ID   OPSG_HUMAN              Reviewed;         364 AA.
AC   P04001;
DT   23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-1986, sequence version 1.
DT   27-MAR-2024, entry version 212.
DE   RecName: Full=Medium-wave-sensitive opsin 1 {ECO:0000305};
DE   AltName: Full=Green cone photoreceptor pigment;
DE   AltName: Full=Green-sensitive opsin;
DE            Short=GOP;
GN   Name=OPN1MW {ECO:0000312|HGNC:HGNC:4206}; Synonyms=GCP;
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 [GENOMIC DNA].
RC   TISSUE=Retinal cone cell;
RX   PubMed=2937147; DOI=10.1126/science.2937147;
RA   Nathans J., Thomas D., Hogness D.S.;
RT   "Molecular genetics of human color vision: the genes encoding blue, green,
RT   and red pigments.";
RL   Science 232:193-202(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [3]
RP   REVIEW.
RX   PubMed=3303660; DOI=10.1016/0042-6989(86)90115-x;
RA   Applebury M.L., Hargrave P.A.;
RT   "Molecular biology of the visual pigments.";
RL   Vision Res. 26:1881-1895(1986).
RN   [4]
RP   SUBUNIT, GLYCOSYLATION AT ASN-34, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=28402104; DOI=10.1021/acs.biochem.7b00165;
RA   Hofmann L., Alexander N.S., Sun W., Zhang J., Orban T., Palczewski K.;
RT   "Hydrogen/deuterium exchange mass spectrometry of human green opsin reveals
RT   a conserved Pro-Pro motif in extracellular loop 2 of monostable visual G
RT   protein-coupled receptors.";
RL   Biochemistry 56:2338-2348(2017).
RN   [5]
RP   VARIANT CBD ARG-203, AND FUNCTION.
RX   PubMed=1302020; DOI=10.1038/ng0792-251;
RA   Winderickx J., Sanocki E., Lindsey D.T., Teller D.Y., Motulsky A.G.,
RA   Deeb S.S.;
RT   "Defective colour vision associated with a missense mutation in the human
RT   green visual pigment gene.";
RL   Nat. Genet. 1:251-256(1992).
RN   [6]
RP   GLYCOSYLATION, AND REGION.
RX   PubMed=30948514; DOI=10.1074/jbc.ra118.006835;
RA   Salom D., Jin H., Gerken T.A., Yu C., Huang L., Palczewski K.;
RT   "Human red and green cone opsins are O-glycosylated at an N-terminal
RT   Ser/Thr-rich domain conserved in vertebrates.";
RL   J. Biol. Chem. 294:8123-8133(2019).
RN   [7]
RP   VARIANT BCM ARG-203.
RX   PubMed=8666378; DOI=10.1006/geno.1995.9998;
RA   Reyniers E., Van Thienen M.N., Meire F., De Boulle K., Devries K.,
RA   Kestelijn P., Willems P.J.;
RT   "Gene conversion between red and defective green opsin gene in blue cone
RT   monochromacy.";
RL   Genomics 29:323-328(1995).
RN   [8]
RP   VARIANTS CBD LYS-94 AND GLN-330, AND FUNCTION.
RX   PubMed=12051694; DOI=10.1016/s0006-291x(02)00458-8;
RA   Ueyama H., Kuwayama S., Imai H., Tanabe S., Oda S., Nishida Y., Wada A.,
RA   Shichida Y., Yamade S.;
RT   "Novel missense mutations in red/green opsin genes in congenital color-
RT   vision deficiencies.";
RL   Biochem. Biophys. Res. Commun. 294:205-209(2002).
RN   [9]
RP   VARIANT COD5 ARG-177, CHARACTERIZATION OF VARIANT COD5 ARG-177, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=20579627; DOI=10.1016/j.ajhg.2010.05.019;
RA   Gardner J.C., Webb T.R., Kanuga N., Robson A.G., Holder G.E., Stockman A.,
RA   Ripamonti C., Ebenezer N.D., Ogun O., Devery S., Wright G.A., Maher E.R.,
RA   Cheetham M.E., Moore A.T., Michaelides M., Hardcastle A.J.;
RT   "X-linked cone dystrophy caused by mutation of the red and green cone
RT   opsins.";
RL   Am. J. Hum. Genet. 87:26-39(2010).
