Gene Dmel\fz

General Information
Symbol	Dmel\fz	Species	D. melanogaster
Name	frizzled	Annotation symbol	CG17697
Feature type	protein_coding_gene	FlyBase ID	FBgn0001085
Created / Updated	2003-12-01/2003-12-01
Genomic Location
Chromosome (arm)	3L	Recombination map	3-41.7
Cytogenetic map	70D4-70D5	Sequence location	3L:14,267,447..14,361,748 [+]
Map ( GBrowse )
Summary Information
Automatically generated summary See sections below for more information	The gene frizzled is referred to in FlyBase by the symbol fz (CG17697, FBgn0001085). It has the cytological map location 70D4-70D5. Its sequence location is 3L:14267447..14361748. Its molecular function is described as: Wnt receptor activity; Wnt-protein binding; transmembrane receptor activity; non-G-protein coupled 7TM receptor activity; G-protein coupled receptor activity. It is involved in the biological processes described with 22 unique terms, many of which group under: anatomical structure development; establishment of planar polarity; cell communication; sensory organ development; signal transduction; macromolecule localization; protein localization; imaginal disc-derived wing hair organization and biogenesis; organ morphogenesis; Wnt receptor signaling pathway; epithelial cell differentiation; homophilic cell adhesion; cell division; regulation of cellular component organization and biogenesis; ommatidial rotation. 170 alleles are reported. The phenotypes of these alleles are annotated with 34 unique terms, many of which group under: adult segment; peripheral nervous system; nervous system; adult mesothoracic segment; organ system; embryonic nervous system; metatarsus; appendage segment; thoracic segment; adult cuticle. It has 2 annotated transcripts and 2 annotated polypeptides.
External Summaries

Phenotypic Description from the Red Book (Lindsley & Zimm 1992)
Gene/Allele symbols may differ from current usage	fz: frizzled fz: frizzled From Bridges and Brehme, 1944, Carnegie Inst. Washington Publ. No. 552: 85. Hairs on thorax directed irregularly toward midline. Thoracic bristles also inturned and often wavy. Postverticals may turn outward. Hairs on wing edge and feet nearly erect; trichomes on wings of flies carrying weaker alleles tend to form swirls rather than lying parallel to one another and pointing distally; stronger alleles can cause random orientation of trichomes. Polarity of chaetae deranged in characteristic ways on wings, notum, halteres, legs, tergites, and sternites; fz M+ clones in M/+ wings cause derangement of polarity in M/+ cells surrounding clone (Gubb and Garcia-Bellido, 1982, J. Embryol. Exp. Morphol. 68: 37-57). In a wild-type background clones of wing cells homozygous for fz alleles that cause eye roughening, but not of those without effect on eye texture, cause adjacent normal trichomes in regions distal, anterior, and posterior, but not proximal to the clone, to orient toward the clone rather than distally as they normally do; no effect on trichomes on opposite surface of the wing (Vinson and Adler, 1987, Nature 329: 549-51). Wing may be reduced. A low level of doubling of trichomes and splitting of chaetae observed. Sex combs may be irregular. Most alleles cause eyes to be rough. Two weak alleles, fz24 and fz34 and two neomorphic alleles, fz13 and fz20, have normal eye textures. Extra leg joints tend to form as mirror-image duplications proximal to the normal joints on tarsal segments one to four. Also polarities of bristles, hairs, and bracts on legs abnormal (Held, Duarte, and Derakhshanian, 1986, Wilhelm Roux's Arch. Dev. Biol. 195: 145-57). RK2. fz13 A neomorphic allele causing severe disruption of trichome orientation in the costal wing cell, a region little affected by most alleles; phenotype of homozygote more severe than that of hemizygote. Also unlike other alleles, homozygous clones of fz13 cells in the wing do not affect orientation of trichomes in surrounding normal cells. A third notable feature of fz13 is that it is without effect on eye texture. fz20 Like fu13.
