FZD9_MOUSE
ID FZD9_MOUSE Reviewed; 592 AA.
AC Q9R216; O35494; Q9CX16; Q9R2B3;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Frizzled-9;
DE Short=Fz-9;
DE Short=mFz3;
DE Short=mFz9;
DE AltName: CD_antigen=CD349;
DE Flags: Precursor;
GN Name=Fzd9; Synonyms=Fzd3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=129/SvJ; TISSUE=Brain;
RX PubMed=10198163; DOI=10.1006/geno.1999.5773;
RA Wang Y.-K., Spoerle R., Paperna T., Schughart K., Francke U.;
RT "Characterization and expression pattern of the frizzled gene Fzd9, the
RT mouse homolog of FZD9 which is deleted in Williams-Beuren syndrome.";
RL Genomics 57:235-248(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 44-592.
RA Van Raay T.J., Rasmussen J.T., Rao M.S.;
RT "A novel mouse frizzled gene expressed in early neural development.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 144-592.
RC STRAIN=BALB/cJ;
RA Calo L., Mimmack M.L., Keverne E.B., Emson P.C.;
RT "Localization of the mouse frizzled gene mFZD3 in the olfactory epithelium
RT and in the vomeronasal organ.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=15930120; DOI=10.1242/dev.01871;
RA Zhao C., Aviles C., Abel R.A., Almli C.R., McQuillen P., Pleasure S.J.;
RT "Hippocampal and visuospatial learning defects in mice with a deletion of
RT frizzled 9, a gene in the Williams syndrome deletion interval.";
RL Development 132:2917-2927(2005).
RN [6]
RP INDUCTION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21402791; DOI=10.1083/jcb.201008012;
RA Albers J., Schulze J., Beil F.T., Gebauer M., Baranowsky A., Keller J.,
RA Marshall R.P., Wintges K., Friedrich F.W., Priemel M., Schilling A.F.,
RA Rueger J.M., Cornils K., Fehse B., Streichert T., Sauter G., Jakob F.,
RA Insogna K.L., Pober B., Knobeloch K.P., Francke U., Amling M., Schinke T.;
RT "Control of bone formation by the serpentine receptor Frizzled-9.";
RL J. Cell Biol. 192:1057-1072(2011).
RN [7]
RP FUNCTION.
RX PubMed=24391920; DOI=10.1371/journal.pone.0084232;
RA Heilmann A., Schinke T., Bindl R., Wehner T., Rapp A., Haffner-Luntzer M.,
RA Nemitz C., Liedert A., Amling M., Ignatius A.;
RT "The Wnt serpentine receptor Frizzled-9 regulates new bone formation in
RT fracture healing.";
RL PLoS ONE 8:E84232-E84232(2013).
RN [8]
RP DEVELOPMENTAL STAGE, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24860427; DOI=10.3389/fncel.2014.00110;
RA Aviles E.C., Pinto C., Hanna P., Ojeda J., Perez V., De Ferrari G.V.,
RA Zamorano P., Albistur M., Sandoval D., Henriquez J.P.;
RT "Frizzled-9 impairs acetylcholine receptor clustering in skeletal muscle
RT cells.";
RL Front. Cell. Neurosci. 8:110-110(2014).
CC -!- FUNCTION: Receptor for WNT2 that is coupled to the beta-catenin
CC canonical signaling pathway, which leads to the activation of
CC disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation
CC of beta-catenin and activation of Wnt target genes (By similarity).
CC Plays a role in neuromuscular junction (NMJ) assembly by negatively
CC regulating the clustering of acetylcholine receptors (AChR) through the
CC beta-catenin canonical signaling pathway (PubMed:24860427). May play a
CC role in neural progenitor cells (NPCs) viability through the beta-
CC catenin canonical signaling pathway by negatively regulating cell cycle
CC arrest leading to inhibition of neuron apoptotic process (By
CC similarity). During hippocampal development, regulates neuroblast
CC proliferation and apoptotic cell death (PubMed:15930120). Controls bone
CC formation through non canonical Wnt signaling mediated via ISG15
CC (PubMed:21402791). Positively regulates bone regeneration through non
CC canonical Wnt signaling (PubMed:24391920).
CC {ECO:0000250|UniProtKB:O00144, ECO:0000250|UniProtKB:Q8K4C8,
CC ECO:0000269|PubMed:15930120, ECO:0000269|PubMed:21402791,
CC ECO:0000269|PubMed:24391920, ECO:0000269|PubMed:24860427}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24860427};
CC Multi-pass membrane protein {ECO:0000255}. Note=Relocalizes DVL1 to the
CC cell membrane leading to phosphorylation of DVL1 and AXIN1
CC relocalization to the cell membrane. {ECO:0000250|UniProtKB:Q8K4C8}.