CC   -!- FUNCTION: Visual pigments are the light-absorbing molecules that
CC       mediate vision. They consist of an apoprotein, opsin, covalently linked
CC       to cis-retinal. {ECO:0000305|PubMed:12051694,
CC       ECO:0000305|PubMed:1302020, ECO:0000305|PubMed:2937147}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Absorption:
CC         Abs(max)=530 nm {ECO:0000305|PubMed:2937147};
CC   -!- SUBUNIT: Monomer. Homodimer. Homotetramer.
CC       {ECO:0000269|PubMed:28402104}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20579627};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: The three color pigments are found in the cone
CC       photoreceptor cells. {ECO:0000305|PubMed:2937147}.
CC   -!- PTM: N-glycosylated (PubMed:30948514). O-glycosylated
CC       (PubMed:30948514). {ECO:0000269|PubMed:30948514}.
CC   -!- PTM: Phosphorylated on some or all of the serine and threonine residues
CC       present in the C-terminal region. {ECO:0000305|PubMed:2937147}.
CC   -!- DISEASE: Colorblindness, partial, deutan series (CBD) [MIM:303800]: A
CC       color vision defect characterized by a dichromasy in which red and
CC       green are confused, without loss of luminance or shift or shortening of
CC       the spectrum. Dichromasy is due to the use of only two types of
CC       photoreceptors, blue plus red in deuteranopia and blue plus green in
CC       protanopia. {ECO:0000269|PubMed:12051694, ECO:0000269|PubMed:1302020}.
CC       Note=The disease is caused by variants affecting the gene represented
CC       in this entry.
CC   -!- DISEASE: Blue cone monochromacy (BCM) [MIM:303700]: A rare X-linked
CC       congenital stationary cone dysfunction syndrome characterized by the
CC       absence of functional long wavelength-sensitive and medium wavelength-
CC       sensitive cones in the retina. Color discrimination is severely
CC       impaired from birth, and vision is derived from the remaining preserved
CC       blue (S) cones and rod photoreceptors. BCM typically presents with
CC       reduced visual acuity, pendular nystagmus, and photophobia. Patients
CC       often have myopia. {ECO:0000269|PubMed:8666378}. Note=The disease is
CC       caused by variants affecting the gene represented in this entry.
CC   -!- DISEASE: Cone dystrophy 5 (COD5) [MIM:303700]: An X-linked cone
CC       dystrophy. Cone dystrophies are retinal dystrophies characterized by
CC       progressive degeneration of the cone photoreceptors with preservation
CC       of rod function, as indicated by electroretinogram. However, some rod
CC       involvement may be present in some cone dystrophies, particularly at
CC       late stage. Affected individuals suffer from photophobia, loss of
CC       visual acuity, color vision and central visual field. Another sign is
CC       the absence of macular lesions for many years. Cone dystrophies are
CC       distinguished from the cone-rod dystrophies in which some loss of
CC       peripheral vision also occurs. {ECO:0000269|PubMed:20579627}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC   -!- CAUTION: Medium-wave-sensitive opsin genes vary in number among
CC       individuals and, together with a single red pigment gene, reside in a
CC       head-to-tail tandem array within the X chromosome. In the GRCh38
CC       reference genome assembly, there are 3 genes in tandem coding for
CC       identical proteins AC P04001, AC P0DN77 and P0DN78. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Mutations of the color pigment genes; Note=Retina
CC       International's Scientific Newsletter;
CC       URL="https://www.retina-international.org/files/sci-news/cppmut.htm";
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DR   EMBL; K03494; AAB59503.1; -; Genomic_DNA.
DR   EMBL; M13306; AAB59503.1; JOINED; Genomic_DNA.
DR   EMBL; K03490; AAB59503.1; JOINED; Genomic_DNA.
DR   EMBL; K03491; AAB59503.1; JOINED; Genomic_DNA.
DR   EMBL; K03492; AAB59503.1; JOINED; Genomic_DNA.