Detailed Mapping Data
FlyBase Computed Cytological Location
Cytogenetic map Evidence for location 70D4-70D5 Limits computationally determined from genome sequence between P{PZ}l(3)70Da⁰²⁴⁰²&P{PZ}btl⁰⁰²⁰⁸ and P{PZ}Mpcp⁰⁰⁵⁶⁴
Experimentally Determined Cytological Location
Cytogenetic map Notes References 70D4-70D7 (determined by in situ hybridisation) (Adler et al., 1990) 70D4-70D7 (determined by in situ hybridisation) (Vinson et al., 1989)
Experimentally Determined Recombination Data
Location	3-41.7 2-42 (Fernandez Gianotti, 1952)
Left of (cM)
Right of (cM)
Notes
Molecular Map Data
Gene Order (in direction of increasing cytology) References Gene Order (overall orientation not stated) References
Gene Model & Products
Please see the GBrowse view of Dmel\fz for information on other features
Comments on Gene Model
	Transposon inserted in intron
Transcript Data
Annotated Transcripts
Name FlyBase ID RefSeq ID Length (nt) Associated CDS (aa) fz-RA FBtr0075743 NM_080073 3794 581 fz-RB FBtr0075742 NM_168587 3765 415
Additional Transcript Data & Comments
Reported size (kB)	4.0 (northern blot) (Vinson et al., 1989) 4.0, >4.0 (northern blot) (Adler et al., 1990)
Comments	The 3.6kb and 4.0kb fz transcripts appear to differ only in the site of polyadenlyation. (Adler et al., 1990)
External Data
Crossreferences
Polypeptide Data
Annotated Polypeptides
Name FlyBase ID Predicted MW (kD) Length (aa) Theoretical pI RefSeq ID GenBank protein fz-PA FBpp0075485 64.8 581 8.22 NP_524812 AAF49746 fz-PB FBpp0075484 46.1 415 7.78 NP_729970 AAN11810
Additional Polypeptide Data & Comments
Reported size (kD)	62, 60 (kD observed) (Park et al., 1994) 62, 60 (kD observed); 62 (kD predicted) (Park et al., 1994) 581, 415 (aa) (Adler et al., 1990) 60, 42 (kD observed) (Krasnow and Adler, 1994) 581 (aa) (Vinson et al., 1989)
Comments	Experiments with heat shock driven transgenes demonstrate that only the longer 581aa form of the fz protein shows any activity and rescues fz mutations. Overexpression results in two distinct tissue polarity phenotypes. (Krasnow and Adler, 1994) The fz protein has 7 putative transmembrane domains. (Vinson et al., 1989) The fz protein contains and odd number of transmembrane domains and is glycosylated. (Park et al., 1994) Experiments with heat shock driven transgenes demonstrate that the shorter 415aa form of the fz protein is unable to rescue fz mutations. No endogenous protein of this size was detected. (Krasnow and Adler, 1994) One of a couple of protein products. (FlyBase, 1992-, FlyBase, 1992-) The 415aa fz protein is essentially a carboxy-terminal truncated class I fz protein. It contains the seven transmembrane domains and is also likely to be an integral membrane protein. (Adler et al., 1990)
External Data
Linkouts	PANTHER - Protein classification by function, families, and pathways • FBgn0001085
Crossreferences	InterPro domains - A database of protein families, domains, and functional sites • Frizzled cysteine-rich domain (IPR000024) Frizzled protein (IPR000539) GPCR, family 2, secretin-like (IPR000832) Frizzled related (IPR015526)
Sequences Consistent with the Gene Model
DDBJ / EMBL / GenBank	DNA sequence Protein sequence Name AA951534 AA952093 AE003535 AAF49746 AE003535 AAN11810 AI519380 AI543818 AW943116 AX093877 AY051808 AAK93232 AZ933376 BI162105 BI164092 BI165032 BI165961 BI169842 BI172180 BI172848 BI173241 BI213065 BI213273 BI214739 BI215177 BI215598 BI216139 BI216461 BI231985 BI232524 BI232715 BI234662 BI234687 BI236646 BI237040 BI239419 BI239546 BI240992 BI241147 BI242073 BI242294 BI242837 BI357809 BI362491 BI362497 BI363808 BI364569 BI365372 BI366072 BI366095 BI368221 BI372060 BI372087 BI374207 BI374223 BI374823 BI375307 BI376061 BI481826 BI482038 BI483689 BI483953 BI578129 