CC -!- TISSUE SPECIFICITY: In the embryo, found in the neural tube, trunk
CC skeletal muscle precursors (myotomes), limb skeletal anlagen,
CC craniofacial regions and nephric ducts. In the adult, expression is
CC abundant in heart, brain, testis and skeletal muscle. In the testis,
CC expressed in all spermatogenic cell types. Lower levels in adult lung,
CC liver and kidney. Barely detectable in spleen. Expressed also in
CC chondrocytes.
CC -!- DEVELOPMENTAL STAGE: Not detected at 7 dpc, weakly at 11 dpc and
CC strongly at 15 dpc and 17 dpc. Expression covers the entire neural tube
CC at 9.5 dpc, decreases at 10.5 dpc and becomes detectable only in the
CC lumbar to tail regions at 11.5 dpc. In the somites, expression begins
CC at 10.5 dpc to become up-regulated all along the rostrocaudal trunk
CC axis at 11.5 dpc. In craniofacial territories, expression is first
CC detected at 11.5 dpc in restricted areas of the nose, the maxillar
CC mandibular and second branchial arch anlagen. At 11.5 dpc,
CC predominantly expressed in restricted areas of the nose, dorsally to
CC the eye and in the caudal pharyngeal region. Highly expressed at early
CC stages of neuromuscular junction assembly (14.5 dpc) and gradually
CC decreases as development proceeds, being more than about 4-fold less
CC expressed in 19.5 dpc. {ECO:0000269|PubMed:10198163}.
CC -!- INDUCTION: Increases during the initial stages of osteoblast
CC differentiation. {ECO:0000269|PubMed:21402791}.
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 -!- DISRUPTION PHENOTYPE: Homozygous Fzd9 knockout mice show deficits in
CC spatial memory behaviors. Heterozygous and homozygous Fzd9 knockout
CC mice appear healthy, develop normally, and are fertile
CC (PubMed:15930120). Homozygous Fzd9 knockout mice display osteopenia
CC (PubMed:21402791). {ECO:0000269|PubMed:15930120,
CC ECO:0000269|PubMed:21402791}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family.
CC {ECO:0000305}.
CC -!- CAUTION: Has been first described as FZD3 in literature. {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; AF088850; AAD27789.1; -; Genomic_DNA.
DR EMBL; AK021164; BAB32311.1; -; mRNA.
DR EMBL; AF033585; AAB87503.2; -; mRNA.
DR EMBL; Y17709; CAB44237.1; -; mRNA.
DR CCDS; CCDS51661.1; -.
DR RefSeq; NP_034376.1; NM_010246.1.
DR AlphaFoldDB; Q9R216; -.
DR SMR; Q9R216; -.
DR IntAct; Q9R216; 2.
DR STRING; 10090.ENSMUSP00000053551; -.
DR GlyGen; Q9R216; 2 sites.
DR iPTMnet; Q9R216; -.
DR PhosphoSitePlus; Q9R216; -.
DR PaxDb; Q9R216; -.
DR PRIDE; Q9R216; -.
DR ProteomicsDB; 273401; -.
DR Antibodypedia; 14305; 546 antibodies from 39 providers.
DR Ensembl; ENSMUST00000062572; ENSMUSP00000053551; ENSMUSG00000049551.
DR GeneID; 14371; -.
DR KEGG; mmu:14371; -.
DR UCSC; uc008zya.2; mouse.
DR CTD; 8326; -.
DR MGI; MGI:1313278; Fzd9.
DR VEuPathDB; HostDB:ENSMUSG00000049551; -.
DR eggNOG; KOG3577; Eukaryota.
DR GeneTree; ENSGT00940000161226; -.
DR HOGENOM; CLU_007873_2_1_1; -.
DR InParanoid; Q9R216; -.
DR OMA; CEGIGYN; -.
DR OrthoDB; 509772at2759; -.
DR PhylomeDB; Q9R216; -.
DR TreeFam; TF317907; -.
DR BioGRID-ORCS; 14371; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Fzd3; mouse.
DR PRO; PR:Q9R216; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9R216; protein.
DR Bgee; ENSMUSG00000049551; Expressed in rib and 164 other tissues.
