ID   CNGA1_HUMAN             Reviewed;         690 AA.
AC   P29973; A8K7K6; J3KPZ2; Q16279; Q16485; Q4W5E3;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 3.
DT   07-APR-2021, entry version 202.
DE   RecName: Full=cGMP-gated cation channel alpha-1;
DE   AltName: Full=Cyclic nucleotide-gated cation channel 1;
DE   AltName: Full=Cyclic nucleotide-gated channel alpha-1;
DE            Short=CNG channel alpha-1;
DE            Short=CNG-1;
DE            Short=CNG1;
DE   AltName: Full=Cyclic nucleotide-gated channel, photoreceptor;
DE   AltName: Full=Rod photoreceptor cGMP-gated channel subunit alpha;
GN   Name=CNGA1; Synonyms=CNCG, CNCG1;
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).
RC   TISSUE=Retina;
RX   PubMed=1372902;
RA   Pittler S.J., Lee A.K., Altherr M.R., Howard T.A., Seldin M.F.,
RA   Hurwitz R.L., Wasmuth J.J., Baehr W.;
RT   "Primary structure and chromosomal localization of human and mouse rod
RT   photoreceptor cGMP-gated cation channel.";
RL   J. Biol. Chem. 267:6257-6262(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Retina;
RX   PubMed=1379636; DOI=10.1523/jneurosci.12-08-03248.1992;
RA   Dhallan R.S., Macke J.P., Eddy R.L., Shows T.B., Reed R.R., Yau K.-W.,
RA   Nathans J.;
RT   "Human rod photoreceptor cGMP-gated channel: amino acid sequence, gene
RT   structure, and functional expression.";
RL   J. Neurosci. 12:3248-3256(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Spleen;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 317-577.
RX   PubMed=7532814; DOI=10.1016/0028-3908(94)90027-2;
RA   Distler M., Biel M., Flockerzi V., Hofmann F.;
RT   "Expression of cyclic nucleotide-gated cation channels in non-sensory
RT   tissues and cells.";
RL   Neuropharmacology 33:1275-1282(1994).
RN   [7]
RP   VARIANT RP49 PHE-320, AND VARIANTS GLN-32 AND ASN-118.
RX   PubMed=7479749; DOI=10.1073/pnas.92.22.10177;
RA   Dryja T.P., Finn J.T., Peng Y.-W., McGee T.L., Berson E.L., Yau K.-W.;
RT   "Mutations in the gene encoding the alpha subunit of the rod cGMP-gated
RT   channel in autosomal recessive retinitis pigmentosa.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:10177-10181(1995).
RN   [8]
RP   INVOLVEMENT IN RP49.
RX   PubMed=15570217;
RA   Zhang Q., Zulfiqar F., Riazuddin S.A., Xiao X., Ahmad Z., Riazuddin S.,
RA   Hejtmancik J.F.;
RT   "Autosomal recessive retinitis pigmentosa in a Pakistani family mapped to
RT   CNGA1 with identification of a novel mutation.";
RL   Mol. Vis. 10:884-889(2004).
CC   -!- FUNCTION: Subunit of the rod cyclic GMP-gated cation channel, which is
CC       involved in the final stage of the phototransduction pathway. When
CC       light hits rod photoreceptors, cGMP concentrations decrease causing
CC       rapid closure of CNGA1/CNGB1 channels and, therefore, hyperpolarization
CC       of the membrane potential. {ECO:0000250|UniProtKB:Q00194}.
CC   -!- SUBUNIT: Forms a heterotetramer with CNGB1 in a 3:1 ratio. May also
CC       form cyclic nucleotide-activated homotetrameric channels, that are
CC       efficiently activated by saturating cGMP, but poorly activated by
CC       saturating cAMP compared to the heterotetramer with CNGB1.
CC       {ECO:0000250|UniProtKB:Q00194}.
