FRIZ3_DROME
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 03-AUG-2022, entry version 168.
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};
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; 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 GlyGen; O77438; 2 sites.
DR PaxDb; O77438; -.
DR DNASU; 31023; -.
DR GeneID; 31023; -.
DR KEGG; dme:Dmel_CG16785; -.
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 Genevisible; O77438; DM.
DR GO; GO:0016021; C:integral component of 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 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; 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 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