DR Genevisible; Q9R216; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0031527; C:filopodium membrane; IDA:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0042813; F:Wnt receptor activity; IDA:UniProtKB.
DR GO; GO:0017147; F:Wnt-protein binding; ISO:MGI.
DR GO; GO:0030183; P:B cell differentiation; IMP:MGI.
DR GO; GO:1990523; P:bone regeneration; IMP:UniProtKB.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0007611; P:learning or memory; IMP:MGI.
DR GO; GO:0051902; P:negative regulation of mitochondrial depolarization; ISS:UniProtKB.
DR GO; GO:1901029; P:negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:0060546; P:negative regulation of necroptotic process; ISS:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:1904394; P:negative regulation of skeletal muscle acetylcholine-gated channel clustering; IMP:UniProtKB.
DR GO; GO:0007405; P:neuroblast proliferation; IMP:MGI.
DR GO; GO:0001503; P:ossification; IMP:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IMP:UniProtKB.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; ISS:UniProtKB.
DR GO; GO:0099173; P:postsynapse organization; ISO:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR GO; GO:0099566; P:regulation of postsynaptic cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:1904393; P:regulation of skeletal muscle acetylcholine-gated channel clustering; IDA:UniProtKB.
DR GO; GO:0001836; P:release of cytochrome c from mitochondria; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; ISO:MGI.
DR CDD; cd07463; CRD_FZ9; 1.
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; IPR041777; FZ9_CRD.
DR InterPro; IPR017981; GPCR_2-like.
DR PANTHER; PTHR11309; PTHR11309; 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 2: Evidence at transcript 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..592
FT /note="Frizzled-9"
FT /id="PRO_0000013004"
FT TOPO_DOM 24..230
FT /note="Extracellular"
FT TRANSMEM 231..251
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..267
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..316
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..356
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 378..401
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..448
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..469
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 470..509
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 510..530
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 531..592
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..156
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT REGION 59..173
FT /note="Required for Wnt-activated receptor activity"
FT /evidence="ECO:0000250|UniProtKB:Q8K4C8"
FT REGION 555..592
FT /note="Required for CTNNB1 accumulation and TCF
FT transcription factor activity"
FT /evidence="ECO:0000250|UniProtKB:Q8K4C8"
FT MOTIF 533..538
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 CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 40..101
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 48..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 85..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 112..153
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 116..140
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT CONFLICT 66
FT /note="S -> P (in Ref. 3; AAB87503)"
FT /evidence="ECO:0000305"
FT CONFLICT 73..74
FT /note="QL -> HC (in Ref. 2; BAB32311)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="L -> F (in Ref. 2; BAB32311)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="P -> S (in Ref. 4; CAB44237)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="E -> K (in Ref. 4; CAB44237)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="A -> P (in Ref. 4; CAB44237)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="G -> D (in Ref. 3; AAB87503)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="V -> F (in Ref. 4; CAB44237)"
FT /evidence="ECO:0000305"
FT CONFLICT 592
FT /note="L -> P (in Ref. 2; BAB32311)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 592 AA; 64995 MW; 21B2D4F8CE232965 CRC64;
MAVPPLLRGA LLLWQLLATG GAALEIGRFD PERGRGPAPC QAMEIPMCRG IGYNLTRMPN
LLGHTSQGEA AAQLAEFSPL VQYGCHSHLR FFLCSLYAPM CTDQVSTPIP ACRPMCEQAR
LRCAPIMEQF NFGWPDSLDC ARLPTRNDPH ALCMEAPENA TAGPTEPHKG LGMLPVAPRP
ARPPGDSAPG PGSGGTCDNP EKFQYVEKSR SCAPRCGPGV EVFWSRRDKD FALVWMAVWS
ALCFFSTAFT VFTFLLEPHR FQYPERPIIF LSMCYNVYSL AFLIRAVAGA QSVACDQEAG
ALYVIQEGLE NTGCTLVFLL LYYFGMASSL WWVVLTLTWF LAAGKKWGHE AIEAHGSYFH
MAAWGLPALK TIVVLTLRKV AGDELTGLCY VASMDPAALT GFVLVPLSCY LVLGTSFLLT
GFVALFHIRK IMKTGGTNTE KLEKLMVKIG VFSILYTVPA TCVIVCYVYE RLNMDFWRLR
ATEQPCTAAT VPGGRRDCSL PGGSVPTVAV FMLKIFMSLV VGITSGVWVW SSKTFQTWQS
LCYRKMAAGR ARAKACRTPG GYGRGTHCHY KAPTVVLHMT KTDPSLENPT HL