CC   -!- INTERACTION:
CC       P29973; Q5ICW4: GRB14; Xeno; NbExp=4; IntAct=EBI-8417095, EBI-7639273;
CC       P29973; Q9JLM9: Grb14; Xeno; NbExp=2; IntAct=EBI-8417095, EBI-8347358;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q00194};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:Q00194}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P29973-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P29973-2; Sequence=VSP_047170;
CC   -!- TISSUE SPECIFICITY: Rod cells in the retina.
CC   -!- DOMAIN: The C-terminal coiled-coil domain mediates homotrimerization of
CC       CNGA subunits. {ECO:0000250}.
CC   -!- DISEASE: Retinitis pigmentosa 49 (RP49) [MIM:613756]: A retinal
CC       dystrophy belonging to the group of pigmentary retinopathies. Retinitis
CC       pigmentosa is characterized by retinal pigment deposits visible on
CC       fundus examination and primary loss of rod photoreceptor cells followed
CC       by secondary loss of cone photoreceptors. Patients typically have night
CC       vision blindness and loss of midperipheral visual field. As their
CC       condition progresses, they lose their far peripheral visual field and
CC       eventually central vision as well. {ECO:0000269|PubMed:15570217,
CC       ECO:0000269|PubMed:7479749}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel (TC
CC       1.A.1.5) family. CNGA1 subfamily. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-5 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB22778.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Mutations of the CNGA1 gene; Note=Retina
CC       International's Scientific Newsletter;
CC       URL="https://www.retina-international.org/files/sci-news/cnga1mut.htm";
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DR   EMBL; M84741; AAA52010.1; -; mRNA.
DR   EMBL; S42457; AAB22778.1; ALT_INIT; mRNA.
DR   EMBL; AK292021; BAF84710.1; -; mRNA.
DR   EMBL; AC096749; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC107068; AAY40919.1; -; Genomic_DNA.
DR   EMBL; CH471069; EAW93048.1; -; Genomic_DNA.
DR   EMBL; S76062; AAD14206.1; -; Genomic_DNA.
DR   PIR; A42161; A42161.
DR   RefSeq; NP_000078.2; NM_000087.3.
DR   RefSeq; NP_001136036.1; NM_001142564.1.
DR   RefSeq; XP_011511925.1; XM_011513623.2. [P29973-1]
DR   RefSeq; XP_016863201.1; XM_017007712.1.
DR   SMR; P29973; -.
DR   BioGRID; 107659; 1.
DR   IntAct; P29973; 2.
DR   MINT; P29973; -.
DR   STRING; 9606.ENSP00000384264; -.
DR   DrugBank; DB04209; Dequalinium.
DR   DrugCentral; P29973; -.
DR   GuidetoPHARMACOLOGY; 394; -.
DR   TCDB; 1.A.1.5.3; the voltage-gated ion channel (vic) superfamily.
DR   GlyGen; P29973; 1 site.
DR   iPTMnet; P29973; -.
DR   PhosphoSitePlus; P29973; -.
DR   BioMuta; CNGA1; -.
DR   DMDM; 239938910; -.
DR   jPOST; P29973; -.
DR   MassIVE; P29973; -.
DR   PaxDb; P29973; -.
DR   PeptideAtlas; P29973; -.
DR   PRIDE; P29973; -.
DR   ProteomicsDB; 54614; -. [P29973-1]
DR   Antibodypedia; 23791; 93 antibodies.
DR   DNASU; 1259; -.
DR   Ensembl; ENST00000402813; ENSP00000384264; ENSG00000198515.
DR   Ensembl; ENST00000420489; ENSP00000389881; ENSG00000198515.
DR   Ensembl; ENST00000514170; ENSP00000426862; ENSG00000198515.
DR   GeneID; 1259; -.
DR   KEGG; hsa:1259; -.
DR   UCSC; uc003gxt.5; human. [P29973-1]
DR   CTD; 1259; -.
DR   DisGeNET; 1259; -.
DR   GeneCards; CNGA1; -.
DR   GeneReviews; CNGA1; -.
DR   HGNC; HGNC:2148; CNGA1.
DR   HPA; ENSG00000198515; Tissue enhanced (liver).
DR   MalaCards; CNGA1; -.
DR   MIM; 123825; gene.
