OPSG_HUMAN
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 03-AUG-2022, entry version 203.
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";
CC ---------------------------------------------------------------------------
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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 GlyGen; P04001; 1 site.
DR iPTMnet; P04001; -.
DR PhosphoSitePlus; P04001; -.
DR BioMuta; OPN1MW; -.
DR DMDM; 129215; -.
DR MassIVE; P04001; -.
DR PRIDE; P04001; -.
DR Antibodypedia; 75857; 63 antibodies from 12 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; ENST00000369929.8; ENSP00000358945.4; NM_001048181.3; NP_001041646.1.
DR MANE-Select; ENST00000595290.6; ENSP00000472316.1; NM_000513.2; NP_000504.1.
DR MANE-Select; ENST00000599405.4; ENSP00000469970.1; NM_001330067.2; NP_001316996.1.
DR UCSC; uc004fkb.4; human.
DR CTD; 101060233; -.
DR CTD; 2652; -.
DR CTD; 728458; -.
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; SAFWCSP; -.
DR OrthoDB; 940057at2759; -.
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 5 CRISPR screens.
DR BioGRID-ORCS; 2652; 7 hits in 205 CRISPR screens.
DR BioGRID-ORCS; 728458; 3 hits in 217 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 vermiform appendix and 13 other tissues.
DR ExpressionAtlas; P04001; baseline and differential.
DR Genevisible; P04001; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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 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 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 PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR PROSITE; PS00238; OPSIN; 1.
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
