMnet; Q9NQW8; -.
DR PhosphoSitePlus; Q9NQW8; -.
DR BioMuta; CNGB3; -.
DR DMDM; 311033366; -.
DR jPOST; Q9NQW8; -.
DR MassIVE; Q9NQW8; -.
DR PaxDb; Q9NQW8; -.
DR PeptideAtlas; Q9NQW8; -.
DR PRIDE; Q9NQW8; -.
DR ProteomicsDB; 82213; -. [Q9NQW8-1]
DR ProteomicsDB; 82214; -. [Q9NQW8-2]
DR Antibodypedia; 59091; 122 antibodies from 24 providers.
DR DNASU; 54714; -.
DR Ensembl; ENST00000320005.6; ENSP00000316605.5; ENSG00000170289.13. [Q9NQW8-1]
DR GeneID; 54714; -.
DR KEGG; hsa:54714; -.
DR MANE-Select; ENST00000320005.6; ENSP00000316605.5; NM_019098.5; NP_061971.3.
DR UCSC; uc003ydx.3; human. [Q9NQW8-1]
DR CTD; 54714; -.
DR DisGeNET; 54714; -.
DR GeneCards; CNGB3; -.
DR GeneReviews; CNGB3; -.
DR HGNC; HGNC:2153; CNGB3.
DR HPA; ENSG00000170289; Tissue enhanced (bone marrow, retina).
DR MalaCards; CNGB3; -.
DR MIM; 248200; phenotype.
DR MIM; 262300; phenotype.
DR MIM; 605080; gene.
DR neXtProt; NX_Q9NQW8; -.
DR OpenTargets; ENSG00000170289; -.
DR Orphanet; 49382; Achromatopsia.
DR Orphanet; 1871; Progressive cone dystrophy.
DR Orphanet; 827; Stargardt disease.
DR PharmGKB; PA26663; -.
DR VEuPathDB; HostDB:ENSG00000170289; -.
DR eggNOG; KOG0499; Eukaryota.
DR GeneTree; ENSGT00940000154824; -.
DR HOGENOM; CLU_005746_11_1_1; -.
DR InParanoid; Q9NQW8; -.
DR OMA; RTWFEYT; -.
DR OrthoDB; 1073751at2759; -.
DR PhylomeDB; Q9NQW8; -.
DR TreeFam; TF318250; -.
DR PathwayCommons; Q9NQW8; -.
DR SignaLink; Q9NQW8; -.
DR BioGRID-ORCS; 54714; 9 hits in 1058 CRISPR screens.
DR ChiTaRS; CNGB3; human.
DR GeneWiki; Cyclic_nucleotide_gated_channel_beta_3; -.
DR GenomeRNAi; 54714; -.
DR Pharos; Q9NQW8; Tchem.
DR PRO; PR:Q9NQW8; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9NQW8; protein.
DR Bgee; ENSG00000170289; Expressed in pigmented layer of retina and 126 other tissues.
DR ExpressionAtlas; Q9NQW8; baseline and differential.
DR Genevisible; Q9NQW8; HS.
DR GO; GO:0017071; C:intracellular cyclic nucleotide activated cation channel complex; IBA:GO_Central.
DR GO; GO:0001750; C:photoreceptor outer segment; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:1902495; C:transmembrane transporter complex; IDA:UniProtKB.
DR GO; GO:0030553; F:cGMP binding; IDA:UniProtKB.
DR GO; GO:0005222; F:intracellular cAMP-activated cation channel activity; IBA:GO_Central.
DR GO; GO:0005223; F:intracellular cGMP-activated cation channel activity; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IBA:GO_Central.
DR GO; GO:0098655; P:cation transmembrane transport; IBA:GO_Central.
DR GO; GO:0006812; P:cation transport; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; NAS:ProtInc.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR032943; CNG6.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR45638:SF8; PTHR45638:SF8; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR PROSITE; PS00888; CNMP_BINDING_1; 1.