DR   MIM; 613756; phenotype.
DR   neXtProt; NX_P29973; -.
DR   Orphanet; 791; Retinitis pigmentosa.
DR   PharmGKB; PA26658; -.
DR   VEuPathDB; HostDB:ENSG00000198515.13; -.
DR   eggNOG; KOG0500; Eukaryota.
DR   HOGENOM; CLU_005746_12_0_1; -.
DR   InParanoid; P29973; -.
DR   OMA; YWLIFDY; -.
DR   OrthoDB; 1073751at2759; -.
DR   PhylomeDB; P29973; -.
DR   TreeFam; TF319048; -.
DR   PathwayCommons; P29973; -.
DR   Reactome; R-HSA-2485179; Activation of the phototransduction cascade.
DR   Reactome; R-HSA-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR   BioGRID-ORCS; 1259; 23 hits in 983 CRISPR screens.
DR   ChiTaRS; CNGA1; human.
DR   GeneWiki; Cyclic_nucleotide-gated_channel_alpha_1; -.
DR   GenomeRNAi; 1259; -.
DR   Pharos; P29973; Tchem.
DR   PRO; PR:P29973; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; P29973; protein.
DR   Bgee; ENSG00000198515; Expressed in amniotic fluid and 135 other tissues.
DR   ExpressionAtlas; P29973; baseline and differential.
DR   Genevisible; P29973; HS.
DR   GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR   GO; GO:0042622; C:photoreceptor outer segment membrane; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0030553; F:cGMP binding; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0022400; P:regulation of rhodopsin mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0016056; P:rhodopsin mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR   CDD; cd00038; CAP_ED; 1.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR032406; CLZ_dom.
DR   InterPro; IPR032945; CNGA1.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR45638:SF9; PTHR45638:SF9; 1.
DR   Pfam; PF16526; CLZ; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF00520; Ion_trans; 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   Alternative splicing; Cell membrane; cGMP; cGMP-binding; Coiled coil;
KW   Disease variant; Glycoprotein; Ion channel; Ion transport;
KW   Ligand-gated ion channel; Membrane; Nucleotide-binding; Reference proteome;
KW   Retinitis pigmentosa; Sensory transduction; Transmembrane;
KW   Transmembrane helix; Transport; Vision.
FT   CHAIN           1..690
FT                   /note="cGMP-gated cation channel alpha-1"
FT                   /id="PRO_0000219308"
FT   TOPO_DOM        1..164
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00194"
FT   TRANSMEM        165..185
FT                   /note="Helical; Name=S1"
FT                   /evidence="ECO:0000250|UniProtKB:Q00194"
FT   TOPO_DOM        186..198
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q00194"
FT   TRANSMEM        199..217
FT                   /note="Helical; Name=S2"
FT                   /evidence="ECO:0000250|UniProtKB:Q00194"
FT   TOPO_DOM        218..239
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00194"
FT   TRANSMEM        240..259
FT                   /note="Helical; Name=S3"
FT                   /evidence="ECO:0000250|UniProtKB:Q00194"
FT   TOPO_DOM        260..266
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q00194"
FT   TRANSMEM        267..288
FT                   /note="Helical; Name=S4"
FT                   /evidence="ECO:0000250|UniProtKB:Q00194"
FT   TOPO_DOM        289..299
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00194"
FT   TRANSMEM        300..326
FT                   /note="Helical; Name=S5"
FT                   /evidence="ECO:0000250|UniProtKB:Q00194"
FT   TOPO_DOM        327..369
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q00194"
FT   TRANSMEM        370..401
FT                   /note="Helical; Name=S6"
FT                   /evidence="ECO:0000250|UniProtKB:Q00194"
FT   TOPO_DOM        402..690
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00194"