BI578382 BI578720 BI580334 BI584411 BI607981 BI610718 BI617419 BI623646 BI627891 BP545138 BP545139 BP553471 BT024389 CL868592 CO185321 CO187068 CO188273 CO190760 CO190911 CO262712 CO262903 CO263511 CO264536 CO265362 CO266290 CO271526 CO271711 CO278229 CO285531 CO288792 CO295053 CO298467 CO299177 CO301673 CO303174 CO303696 CO311345 CO314911 CO327622 CO332090 CO335932 CO336852 CO337507 CO337803 CO338534 CO341281 CZ468672 CZ470087 CZ472260 CZ478448 CZ479142 CZ479504 CZ479505 CZ479546 CZ481175 CZ481176 CZ483452 CZ489475 CZ489476 CZ489683 CZ490629 CZ490630 EC058703 EC061332 EC067757 EC070833 EC071630 EC074254 EC074774 EC074799 EC075182 EC077040 EC082007 EC084651 EC084671 EC088401 EC088529 EC088530 EC194391 EC195603 EC196818 EC198482 EC202652 EC210176 EC213598 EC221491 EC224510 EC228145 EC228801 EC232107 EC240178 EC240447 EC240863 EC242543 EC242757 EC254546 EC258261 EC261563 EC262279 EC264412 EC267045 EC267857 EL873407 EL875570 X54646 CAA38458 X54647 CAA38459 X54648 CAA38460 X54648 CAA38461 X54649 CAA38460 X54649 CAA38461 X54650 CAA38460 X54650 CAA38461 X54651 CAA38460 X54652 CAA38461

UniProtKB/Swiss-Prot	P18537
UniProtKB/TrEMBL

Maps to
Does NOT map to
Identified with	LD32066 (BDGP Project Members, 2000-) D1144 (BDGP Project Members, 1994-1999)
Mapped Features & Mutations
Please see GBrowse or insertion reports for information on insertions of transgenic constructs and features not listed here Type Symbol & Location Additional Notes References point mutation fz[SN] 3L:14,268,556..14,268,556 comment=Site of nucleotide substitution in mutant inferred by FlyBase based on reported amino acid change. evidence=experimental na_change=T14268556A pr_change=C134\|fz-PB,C134\|fz-PA reported_pr_change=C134@ (Povelones et al., 2005) point mutation fz[CL] 3L:14,268,704..14,268,704 comment=Site of nucleotide substitution in mutant inferred by FlyBase based on reported amino acid change. evidence=experimental na_change=A14268704T pr_change=K184\|fz-PB,K184\|fz-PA reported_pr_change=K184@ (Povelones et al., 2005) point mutation fz[HE1l] 3L:14,298,010..14,298,010 comment=Position of mutation on reference sequence inferred from Figure 3. evidence=experimental na_change=G14298010A pr_change=C229Y\|fz-PB,C229Y\|fz-PA reported_na_change=G?A reported_pr_change=C229Y (Jones et al., 1996, Povelones et al., 2005) point mutation fz[13] 3L:14,305,000..14,305,000 comment=P278 is in the first cytoplasmic loop of the fz protein. evidence=experimental na_change=C14305000T pr_change=P278S\|fz-PB,P278S\|fz-PA reported_na_change=C?T reported_pr_change=P278S (Jones et al., 1996, Povelones et al., 2005) point mutation fz[20] 3L:14,305,000..14,305,000 comment=P278 is in the first cytoplasmic loop of the fz protein. evidence=experimental na_change=C14305000T pr_change=P278S\|fz-PB,P278S\|fz-PA reported_na_change=C?T reported_pr_change=P278S (Jones et al., 1996) point mutation fz[16] 3L:14,305,001..14,305,001 comment=P278 is in the first cytoplasmic loop of the fz protein. evidence=experimental na_change=C14305001T pr_change=P278L\|fz-PB,P278L\|fz-PA reported_na_change=C?T reported_pr_change=P278L (Jones et al., 1996) point mutation fz[19] 3L:14,305,001..14,305,001 comment=P278 is in the first cytoplasmic loop of the fz protein. evidence=experimental na_change=C14305001T pr_change=P278L\|fz-PB,P278L\|fz-PA reported_na_change=C?T reported_pr_change=P278L (Adler et al., 1994, Povelones et al., 2005) point mutation fz[JW] 3L:14,305,132..14,305,132 comment=Site of nucleotide substitution in mutant inferred by FlyBase based on reported amino acid change. evidence=experimental na_change=C14305132T pr_change=Q322\|fz-PB,Q322\|fz-PA reported_pr_change=Q322@ (Povelones et al., 2005) point mutation fz[RN] 3L:14,310,285..14,310,286