DR PROSITE; PS00889; CNMP_BINDING_2; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; cGMP; cGMP-binding; Disease variant;
KW Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
KW Membrane; Nucleotide-binding; Reference proteome; Sensory transduction;
KW Stargardt disease; Transmembrane; Transmembrane helix; Transport; Vision.
FT CHAIN 1..809
FT /note="Cyclic nucleotide-gated cation channel beta-3"
FT /id="PRO_0000219320"
FT TOPO_DOM 1..216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical; Name=H1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..250
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical; Name=H2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical; Name=H3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..359
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..380
FT /note="Helical; Name=H4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 381..417
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical; Name=H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 439..504
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 505..525
FT /note="Helical; Name=H6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 526..809
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..754
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 532..676
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000250"
FT BINDING 592
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000250"
FT BINDING 604
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000250"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 590..594
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10888875"
FT /id="VSP_009742"
FT VARIANT 25
FT /note="R -> H (in dbSNP:rs141098074)"
FT /evidence="ECO:0000269|PubMed:15712225"
FT /id="VAR_047606"
FT VARIANT 27
FT /note="N -> S (in dbSNP:rs35807406)"
FT /evidence="ECO:0000269|PubMed:15712225"
FT /id="VAR_047607"
FT VARIANT 107
FT /note="G -> R (in ACHM3; unknown pathological significance;
FT dbSNP:rs146688972)"
FT /evidence="ECO:0000269|PubMed:15712225"
FT /id="VAR_047608"
FT VARIANT 148
FT /note="K -> E (in ACHM3; dbSNP:rs369138501)"
FT /evidence="ECO:0000269|PubMed:12357335"
FT /id="VAR_047609"
FT VARIANT 156
FT /note="S -> F (in ACHM3; dbSNP:rs139207764)"
FT /evidence="ECO:0000269|PubMed:15657609"
FT /id="VAR_047610"
FT VARIANT 199
FT /note="E -> K (in ACHM3; unknown pathological significance;
FT dbSNP:rs114305748)"
FT /evidence="ECO:0000269|PubMed:15712225"
FT /id="VAR_047611"
FT VARIANT 203
FT /note="R -> Q (in dbSNP:rs16916632)"
FT /evidence="ECO:0000269|PubMed:15712225"
FT /id="VAR_025524"
FT VARIANT 234
FT /note="C -> W (in dbSNP:rs6471482)"
FT /evidence="ECO:0000269|PubMed:10958649"
FT /id="VAR_018109"
FT VARIANT 298
FT /note="T -> P (in dbSNP:rs4961206)"
FT /evidence="ECO:0000269|PubMed:10958649,
FT ECO:0000269|PubMed:15712225"
FT /id="VAR_018110"
FT VARIANT 307
FT /note="I -> V (in dbSNP:rs13265557)"
FT /evidence="ECO:0000269|PubMed:14757870,
