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 24-JAN-2024, entry version 178. 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 CC (TC 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}; 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; 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 PDB; 8ETP; EM; 3.52 A; D=1-809. DR PDB; 8EU3; EM; 3.62 A; D=1-809. DR PDB; 8EUC; EM; 3.61 A; D=1-809. DR PDB; 8EV8; EM; 3.11 A; D=79-809. DR PDB; 8EV9; EM; 3.33 A; D=79-809. DR PDB; 8EVA; EM; 3.33 A; D=79-809. DR PDB; 8EVB; EM; 3.60 A; D=79-809. DR PDB; 8EVC; EM; 3.33 A; D=79-809. DR PDBsum; 7RHS; -. DR PDBsum; 8ETP; -. DR PDBsum; 8EU3; -. DR PDBsum; 8EUC; -. DR PDBsum; 8EV8; -. DR PDBsum; 8EV9; -. DR PDBsum; 8EVA; -. DR PDBsum; 8EVB; -. DR PDBsum; 8EVC; -. DR AlphaFoldDB; Q9NQW8; -. DR EMDB; EMD-24468; -. DR EMDB; EMD-28595; -. DR EMDB; EMD-28603; -. DR EMDB; EMD-28611; -. DR EMDB; EMD-28622; -. DR EMDB; EMD-28623; -. DR EMDB; EMD-28624; -. DR EMDB; EMD-28625; -. DR EMDB; EMD-28626; -. DR SMR; Q9NQW8; -. DR BioGRID; 120106; 5. 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 GlyCosmos; Q9NQW8; 1 site, No reported glycans. 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; 9606-ENSP00000316605; -. DR PeptideAtlas; Q9NQW8; -. DR ProteomicsDB; 82213; -. [Q9NQW8-1] DR ProteomicsDB; 82214; -. [Q9NQW8-2] DR Antibodypedia; 59091; 150 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 AGR; HGNC:2153; -. 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; FRVCMDH; -. DR OrthoDB; 74296at2759; -. DR PhylomeDB; Q9NQW8; -. DR TreeFam; TF318250; -. DR PathwayCommons; Q9NQW8; -. DR SignaLink; Q9NQW8; -. DR BioGRID-ORCS; 54714; 10 hits in 1138 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 male germ line stem cell (sensu Vertebrata) in testis and 128 other cell types or tissues. DR ExpressionAtlas; Q9NQW8; baseline and differential. 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:monoatomic cation transmembrane transport; IBA:GO_Central. DR GO; GO:0006812; P:monoatomic 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; 1.10.287.70; -; 1. DR Gene3D; 1.10.287.630; Helix hairpin bin; 1. DR Gene3D; 2.60.120.10; Jelly Rolls; 1. DR InterPro; IPR018488; cNMP-bd_CS. DR InterPro; IPR000595; cNMP-bd_dom. DR InterPro; IPR018490; cNMP-bd_dom_sf. DR InterPro; IPR005821; Ion_trans_dom. DR InterPro; IPR014710; RmlC-like_jellyroll. DR PANTHER; PTHR45638:SF8; CYCLIC NUCLEOTIDE-GATED CATION CHANNEL BETA-3; 1. DR PANTHER; PTHR45638; CYCLIC NUCLEOTIDE-GATED CATION CHANNEL SUBUNIT A; 1. DR Pfam; PF00027; cNMP_binding; 1. DR Pfam; PF00520; Ion_trans; 1. DR SMART; SM00100; cNMP; 1. DR SUPFAM; SSF51206; cAMP-binding domain-like; 1. DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1. DR PROSITE; PS00888; CNMP_BINDING_1; 1. DR PROSITE; PS00889; CNMP_BINDING_2; 1. DR PROSITE; PS50042; CNMP_BINDING_3; 1. DR Genevisible; Q9NQW8; HS. 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; uncertain 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; uncertain 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; uncertain FT 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; uncertain 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; uncertain significance)" FT /evidence="ECO:0000269|PubMed:15712225" FT /id="VAR_047616" FT VARIANT 513 FT /note="D -> Y (in ACHM3; uncertain 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; uncertain 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" FT STRAND 208..210 FT /evidence="ECO:0007829|PDB:7RHS" FT STRAND 212..214 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 216..241 FT /evidence="ECO:0007829|PDB:7RHS" FT TURN 247..249 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 250..270 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 272..274 FT /evidence="ECO:0007829|PDB:7RHS" FT STRAND 277..279 FT /evidence="ECO:0007829|PDB:7RHS" FT STRAND 282..284 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 287..295 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 299..306 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 310..314 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 321..329 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 331..344 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 348..378 FT /evidence="ECO:0007829|PDB:7RHS" FT STRAND 382..386 FT /evidence="ECO:0007829|PDB:7RHS" FT STRAND 389..391 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 393..405 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 417..448 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 450..468 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 473..489 FT /evidence="ECO:0007829|PDB:7RHS" FT STRAND 491..493 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 496..499 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 504..520 FT /evidence="ECO:0007829|PDB:7RHS" FT STRAND 523..528 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 530..538 FT /evidence="ECO:0007829|PDB:7RHS" FT STRAND 541..545 FT /evidence="ECO:0007829|PDB:7RHS" FT STRAND 550..552 FT /evidence="ECO:0007829|PDB:7RHS" FT STRAND 560..564 FT /evidence="ECO:0007829|PDB:7RHS" FT STRAND 569..572 FT /evidence="ECO:0007829|PDB:7RHS" FT STRAND 574..577 FT /evidence="ECO:0007829|PDB:7RHS" FT STRAND 579..584 FT /evidence="ECO:0007829|PDB:7RHS" FT STRAND 588..590 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 593..595 FT /evidence="ECO:0007829|PDB:7RHS" FT STRAND 606..612 FT /evidence="ECO:0007829|PDB:7RHS" FT STRAND 614..620 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 621..628 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 632..645 FT /evidence="ECO:0007829|PDB:7RHS" 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 //