ID   OPSR_HUMAN              Reviewed;         364 AA.
AC   P04000;
DT   23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-FEB-2022, sequence version 2.
DT   02-SEP-2026, entry version 219.
DE   RecName: Full=Long-wave-sensitive opsin 1 {ECO:0000303|Ref.6};
DE   AltName: Full=Red cone photoreceptor pigment;
DE   AltName: Full=Red-sensitive opsin;
DE            Short=ROP;
GN   Name=OPN1LW {ECO:0000312|HGNC:HGNC:9936}; Synonyms=RCP;
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], VARIANTS LEU-153 AND SER-180, FUNCTION,
RP   AND TISSUE SPECIFICITY.
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], AND VARIANTS LEU-153 AND
RP   SER-180.
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   FUNCTION, INDUCTION BY LIGHT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=6140680; DOI=10.1098/rspb.1983.0091;
RA   Dartnall H.J., Bowmaker J.K., Mollon J.D.;
RT   "Human visual pigments: microspectrophotometric results from the eyes of
RT   seven persons.";
RL   Proc. R. Soc. Lond., B, Biol. Sci. 220:115-130(1983).
RN   [4]
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   [5]
RP   FUNCTION.
RX   PubMed=21314100; DOI=10.1021/np100749j;
RA   Kono M., Crouch R.K.;
RT   "Probing human red cone opsin activity with retinal analogues.";
RL   J. Nat. Prod. 74:391-394(2011).
RN   [6] {ECO:0007744|PDB:8IU2}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.35 ANGSTROMS) IN COMPLEX WITH RETINAL,
RP   DISULFIDE BOND, AND MUTAGENESIS OF GLU-129.
RA   Li J., Zhang J.;
RT   "Cryo-EM structure of Long-wave-sensitive opsin 1.";
RL   Submitted (MAR-2023) to the PDB data bank.
RN   [7]
RP   VARIANT SER-180.
RX   PubMed=1557123; DOI=10.1038/356431a0;
RA   Winderickx J., Lindsey D.T., Sanocki E., Teller D.Y., Motulsky A.G.,
RA   Deeb S.S.;
RT   "Polymorphism in red photopigment underlies variation in colour matching.";
RL   Nature 356:431-433(1992).
RN   [8]
RP   VARIANTS BCM ARG-203 AND LEU-307, AND FUNCTION.
RX   PubMed=8213841;
RA   Nathans J., Maumenee I.H., Zrenner E., Sadowski B., Sharpe L.T.,
RA   Lewis R.A., Hansen E., Rosenberg T., Schwartz M., Heckenlively J.R.;
RT   "Genetic heterogeneity among blue-cone monochromats.";
RL   Am. J. Hum. Genet. 53:987-1000(1993).
RN   [9]
RP   VARIANT BCM ARG-203, AND FUNCTION.
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   [10]
RP   VARIANT CBP GLU-338, 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).
CC   -!- FUNCTION: G protein-coupled photoreceptor that selectively activates
CC       transducin G alpha protein (G(t)) in response to long-wavelength (red)
CC       light (PubMed:21314100, PubMed:2937147, PubMed:6140680). This
CC       activation leads to increased cGMP phosphodiesterase activity,
CC       resulting in decreased intracellular cGMP and subsequent closure of
CC       cGMP-gated ion channels (PubMed:21314100, PubMed:2937147,
CC       PubMed:6140680). The process is initiated when the opsin-bound cis-
CC       retinal chromophore absorbs a photon and isomerizes to all-trans-
CC       retinal, inducing a conformational change in the opsin that triggers
CC       the G protein-mediated phototransduction cascade (PubMed:21314100,
CC       PubMed:2937147, PubMed:6140680). Mediates visual perception of red
CC       light in cone photoreceptor cells (PubMed:12051694, PubMed:8213841,
CC       PubMed:8666378). {ECO:0000269|PubMed:12051694,
CC       ECO:0000269|PubMed:21314100, ECO:0000269|PubMed:2937147,
CC       ECO:0000269|PubMed:6140680, ECO:0000269|PubMed:8213841,
CC       ECO:0000269|PubMed:8666378}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Absorption:
CC         Abs(max)=558 nm {ECO:0000269|PubMed:6140680};
CC   -!- INTERACTION:
CC       P04000; Q8IXM6: NRM; NbExp=3; IntAct=EBI-13294781, EBI-10262547;
CC       P04000; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-13294781, EBI-11988865;
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       {ECO:0000255}. Photoreceptor outer segment membrane
CC       {ECO:0000250|UniProtKB:Q9W6A7}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: The red (OPN1LW), green (OPN1MW), and blue (OPN1SW)
CC       photoreceptor pigments are found in cone cells.