FT ECO:0000269|PubMed:15712225"
FT /id="VAR_024418"
FT VARIANT 309
FT /note="P -> L (in ACHM3; dbSNP:rs1554612145)"
FT /evidence="ECO:0000269|PubMed:15657609"
FT /id="VAR_047612"
FT VARIANT 403
FT /note="R -> Q (found in macular degeneration; unknown
FT pathological significance; dbSNP:rs147876778)"
FT /evidence="ECO:0000269|PubMed:15712225"
FT /id="VAR_047613"
FT VARIANT 435
FT /note="S -> F (in ACHM3; dbSNP:rs121918344)"
FT /evidence="ECO:0000269|PubMed:10888875,
FT ECO:0000269|PubMed:10958649, ECO:0000269|PubMed:15657609"
FT /id="VAR_018111"
FT VARIANT 466
FT /note="M -> T (in ACHM3; unknown pathological significance;
FT dbSNP:rs35010099)"
FT /evidence="ECO:0000269|PubMed:15712225"
FT /id="VAR_047614"
FT VARIANT 469
FT /note="Y -> D (in STGD1; dbSNP:rs35365413)"
FT /evidence="ECO:0000269|PubMed:15712225"
FT /id="VAR_047615"
FT VARIANT 494
FT /note="D -> N (in ACHM3; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:15712225"
FT /id="VAR_047616"
FT VARIANT 513
FT /note="D -> Y (in ACHM3; unknown pathological significance;
FT dbSNP:rs765884344)"
FT /evidence="ECO:0000269|PubMed:15712225"
FT /id="VAR_047617"
FT VARIANT 525
FT /note="F -> N (in ACHM3; requires 2 nucleotide
FT substitutions)"
FT /evidence="ECO:0000269|PubMed:14757870"
FT /id="VAR_047618"
FT VARIANT 558
FT /note="G -> C (in ACHM3; dbSNP:rs749413012)"
FT /evidence="ECO:0000269|PubMed:15712225"
FT /id="VAR_047619"
FT VARIANT 595
FT /note="L -> F (in ACHM3; dbSNP:rs1554604849)"
FT /evidence="ECO:0000269|PubMed:15712225"
FT /id="VAR_047620"
FT VARIANT 672
FT /note="T -> P (in ACHM3; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:15712225"
FT /id="VAR_047621"
FT VARIANT 720..726
FT /note="Missing (in ACHM3)"
FT /evidence="ECO:0000269|PubMed:15657609"
FT /id="VAR_047622"
FT VARIANT 750
FT /note="P -> S (in dbSNP:rs3735971)"
FT /id="VAR_025525"
FT VARIANT 755
FT /note="E -> G (in dbSNP:rs3735972)"
FT /evidence="ECO:0000269|PubMed:10958649,
FT ECO:0000269|PubMed:15712225"
FT /id="VAR_018112"
SQ SEQUENCE 809 AA; 92167 MW; D16EE71A6149BDB5 CRC64;
MFKSLTKVNK VKPIGENNEN EQSSRRNEEG SHPSNQSQQT TAQEENKGEE KSLKTKSTPV
TSEEPHTNIQ DKLSKKNSSG DLTTNPDPQN AAEPTGTVPE QKEMDPGKEG PNSPQNKPPA
APVINEYADA QLHNLVKRMR QRTALYKKKL VEGDLSSPEA SPQTAKPTAV PPVKESDDKP
TEHYYRLLWF KVKKMPLTEY LKRIKLPNSI DSYTDRLYLL WLLLVTLAYN WNCCFIPLRL
VFPYQTADNI HYWLIADIIC DIIYLYDMLF IQPRLQFVRG GDIIVDSNEL RKHYRTSTKF
QLDVASIIPF DICYLFFGFN PMFRANRMLK YTSFFEFNHH LESIMDKAYI YRVIRTTGYL
LFILHINACV YYWASNYEGI GTTRWVYDGE GNEYLRCYYW AVRTLITIGG LPEPQTLFEI
VFQLLNFFSG VFVFSSLIGQ MRDVIGAATA NQNYFRACMD DTIAYMNNYS IPKLVQKRVR
TWYEYTWDSQ RMLDESDLLK TLPTTVQLAL AIDVNFSIIS KVDLFKGCDT QMIYDMLLRL
KSVLYLPGDF VCKKGEIGKE MYIIKHGEVQ VLGGPDGTKV LVTLKAGSVF GEISLLAAGG
GNRRTANVVA HGFANLLTLD KKTLQEILVH YPDSERILMK KARVLLKQKA KTAEATPPRK
DLALLFPPKE ETPKLFKTLL GGTGKASLAR LLKLKREQAA QKKENSEGGE EEGKENEDKQ
KENEDKQKEN EDKGKENEDK DKGREPEEKP LDRPECTASP IAVEEEPHSV RRTVLPRGTS
RQSLIISMAP SAEGGEEVLT IEVKEKAKQ
