ID   FRIZ3_DROME             Reviewed;         581 AA.
AC   O77438; Q540W1; Q9I7Z7; Q9NIU0; Q9U902; Q9W5D5;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2002, sequence version 2.
DT   08-NOV-2023, entry version 172.
DE   RecName: Full=Frizzled-3;
DE            Short=dFz3;
DE   Flags: Precursor;
GN   Name=fz3; ORFNames=CG16785;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=10498678; DOI=10.1242/dev.126.20.4421;
RA   Sato A., Kojima T., Ui-Tei K., Miyata Y., Saigo K.;
RT   "Dfrizzled-3, a new Drosophila Wnt receptor, acting as an attenuator of
RT   Wingless signaling in wingless hypomorphic mutants.";
RL   Development 126:4421-4430(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=10704878; DOI=10.1016/s0925-4773(99)00313-5;
RA   Sivasankaran R., Calleja M., Morata G., Basler K.;
RT   "The Wingless target gene Dfz3 encodes a new member of the Drosophila
RT   Frizzled family.";
RL   Mech. Dev. 91:427-431(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Oregon-R;
RX   PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA   Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA   Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA   Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA   Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA   Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA   Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA   McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA   Glover D.M.;
RT   "From sequence to chromosome: the tip of the X chromosome of D.
RT   melanogaster.";
RL   Science 287:2220-2222(2000).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA   Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA   Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA   Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA   Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Receptor for Wnt proteins. Most of frizzled receptors are
CC       coupled to the beta-catenin canonical signaling pathway, which leads to
CC       the activation of disheveled proteins, inhibition of GSK-3 kinase,
CC       nuclear accumulation of beta-catenin and activation of Wnt target
CC       genes. A second signaling pathway involving PKC and calcium fluxes has
CC       been seen for some family members, but it is not yet clear if it
CC       represents a distinct pathway or if it can be integrated in the
CC       canonical pathway, as PKC seems to be required for Wnt-mediated
CC       inactivation of GSK-3 kinase. Both pathways seem to involve
CC       interactions with G-proteins. Required to coordinate the cytoskeletons
CC       of epidermal cells to produce a parallel array of cuticular hairs and
CC       bristles. {ECO:0000269|PubMed:10498678, ECO:0000269|PubMed:10704878}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Wing, leg and eye imaginal disks. In embryos,
CC       expressed is seen in brain, proventriculus, Malpighian tubules, anal
CC       plate and visceral mesoderm of parasegment 8.
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryos from stage 11 and in larvae.
CC   -!- DOMAIN: The FZ domain is involved in binding with Wnt ligands.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA20896.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB018565; BAA84677.1; -; mRNA.
DR   EMBL; AF195242; AAF63250.1; -; mRNA.
DR   EMBL; AE014298; AAF45547.1; -; Genomic_DNA.
DR   EMBL; AL031583; CAA20896.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL132792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AY119641; AAM50295.1; -; mRNA.
DR   PIR; T13484; T13484.
DR   RefSeq; NP_001284760.1; NM_001297831.1.
DR   RefSeq; NP_525035.2; NM_080296.3.
DR   AlphaFoldDB; O77438; -.
DR   SMR; O77438; -.
DR   BioGRID; 57591; 4.
DR   STRING; 7227.FBpp0111841; -.
DR   GlyCosmos; O77438; 2 sites, No reported glycans.
DR   GlyGen; O77438; 2 sites.
DR   PaxDb; 7227-FBpp0111841; -.
DR   DNASU; 31023; -.
DR   GeneID; 31023; -.
DR   KEGG; dme:Dmel_CG16785; -.
DR   AGR; FB:FBgn0027343; -.
DR   CTD; 31023; -.
DR   FlyBase; FBgn0027343; fz3.
DR   VEuPathDB; VectorBase:FBgn0027343; -.
DR   eggNOG; KOG3577; Eukaryota.
DR   HOGENOM; CLU_007873_5_1_1; -.
DR   InParanoid; O77438; -.
DR   PhylomeDB; O77438; -.
DR   SignaLink; O77438; -.
DR   BioGRID-ORCS; 31023; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 31023; -.
DR   PRO; PR:O77438; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   ExpressionAtlas; O77438; baseline and differential.
DR   GO; GO:0016020; C:membrane; ISS:FlyBase.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0042813; F:Wnt receptor activity; IBA:GO_Central.
DR   GO; GO:0017147; F:Wnt-protein binding; IPI:FlyBase.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR   GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:UniProtKB.
DR   GO; GO:0035567; P:non-canonical Wnt signaling pathway; IBA:GO_Central.
DR   CDD; cd15031; 7tmF_FZD3_insect; 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:SF142; FRIZZLED-3; 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; O77438; DM.
PE   2: Evidence at transcript level;
KW   Developmental protein; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Membrane; Receptor; Reference proteome; Signal; Transducer;
KW   Transmembrane; Transmembrane helix; Wnt signaling pathway.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..581
FT                   /note="Frizzled-3"
FT                   /id="PRO_0000013013"
FT   TOPO_DOM        20..237
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        238..258
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        259..270
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        271..291
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        292..321
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        322..342
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        343..359
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        360..380
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        381..393
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        394..414
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        415..442
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        443..463
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        464..488
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        489..509
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        510..581
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          35..156
FT                   /note="FZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   MOTIF           579..581
FT                   /note="PDZ-binding"
FT   CARBOHYD        54
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        206
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..141
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   CONFLICT        56
FT                   /note="T -> I (in Ref. 1; BAA84677)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        192
FT                   /note="A -> V (in Ref. 1; BAA84677)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        276
FT                   /note="L -> P (in Ref. 1; BAA84677)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        304
FT                   /note="G -> W (in Ref. 3; AAF45547/AAM50295)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        376
FT                   /note="A -> V (in Ref. 1; BAA84677)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   581 AA;  63252 MW;  07A8BBFF2A9E3F93 CRC64;
     MYAASILILH LTWAVATIAA NGAGHNGPVA SGAGPNGLQC QPIAVSACQG LGYNMTALPN
     LAGHTNQLEA ELQIAKLVPL IESGCSRRAR FLLCSSLFPL CTPDVPRPVA ACKLLCETVR
     GECMENAPPE LMELWPSFLN CDGLPQPEKH ELCMQIPQEV AVPGGSPSGP PTTGSPGVED
     HPQTYRFWKS GASPTSDLAG VLCPQNFSGS PFNPEECVPQ CQRDAFHTSS QKKTSETLIL
     GLSAVCFVLT LFALVTFWAE PTRFGYPERP VLFLCLCYNL FSVCYLERIV FHNQARMHDV
     ELQGRLMRPG CLLTPPCLAS YITTSYLSLC AASWWLIFAL CFYLSSHKKW SSEALEKRSG
     LFHVLAWVPP LAPPIAALLL EKVRPSELTG MCYAPGFVEL PALVLLLLGL YFTLRASRSL
     LSLQQQLQPT LAHHRFGQIR KRFVLFSLLY FAPTTAGVVA ALCERYADSV PSCSTPDDCL
     SPTPLSAWPA LVRIFFQLVG GTLTGLWVWS RKTCESYRNR LGASGTPTSS LMNQSKAAGA
     LPKKHLYTSG KSMLPTGGIT PLYAGISFHN VPVYNPNQSR V
//