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 27-MAR-2024, entry version 202. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 14. 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 GlyCosmos; Q9UP38; 4 sites, 2 glycans. 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; 9606-ENSP00000287934; -. DR PeptideAtlas; Q9UP38; -. DR ProteomicsDB; 85351; -. DR ABCD; Q9UP38; 43 sequenced antibodies. DR Antibodypedia; 4574; 515 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 AGR; HGNC:4038; -. 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; GQENCGA; -. DR OrthoDB; 5483535at2759; -. 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 1154 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 186 other cell types or tissues. DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. 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:1904948; P:midbrain dopaminergic neuron differentiation; NAS:ParkinsonsUK-UCL. 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:0045892; P:negative regulation of DNA-templated transcription; IEA:Ensembl. DR GO; GO:1903377; P:negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; IEA:Ensembl. DR GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB. DR GO; GO:0035567; P:non-canonical Wnt signaling pathway; IBA:GO_Central. 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:0045893; P:positive regulation of DNA-templated transcription; IDA:BHF-UCL. DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:ARUK-UCL. DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:BHF-UCL. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl. DR GO; GO:0099054; P:presynapse assembly; TAS:ParkinsonsUK-UCL. DR GO; GO:2000739; P:regulation of mesenchymal stem cell differentiation; IMP:BHF-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 CDD; cd15247; 7tmF_FZD1; 1. DR CDD; cd07465; CRD_FZ1; 1. DR Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR015526; Frizzled/SFRP. DR InterPro; IPR000539; Frizzled/Smoothened_7TM. DR InterPro; IPR020067; Frizzled_dom. DR InterPro; IPR036790; Frizzled_dom_sf. DR InterPro; IPR017981; GPCR_2-like_7TM. DR PANTHER; PTHR11309; FRIZZLED; 1. DR PANTHER; PTHR11309:SF81; FRIZZLED-1; 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; Frizzled cysteine-rich domain; 1. DR PROSITE; PS50038; FZ; 1. DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1. DR Genevisible; Q9UP38; HS. 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 //