DR   EMBL; K03493; AAB59503.1; JOINED; Genomic_DNA.
DR   EMBL; K03497; AAB59525.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; K03495; AAB59525.1; JOINED; Genomic_DNA.
DR   EMBL; K03496; AAB59525.1; JOINED; Genomic_DNA.
DR   EMBL; AC244097; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS14743.1; -.
DR   CCDS; CCDS35447.1; -.
DR   PIR; A03158; OOHUG.
DR   RefSeq; NP_000504.1; NM_000513.2.
DR   RefSeq; NP_001041646.1; NM_001048181.2.
DR   RefSeq; NP_001316996.1; NM_001330067.1.
DR   RefSeq; XP_016855469.1; XM_016999980.1.
DR   AlphaFoldDB; P04001; -.
DR   SMR; P04001; -.
DR   GlyCosmos; P04001; 1 site, No reported glycans.
DR   GlyGen; P04001; 1 site.
DR   iPTMnet; P04001; -.
DR   PhosphoSitePlus; P04001; -.
DR   BioMuta; OPN1MW; -.
DR   DMDM; 129215; -.
DR   MassIVE; P04001; -.
DR   PeptideAtlas; P04001; -.
DR   Antibodypedia; 75857; 72 antibodies from 13 providers.
DR   DNASU; 2652; -.
DR   Ensembl; ENST00000595290.6; ENSP00000472316.1; ENSG00000268221.6.
DR   GeneID; 101060233; -.
DR   GeneID; 2652; -.
DR   GeneID; 728458; -.
DR   KEGG; hsa:101060233; -.
DR   KEGG; hsa:2652; -.
DR   KEGG; hsa:728458; -.
DR   MANE-Select; ENST00000595290.6; ENSP00000472316.1; NM_000513.2; NP_000504.1.
DR   UCSC; uc004fkb.4; human.
DR   AGR; HGNC:26952; -.
DR   AGR; HGNC:4206; -.
DR   AGR; HGNC:51831; -.
DR   DisGeNET; 101060233; -.
DR   DisGeNET; 2652; -.
DR   DisGeNET; 728458; -.
DR   GeneCards; OPN1MW; -.
DR   HGNC; HGNC:4206; OPN1MW.
DR   HPA; ENSG00000268221; Tissue enriched (retina).
DR   MalaCards; OPN1MW; -.
DR   MIM; 300821; gene.
DR   MIM; 303700; phenotype.
DR   MIM; 303800; phenotype.
DR   neXtProt; NX_P04001; -.
DR   OpenTargets; ENSG00000268221; -.
DR   Orphanet; 16; Blue cone monochromatism.
DR   Orphanet; 1872; Cone rod dystrophy.
DR   Orphanet; 319698; NON RARE IN EUROPE: Partial color blindness, deutan type.
DR   Orphanet; 90001; X-linked cone dysfunction syndrome with myopia.
DR   PharmGKB; PA142671229; -.
DR   VEuPathDB; HostDB:ENSG00000268221; -.
DR   HOGENOM; CLU_009579_3_0_1; -.
DR   InParanoid; P04001; -.
DR   OMA; CAITMAE; -.
DR   OrthoDB; 5350930at2759; -.
DR   PhylomeDB; P04001; -.
DR   TreeFam; TF324998; -.
DR   PathwayCommons; P04001; -.
DR   Reactome; R-HSA-2187335; The retinoid cycle in cones (daylight vision).
DR   Reactome; R-HSA-2453864; Retinoid cycle disease events.
DR   Reactome; R-HSA-418594; G alpha (i) signalling events.
DR   Reactome; R-HSA-419771; Opsins.
DR   SignaLink; P04001; -.
DR   SIGNOR; P04001; -.
DR   BioGRID-ORCS; 101060233; 1 hit in 6 CRISPR screens.
DR   BioGRID-ORCS; 2652; 7 hits in 250 CRISPR screens.
DR   BioGRID-ORCS; 728458; 4 hits in 254 CRISPR screens.
DR   ChiTaRS; OPN1MW; human.
DR   GeneWiki; OPN1MW; -.