CC       {ECO:0000269|PubMed:2937147}.
CC   -!- INDUCTION: Maximally activated by long-wavelength light near 560 nm,
CC       corresponding to the red region of the visible spectrum in retinal cone
CC       cell. {ECO:0000269|PubMed:2937147}.
CC   -!- PTM: Contains one retinal chromophore covalently bound to a lysine
CC       residue via a Schiff base. Upon light absorption, the bound 11-cis-
CC       retinal isomerizes to all-trans-retinal. Following activation, the
CC       covalently bound all-trans-retinal is released through hydrolysis of
CC       the Schiff base, and OPN1 is regenerated by binding a new 11-cis-
CC       retinal molecule. {ECO:0000269|Ref.6}.
CC   -!- PTM: Phosphorylated on some or all of the serine and threonine residues
CC       present in the C-terminal region.
CC   -!- DISEASE: Colorblindness, partial, protan series (CBP) [MIM:303900]: An
CC       X-linked color vision defect characterized by a dichromasy in which red
CC       and green are confused, with loss of luminance and shift of brightness
CC       and hue curves toward the short wave end of the spectrum. Dichromasy is
CC       due to the use of only two types of photoreceptors, blue plus red in
CC       deuteranopia and blue plus green in protanopia.
CC       {ECO:0000269|PubMed:12051694}. Note=The disease is caused by variants
CC       affecting the gene represented 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:8213841,
CC       ECO:0000269|PubMed:8666378}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the G protein-coupled receptor 1 family. Opsin
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; M13305; AAB59524.1; -; Genomic_DNA.
DR   EMBL; M13300; AAB59524.1; JOINED; Genomic_DNA.
DR   EMBL; M13301; AAB59524.1; JOINED; Genomic_DNA.
DR   EMBL; M13302; AAB59524.1; JOINED; Genomic_DNA.
DR   EMBL; M13303; AAB59524.1; JOINED; Genomic_DNA.
DR   EMBL; M13304; AAB59524.1; JOINED; Genomic_DNA.
DR   EMBL; Z68193; CAA92342.1; -; Genomic_DNA.
DR   CCDS; CCDS14742.1; -.
DR   PIR; A03157; OOHUR.
DR   RefSeq; NP_064445.2; NM_020061.6.
DR   PDB; 8IU2; EM; 3.35 A; R=1-364.
DR   AlphaFoldDB; P04000; -.
DR   EMDB; EMD-35714; -.
DR   SMR; P04000; -.
DR   FunCoup; P04000; 306.
DR   IntAct; P04000; 3.
DR   NDEx; IQUERY-CP-OPN1LW; 1 NDEx IQuery Curated Pathway.
DR   STRING; 9606.ENSP00000358967; -.
DR   ChEMBL; CHEMBL1949482; -.
DR   TCDB; 9.A.14.1.1; the g-protein-coupled receptor (gpcr) family.
DR   GlyCosmos; P04000; 2 sites, No reported glycans.
DR   GlyGen; P04000; 2 sites.
DR   BioMuta; OPN1LW; -.
DR   DMDM; 129219; -.
DR   MassIVE; P04000; -.
DR   PaxDb; 9606-ENSP00000358967; -.
DR   PeptideAtlas; P04000; -.
DR   Antibodypedia; 64269; 46 antibodies from 10 providers.
DR   DNASU; 5956; -.
DR   Ensembl; ENST00000369951.9; ENSP00000358967.4; ENSG00000102076.10.
DR   GeneID; 5956; -.
DR   KEGG; hsa:5956; -.
DR   MANE-Select; ENST00000369951.9; ENSP00000358967.4; NM_020061.6; NP_064445.2.
DR   UCSC; uc033fax.1; human.
DR   AGR; HGNC:9936; -.
DR   ClinPGx; PA31936; -.
DR   CTD; 5956; -.
DR   DisGeNET; 5956; -.
DR   GeneCards; OPN1LW; -.
DR   HGNC; HGNC:9936; OPN1LW.
DR   HPA; ENSG00000102076; Tissue enriched (retina).
