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   24-JAN-2024, entry version 168.
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   GlyCosmos; Q9R216; 2 sites, No reported glycans.
DR   GlyGen; Q9R216; 2 sites.
DR   iPTMnet; Q9R216; -.
DR   PhosphoSitePlus; Q9R216; -.
DR   PaxDb; 10090-ENSMUSP00000053551; -.
DR   ProteomicsDB; 273401; -.
DR   Antibodypedia; 14305; 587 antibodies from 39 providers.
DR   Ensembl; ENSMUST00000062572.3; ENSMUSP00000053551.3; ENSMUSG00000049551.3.
DR   GeneID; 14371; -.
DR   KEGG; mmu:14371; -.
DR   UCSC; uc008zya.2; mouse.
DR   AGR; MGI:1313278; -.
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; 5483535at2759; -.
DR   PhylomeDB; Q9R216; -.
DR   TreeFam; TF317907; -.
DR   BioGRID-ORCS; 14371; 0 hits in 78 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 166 other cell types or tissues.
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: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:0035567; P:non-canonical Wnt signaling pathway; IBA:GO_Central.
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; cd15036; 7tmF_FZD9; 1.
DR   CDD; cd07463; CRD_FZ9; 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; IPR041777; FZ9_CRD.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
DR   PANTHER; PTHR11309; FRIZZLED; 1.
DR   PANTHER; PTHR11309:SF79; FRIZZLED-9; 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; Q9R216; MM.
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
//