DR   Pharos; P04001; Tdark.
DR   PRO; PR:P04001; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; P04001; Protein.
DR   Bgee; ENSG00000268221; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 14 other cell types or tissues.
DR   ExpressionAtlas; P04001; baseline.
DR   GO; GO:0097381; C:photoreceptor disc membrane; TAS:Reactome.
DR   GO; GO:0001750; C:photoreceptor outer segment; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0008020; F:G protein-coupled photoreceptor activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR   GO; GO:0009881; F:photoreceptor activity; IMP:CACAO.
DR   GO; GO:0071482; P:cellular response to light stimulus; IBA:GO_Central.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0007602; P:phototransduction; IBA:GO_Central.
DR   GO; GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB.
DR   GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR001760; Opsin.
DR   InterPro; IPR000378; Opsin_red/grn.
DR   InterPro; IPR027430; Retinal_BS.
DR   PANTHER; PTHR24240:SF17; MEDIUM-WAVE-SENSITIVE OPSIN 1-RELATED; 1.
DR   PANTHER; PTHR24240; OPSIN; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00575; OPSINREDGRN.
DR   SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   PROSITE; PS00238; OPSIN; 1.
DR   Genevisible; P04001; HS.
PE   1: Evidence at protein level;
KW   Cell membrane; Chromophore; Disease variant; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW   Photoreceptor protein; Receptor; Reference proteome; Retinal protein;
KW   Sensory transduction; Transducer; Transmembrane; Transmembrane helix;
KW   Vision.
FT   CHAIN           1..364
FT                   /note="Medium-wave-sensitive opsin 1"
FT                   /id="PRO_0000197785"
FT   TOPO_DOM        1..52
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        53..77
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        78..89
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        90..115
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        116..129
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        130..149
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        150..168
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        169..192
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        193..218
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        219..246
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        247..268
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        269..292
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        293..300
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        301..325
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        326..364
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          17..43
FT                   /note="Required for 11-cis-retinal regeneration"
FT                   /evidence="ECO:0000269|PubMed:30948514"
FT   MOD_RES         312
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        34
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:28402104"
FT   DISULFID        126..203
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   VARIANT         94
FT                   /note="N -> K (in CBD; dbSNP:rs104894915)"
FT                   /evidence="ECO:0000269|PubMed:12051694"
FT                   /id="VAR_064051"
FT   VARIANT         177
FT                   /note="W -> R (in COD5; results in protein misfolding and
FT                   retention in the endoplasmic reticulum; dbSNP:rs267606927)"
FT                   /evidence="ECO:0000269|PubMed:20579627"
FT                   /id="VAR_064052"
FT   VARIANT         203
FT                   /note="C -> R (in CBD and BCM; dbSNP:rs104894914)"
FT                   /evidence="ECO:0000269|PubMed:1302020,
FT                   ECO:0000269|PubMed:8666378"
FT                   /id="VAR_004841"
FT   VARIANT         330
FT                   /note="R -> Q (in CBD; dbSNP:rs104894916)"
FT                   /evidence="ECO:0000269|PubMed:12051694"
FT                   /id="VAR_064053"
SQ   SEQUENCE   364 AA;  40584 MW;  A98D046958C72AE9 CRC64;
     MAQQWSLQRL AGRHPQDSYE DSTQSSIFTY TNSNSTRGPF EGPNYHIAPR WVYHLTSVWM
     IFVVIASVFT NGLVLAATMK FKKLRHPLNW ILVNLAVADL AETVIASTIS VVNQVYGYFV
     LGHPMCVLEG YTVSLCGITG LWSLAIISWE RWMVVCKPFG NVRFDAKLAI VGIAFSWIWA
     AVWTAPPIFG WSRYWPHGLK TSCGPDVFSG SSYPGVQSYM IVLMVTCCIT PLSIIVLCYL
     QVWLAIRAVA KQQKESESTQ KAEKEVTRMV VVMVLAFCFC WGPYAFFACF AAANPGYPFH
     PLMAALPAFF AKSATIYNPV IYVFMNRQFR NCILQLFGKK VDDGSELSSA SKTEVSSVSS
     VSPA
//