DR   MalaCards; OPN1LW; -.
DR   MIM; 300822; gene.
DR   MIM; 303700; phenotype.
DR   MIM; 303900; phenotype.
DR   OpenTargets; ENSG00000102076; -.
DR   Orphanet; 16; Blue cone monochromatism.
DR   Orphanet; 1872; Cone rod dystrophy.
DR   Orphanet; 90001; X-linked cone dysfunction syndrome with myopia.
DR   VEuPathDB; HostDB:ENSG00000102076; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01030000234549; -.
DR   HOGENOM; CLU_009579_3_0_1; -.
DR   InParanoid; P04000; -.
DR   OMA; EWGKQSF; -.
DR   OrthoDB; 8545112at2759; -.
DR   PAN-GO; P04000; 7 GO annotations based on evolutionary models.
DR   PhylomeDB; P04000; -.
DR   PathwayCommons; P04000; -.
DR   Reactome; R-HSA-2187335; The retinoid cycle in cones (daylight vision).
DR   Reactome; R-HSA-418594; G alpha (i) signalling events.
DR   Reactome; R-HSA-419771; Opsins.
DR   Reactome; R-HSA-9918450; Defective visual phototransduction due to OPN1LW loss of function.
DR   SignaLink; P04000; -.
DR   Agora; ENSG00000102076; -.
DR   ChiTaRS; OPN1LW; human.
DR   Pharos; P04000; Tbio.
DR   PRO; PR:P04000; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; P04000; protein.
DR   Bgee; ENSG00000102076; Expressed in ganglionic eminence and 9 other cell types or tissues.
DR   ExpressionAtlas; P04000; baseline and differential.
DR   GO; GO:0120201; C:cone photoreceptor disc membrane; ISS:UniProt.
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; IBA:GO_Central.
DR   GO; GO:0008020; F:G protein-coupled photoreceptor activity; IBA:GO_Central.
DR   GO; GO:0009881; F:photoreceptor activity; IMP:CACAO.
DR   GO; GO:0016038; P:absorption of visible light; IDA:UniProtKB.
DR   GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; TAS:UniProt.
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:0007165; P:signal transduction; TAS:ProtInc.
DR   GO; GO:0007601; P:visual perception; IMP:UniProt.
DR   CDD; cd15081; 7tmA_LWS_opsin; 1.
DR   FunFam; 1.20.1070.10:FF:000090; Long-wave-sensitive opsin 1; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR050125; GPCR_opsins.
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; OPSIN; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00575; OPSINREDGRN.
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   PDBsum; 8IU2; -.
PE   1: Evidence at protein level;
KW   3D-structure; Cell projection; Chromophore; Disease variant;
KW   Disulfide bond; G protein-coupled receptor; Glycoprotein; Membrane;
KW   Phosphoprotein; Photoreceptor protein; Receptor; Reference proteome;
KW   Retinal protein; Sensory transduction; Transducer; Transmembrane;
KW   Transmembrane helix; Vision.
FT   CHAIN           1..364
FT                   /note="Long-wave-sensitive opsin 1"
FT                   /id="PRO_0000197802"
FT   TOPO_DOM        1..52
FT                   /note="Extracellular"
FT   TRANSMEM        53..77
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        78..89
FT                   /note="Cytoplasmic"
FT   TRANSMEM        90..115
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        116..129
FT                   /note="Extracellular"
FT   TRANSMEM        130..149
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        150..168
FT                   /note="Cytoplasmic"
FT   TRANSMEM        169..192
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        193..218
FT                   /note="Extracellular"
FT   TRANSMEM        219..246
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        247..268
FT                   /note="Cytoplasmic"
FT   TRANSMEM        269..292
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        293..300
FT                   /note="Extracellular"
FT   TRANSMEM        301..325
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        326..364
FT                   /note="Cytoplasmic"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         312
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000269|Ref.6, ECO:0007744|PDB:8IU2"
FT   CARBOHYD        22