FT   NP_BIND         487..609
FT                   /note="3',5'-cGMP"
FT                   /evidence="ECO:0000255"
FT   REGION          350..360
FT                   /note="P-helix"
FT                   /evidence="ECO:0000250|UniProtKB:Q00194"
FT   REGION          361..369
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000250|UniProtKB:Q00194"
FT   REGION          402..484
FT                   /note="C-linker"
FT                   /evidence="ECO:0000250|UniProtKB:Q00194"
FT   REGION          485..612
FT                   /note="Cyclic nucleotide-binding domain (CNBD)"
FT                   /evidence="ECO:0000250|UniProtKB:Q00194"
FT   COILED          623..666
FT                   /evidence="ECO:0000250|UniProtKB:Q00194"
FT   BINDING         546
FT                   /note="3',5'-cGMP"
FT                   /evidence="ECO:0000255"
FT   BINDING         561
FT                   /note="3',5'-cGMP"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        329
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00194"
FT   VAR_SEQ         1
FT                   /note="M -> MESRSSPRLECSGAISAHCSLHLPDSSDFQLIFVFLVEMGFHHVGQA
FT                   GLELLISSDLPTSASQSAGITDM (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:1379636"
FT                   /id="VSP_047170"
FT   VARIANT         32
FT                   /note="R -> Q (in dbSNP:rs76537883)"
FT                   /evidence="ECO:0000269|PubMed:7479749"
FT                   /id="VAR_009295"
FT   VARIANT         118
FT                   /note="D -> N (in dbSNP:rs28642966)"
FT                   /evidence="ECO:0000269|PubMed:7479749"
FT                   /id="VAR_009296"
FT   VARIANT         122
FT                   /note="N -> D (in dbSNP:rs28642966)"
FT                   /id="VAR_047385"
FT   VARIANT         320
FT                   /note="S -> F (in RP49; dbSNP:rs62625014)"
FT                   /evidence="ECO:0000269|PubMed:7479749"
FT                   /id="VAR_009297"
FT   CONFLICT        35
FT                   /note="E -> V (in Ref. 3; BAF84710)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        50
FT                   /note="S -> Y (in Ref. 1; AAA52010)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        89
FT                   /note="L -> I (in Ref. 1; AAA52010)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        150..151
FT                   /note="EE -> HH (in Ref. 1; AAA52010)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        209
FT                   /note="I -> V (in Ref. 3; BAF84710)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        543
FT                   /note="Y -> T (in Ref. 1; AAA52010)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        681..682
FT                   /note="GA -> WS (in Ref. 1; AAA52010)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   690 AA;  79586 MW;  F1045A210FE33DC0 CRC64;
     MKLSMKNNII NTQQSFVTMP NVIVPDIEKE IRRMENGACS SFSEDDDSAS TSEESENENP
     HARGSFSYKS LRKGGPSQRE QYLPGAIALF NVNNSSNKDQ EPEEKKKKKK EKKSKSDDKN
     ENKNDPEKKK KKKDKEKKKK EEKSKDKKEE EKKEVVVIDP SGNTYYNWLF CITLPVMYNW
     TMVIARACFD ELQSDYLEYW LILDYVSDIV YLIDMFVRTR TGYLEQGLLV KEELKLINKY
     KSNLQFKLDV LSLIPTDLLY FKLGWNYPEI RLNRLLRFSR MFEFFQRTET RTNYPNIFRI
     SNLVMYIVII IHWNACVFYS ISKAIGFGND TWVYPDINDP EFGRLARKYV YSLYWSTLTL
     TTIGETPPPV RDSEYVFVVV DFLIGVLIFA TIVGNIGSMI SNMNAARAEF QARIDAIKQY
     MHFRNVSKDM EKRVIKWFDY LWTNKKTVDE KEVLKYLPDK LRAEIAINVH LDTLKKVRIF
     ADCEAGLLVE LVLKLQPQVY SPGDYICKKG DIGREMYIIK EGKLAVVADD GVTQFVVLSD
     GSYFGEISIL NIKGSKAGNR RTANIKSIGY SDLFCLSKDD LMEALTEYPD AKTMLEEKGK
     QILMKDGLLD LNIANAGSDP KDLEEKVTRM EGSVDLLQTR FARILAEYES MQQKLKQRLT
     KVEKFLKPLI DTEFSSIEGP GAESGPIDST
//