FZD1_HUMAN
ID FZD1_HUMAN Reviewed; 647 AA.
AC Q9UP38; A4D1E8; O94815; Q549T8;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Frizzled-1;
DE Short=Fz-1;
DE Short=hFz1;
DE AltName: Full=FzE1;
DE Flags: Precursor;
GN Name=FZD1;
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], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Prostatic carcinoma;
RX PubMed=10557084; DOI=10.1038/sj.onc.1202985;
RA Gazit A., Yaniv A., Bafico A., Pramila T., Igarashi M., Kitajewski J.,
RA Aaronson S.A.;
RT "Human frizzled 1 interacts with transforming Wnts to transduce a TCF
RT dependent transcriptional response.";
RL Oncogene 18:5959-5966(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Fetal lung;
RX PubMed=9813155; DOI=10.1006/bbrc.1998.9607;
RA Sagara N., Toda G., Hirai M., Terada M., Katoh M.;
RT "Molecular cloning, differential expression, and chromosomal localization
RT of human frizzled-1, frizzled-2, and frizzled-7.";
RL Biochem. Biophys. Res. Commun. 252:117-122(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 357-418.
RC TISSUE=Esophageal carcinoma;
RX PubMed=9707618; DOI=10.1073/pnas.95.17.10164;
RA Tanaka S., Akiyoshi T., Mori M., Wands J.R., Sugimachi K.;
RT "A novel frizzled gene identified in human esophageal carcinoma mediates
RT APC/beta-catenin signals.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:10164-10169(1998).
RN [8]
RP INTERACTION WITH MYOC.
RX PubMed=19188438; DOI=10.1128/mcb.01274-08;
RA Kwon H.S., Lee H.S., Ji Y., Rubin J.S., Tomarev S.I.;
RT "Myocilin is a modulator of Wnt signaling.";
RL Mol. Cell. Biol. 29:2139-2154(2009).
RN [9]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH C.DIFFICILE TCDB
RP (MICROBIAL INFECTION).
RX PubMed=27680706; DOI=10.1038/nature19799;
RA Tao L., Zhang J., Meraner P., Tovaglieri A., Wu X., Gerhard R., Zhang X.,
RA Stallcup W.B., Miao J., He X., Hurdle J.G., Breault D.T., Brass A.L.,
RA Dong M.;
RT "Frizzled proteins are colonic epithelial receptors for C. difficile toxin
RT B.";
RL Nature 538:350-355(2016).
CC -!- FUNCTION: Receptor for Wnt proteins (PubMed:10557084). Activated by
CC WNT3A, WNT3, WNT1 and to a lesser extent WNT2, but apparently not by
CC WNT4, WNT5A, WNT5B, WNT6, WNT7A or WNT7B (PubMed:10557084).
CC Contradictory results showing activation by WNT7B have been described
CC for mouse (By similarity). Functions in the canonical Wnt/beta-catenin
CC signaling pathway (PubMed:10557084). The canonical Wnt/beta-catenin
CC signaling pathway leads to the activation of disheveled proteins,
CC inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and
CC activation of Wnt target genes (PubMed:10557084). A second signaling
CC pathway involving PKC and calcium fluxes has been seen for some family
CC members, but it is not yet clear if it represents a distinct pathway or
CC if it can be integrated in the canonical pathway, as PKC seems to be
CC required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways
CC seem to involve interactions with G-proteins. May be involved in
CC transduction and intercellular transmission of polarity information
CC during tissue morphogenesis and/or in differentiated tissues
CC (Probable). {ECO:0000250|UniProtKB:O70421, ECO:0000269|PubMed:10557084,
CC ECO:0000305}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for C.difficile
CC toxin TcdB in the colonic epithelium. {ECO:0000269|PubMed:27680706}.
CC -!- SUBUNIT: Interacts with MYOC (PubMed:19188438). Interacts with WNT7B
CC (By similarity). {ECO:0000250|UniProtKB:O70421,
CC ECO:0000269|PubMed:19188438}.
CC -!- SUBUNIT: (Microbial infection) Interacts with C.difficile toxin TcdB;
CC frizzled receptors constitute the major host receptors for TcdB in the
CC colonic epithelium. {ECO:0000269|PubMed:27680706}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10557084};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in adult heart, placenta, lung, kidney,
CC pancreas, prostate, and ovary and in fetal lung and kidney.
CC {ECO:0000269|PubMed:9813155}.
CC -!- DOMAIN: Lys-Thr-X-X-X-Trp motif interacts with the PDZ domain of Dvl
CC (Disheveled) family members and is involved in the activation of the
CC Wnt/beta-catenin signaling pathway. {ECO:0000250}.
CC -!- DOMAIN: The FZ domain is involved in binding with Wnt ligands.
CC {ECO:0000250}.