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BGI7"
FT   CARBOHYD        34
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        126..203
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521,
FT                   ECO:0000269|Ref.6, ECO:0007744|PDB:8IU2"
FT   VARIANT         111
FT                   /note="I -> V (in dbSNP:rs1065421)"
FT                   /id="VAR_012010"
FT   VARIANT         116
FT                   /note="S -> Y (in dbSNP:rs1065422)"
FT                   /id="VAR_012011"
FT   VARIANT         153
FT                   /note="M -> L (in dbSNP:rs713)"
FT                   /evidence="ECO:0000269|PubMed:15772651,
FT                   ECO:0000269|PubMed:2937147"
FT                   /id="VAR_012012"
FT   VARIANT         180
FT                   /note="A -> S (in 62% of the population;
FT                   dbSNP:rs1557157655)"
FT                   /evidence="ECO:0000269|PubMed:1557123,
FT                   ECO:0000269|PubMed:15772651, ECO:0000269|PubMed:2937147"
FT                   /id="VAR_004842"
FT   VARIANT         203
FT                   /note="C -> R (in BCM; dbSNP:rs121434621)"
FT                   /evidence="ECO:0000269|PubMed:8213841,
FT                   ECO:0000269|PubMed:8666378"
FT                   /id="VAR_009298"
FT   VARIANT         230
FT                   /note="I -> T (in dbSNP:rs148583295)"
FT                   /id="VAR_012014"
FT   VARIANT         274
FT                   /note="I -> V (in dbSNP:rs2315122)"
FT                   /id="VAR_050612"
FT   VARIANT         298
FT                   /note="A -> P (in dbSNP:rs1065440)"
FT                   /id="VAR_012015"
FT   VARIANT         307
FT                   /note="P -> L (in BCM; dbSNP:rs782797093)"
FT                   /evidence="ECO:0000269|PubMed:8213841"
FT                   /id="VAR_009299"
FT   VARIANT         338
FT                   /note="G -> E (in CBP; dbSNP:rs104894913)"
FT                   /evidence="ECO:0000269|PubMed:12051694"
FT                   /id="VAR_064054"
FT   MUTAGEN         129
FT                   /note="E->Q: Constitutively active."
FT                   /evidence="ECO:0000269|Ref.6"
FT   HELIX           50..80
FT                   /evidence="ECO:0007829|PDB:8IU2"
FT   HELIX           87..89
FT                   /evidence="ECO:0007829|PDB:8IU2"
FT   HELIX           90..114
FT                   /evidence="ECO:0007829|PDB:8IU2"
FT   TURN            115..117
FT                   /evidence="ECO:0007829|PDB:8IU2"
FT   HELIX           123..156
FT                   /evidence="ECO:0007829|PDB:8IU2"
FT   HELIX           166..182
FT                   /evidence="ECO:0007829|PDB:8IU2"
FT   HELIX           186..189
FT                   /evidence="ECO:0007829|PDB:8IU2"
FT   STRAND          200..204
FT                   /evidence="ECO:0007829|PDB:8IU2"
FT   HELIX           216..227
FT                   /evidence="ECO:0007829|PDB:8IU2"
FT   HELIX           229..252
FT                   /evidence="ECO:0007829|PDB:8IU2"
FT   HELIX           257..293
FT                   /evidence="ECO:0007829|PDB:8IU2"
FT   STRAND          294..296
FT                   /evidence="ECO:0007829|PDB:8IU2"
FT   HELIX           298..300
FT                   /evidence="ECO:0007829|PDB:8IU2"
FT   HELIX           301..319
FT                   /evidence="ECO:0007829|PDB:8IU2"
FT   HELIX           320..324
FT                   /evidence="ECO:0007829|PDB:8IU2"
FT   HELIX           327..334
FT                   /evidence="ECO:0007829|PDB:8IU2"
SQ   SEQUENCE   364 AA;  40574 MW;  730367A9CA3AB7D0 CRC64;
     MAQQWSLQRL AGRHPQDSYE DSTQSSIFTY TNSNSTRGPF EGPNYHIAPR WVYHLTSVWM
     IFVVTASVFT NGLVLAATMK FKKLRHPLNW ILVNLAVADL AETVIASTIS IVNQVSGYFV
     LGHPMCVLEG YTVSLCGITG LWSLAIISWE RWMVVCKPFG NVRFDAKLAI VGIAFSWIWA
     AVWTAPPIFG WSRYWPHGLK TSCGPDVFSG SSYPGVQSYM IVLMVTCCII PLAIIMLCYL
     QVWLAIRAVA KQQKESESTQ KAEKEVTRMV VVMIFAYCVC WGPYTFFACF AAANPGYAFH
     PLMAALPAYF AKSATIYNPV IYVFMNRQFR NCILQLFGKK VDDGSELSSA SKTEVSSVSS
     VSPA
//