CC -!- PTM: Ubiquitinated by ZNRF3, leading to its degradation by the
CC proteasome. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family.
CC {ECO:0000305}.
CC -!- CAUTION: Activation by specific Wnt family members may depend on the
CC cells used for the experiment. Contradictory results have been reported
CC for activation by WNT7B in human and mouse. {ECO:0000305}.
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DR EMBL; AF072872; AAD41636.1; -; mRNA.
DR EMBL; AB017363; BAA34666.1; -; mRNA.
DR EMBL; AC084381; AAS02008.1; -; Genomic_DNA.
DR EMBL; CH236949; EAL24161.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76871.1; -; Genomic_DNA.
DR EMBL; BC051271; AAH51271.1; -; mRNA.
DR CCDS; CCDS5620.1; -.
DR PIR; JE0337; JE0337.
DR RefSeq; NP_003496.1; NM_003505.1.
DR AlphaFoldDB; Q9UP38; -.
DR SMR; Q9UP38; -.
DR BioGRID; 113917; 13.
DR IntAct; Q9UP38; 9.
DR STRING; 9606.ENSP00000287934; -.
DR BindingDB; Q9UP38; -.
DR ChEMBL; CHEMBL2346493; -.
DR GuidetoPHARMACOLOGY; 229; -.
DR TCDB; 9.A.14.16.1; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; Q9UP38; 4 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; Q9UP38; -.
DR PhosphoSitePlus; Q9UP38; -.
DR BioMuta; FZD1; -.
DR DMDM; 92058705; -.
DR EPD; Q9UP38; -.
DR jPOST; Q9UP38; -.
DR MassIVE; Q9UP38; -.
DR MaxQB; Q9UP38; -.
DR PaxDb; Q9UP38; -.
DR PeptideAtlas; Q9UP38; -.
DR PRIDE; Q9UP38; -.
DR ProteomicsDB; 85351; -.
DR ABCD; Q9UP38; 43 sequenced antibodies.
DR Antibodypedia; 4574; 463 antibodies from 35 providers.
DR DNASU; 8321; -.
DR Ensembl; ENST00000287934.4; ENSP00000287934.2; ENSG00000157240.4.
DR GeneID; 8321; -.
DR KEGG; hsa:8321; -.
DR MANE-Select; ENST00000287934.4; ENSP00000287934.2; NM_003505.2; NP_003496.1.
DR UCSC; uc003ula.4; human.
DR CTD; 8321; -.
DR DisGeNET; 8321; -.
DR GeneCards; FZD1; -.
DR HGNC; HGNC:4038; FZD1.
DR HPA; ENSG00000157240; Low tissue specificity.
DR MIM; 603408; gene.
DR neXtProt; NX_Q9UP38; -.
DR OpenTargets; ENSG00000157240; -.
DR PharmGKB; PA28455; -.
DR VEuPathDB; HostDB:ENSG00000157240; -.
DR eggNOG; KOG3577; Eukaryota.
DR GeneTree; ENSGT00940000162584; -.
DR HOGENOM; CLU_007873_2_1_1; -.
DR InParanoid; Q9UP38; -.
DR OMA; RSHGMMY; -.
DR OrthoDB; 330751at2759; -.
DR PhylomeDB; Q9UP38; -.
DR TreeFam; TF317907; -.
DR PathwayCommons; Q9UP38; -.
DR Reactome; R-HSA-201681; TCF dependent signaling in response to WNT.
DR Reactome; R-HSA-373080; Class B/2 (Secretin family receptors).
DR Reactome; R-HSA-4086400; PCP/CE pathway.
DR Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-HSA-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR SignaLink; Q9UP38; -.
DR SIGNOR; Q9UP38; -.
DR BioGRID-ORCS; 8321; 11 hits in 1076 CRISPR screens.
DR ChiTaRS; FZD1; human.
DR GeneWiki; FZD1; -.
DR GenomeRNAi; 8321; -.
DR Pharos; Q9UP38; Tchem.
DR PRO; PR:Q9UP38; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9UP38; protein.
DR Bgee; ENSG00000157240; Expressed in mammary duct and 184 other tissues.
DR Genevisible; Q9UP38; HS.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:1990909; C:Wnt signalosome; IC:ParkinsonsUK-UCL.
DR GO; GO:0005109; F:frizzled binding; IPI:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL.
DR GO; GO:0042813; F:Wnt receptor activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0017147; F:Wnt-protein binding; IPI:UniProtKB.
DR GO; GO:0036520; P:astrocyte-dopaminergic neuron signaling; IEA:Ensembl.
DR GO; GO:0035425; P:autocrine signaling; IDA:BHF-UCL.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:UniProtKB.
DR GO; GO:0044338; P:canonical Wnt signaling pathway involved in mesenchymal stem cell differentiation; IMP:BHF-UCL.
DR GO; GO:0044339; P:canonical Wnt signaling pathway involved in osteoblast differentiation; IMP:BHF-UCL.
DR GO; GO:0007267; P:cell-cell signaling; IDA:BHF-UCL.
DR GO; GO:0045446; P:endothelial cell differentiation; IEA:Ensembl.
DR GO; GO:0060022; P:hard palate development; IEA:Ensembl.
DR GO; GO:0003149; P:membranous septum morphogenesis; IEA:Ensembl.
DR GO; GO:0003150; P:muscular septum morphogenesis; IEA:Ensembl.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IEA:Ensembl.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB.
DR GO; GO:0003151; P:outflow tract morphogenesis; IEA:Ensembl.
DR GO; GO:0090179; P:planar cell polarity pathway involved in neural tube closure; IEA:Ensembl.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:ARUK-UCL.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR GO; GO:0099054; P:presynapse assembly; TAS:ParkinsonsUK-UCL.
DR GO; GO:1905606; P:regulation of presynapse assembly; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:BHF-UCL.
DR GO; GO:1904953; P:Wnt signaling pathway involved in midbrain dopaminergic neuron differentiation; NAS:ParkinsonsUK-UCL.
DR Gene3D; 1.10.2000.10; -; 1.
DR InterPro; IPR015526; Frizzled/SFRP.
DR InterPro; IPR000539; Frizzled/Smoothened_TM.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR026550; FZD1/2.
DR InterPro; IPR017981; GPCR_2-like.
DR PANTHER; PTHR11309; PTHR11309; 1.
DR PANTHER; PTHR11309:SF34; PTHR11309:SF34; 1.
DR Pfam; PF01534; Frizzled; 1.
DR Pfam; PF01392; Fz; 1.
DR PRINTS; PR00489; FRIZZLED.
DR SMART; SM00063; FRI; 1.
DR SMART; SM01330; Frizzled; 1.
DR SUPFAM; SSF63501; SSF63501; 1.
DR PROSITE; PS50038; FZ; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Developmental protein; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix;
KW Ubl conjugation; Wnt signaling pathway.
FT SIGNAL 1..69
FT /evidence="ECO:0000255"
FT CHAIN 70..647
FT /note="Frizzled-1"
FT /id="PRO_0000012973"
FT TOPO_DOM 73..322
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..343
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 344..354
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376..402
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..445
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..466
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 467..489
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 490..510
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 511..536
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 537..557
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 558..601
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 602..622
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 623..647
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 111..230
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT REGION 74..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 625..630
FT /note="Lys-Thr-X-X-X-Trp motif, mediates interaction with
FT the PDZ domain of Dvl family members"
FT /evidence="ECO:0000250"
FT MOTIF 645..647
FT /note="PDZ-binding"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 116..177
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 124..170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 161..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 187..227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 191..215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT VARIANT 343
FT /note="V -> M (in dbSNP:rs3750146)"
FT /id="VAR_049290"
FT CONFLICT 93
FT /note="P -> PP (in Ref. 1; AAD41636)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 647 AA; 71158 MW; 7FC916A736482826 CRC64;
MAEEEAPKKS RAAGGGASWE LCAGALSARL AEEGSGDAGG RRRPPVDPRR LARQLLLLLW
LLEAPLLLGV RAQAAGQGPG QGPGPGQQPP PPPQQQQSGQ QYNGERGISV PDHGYCQPIS
IPLCTDIAYN QTIMPNLLGH TNQEDAGLEV HQFYPLVKVQ CSAELKFFLC SMYAPVCTVL
EQALPPCRSL CERARQGCEA LMNKFGFQWP DTLKCEKFPV HGAGELCVGQ NTSDKGTPTP
SLLPEFWTSN PQHGGGGHRG GFPGGAGASE RGKFSCPRAL KVPSYLNYHF LGEKDCGAPC
EPTKVYGLMY FGPEELRFSR TWIGIWSVLC CASTLFTVLT YLVDMRRFSY PERPIIFLSG
CYTAVAVAYI AGFLLEDRVV CNDKFAEDGA RTVAQGTKKE GCTILFMMLY FFSMASSIWW
VILSLTWFLA AGMKWGHEAI EANSQYFHLA AWAVPAIKTI TILALGQVDG DVLSGVCFVG
LNNVDALRGF VLAPLFVYLF IGTSFLLAGF VSLFRIRTIM KHDGTKTEKL EKLMVRIGVF
SVLYTVPATI VIACYFYEQA FRDQWERSWV AQSCKSYAIP CPHLQAGGGA PPHPPMSPDF
TVFMIKYLMT LIVGITSGFW IWSGKTLNSW RKFYTRLTNS KQGETTV
