ID Q542J1_MOUSE Unreviewed; 709 AA. AC Q542J1; DT 24-MAY-2005, integrated into UniProtKB/TrEMBL. DT 24-MAY-2005, sequence version 1. DT 27-MAR-2024, entry version 143. DE RecName: Full=Frizzled-6 {ECO:0000256|ARBA:ARBA00018155}; GN Name=Fzd6 {ECO:0000313|MGI:MGI:108474}; 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 {ECO:0000313|EMBL:BAC40329.1}; RN [1] {ECO:0000313|EMBL:BAC40329.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAC40329.1}; RC TISSUE=Thymus {ECO:0000313|EMBL:BAC40329.1}; RX PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9; RA Carninci P., Hayashizaki Y.; RT "High-efficiency full-length cDNA cloning."; RL Methods Enzymol. 303:19-44(1999). RN [2] {ECO:0000313|EMBL:BAC40329.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAC40329.1}; RC TISSUE=Thymus {ECO:0000313|EMBL:BAC40329.1}; RX PubMed=11042159; DOI=10.1101/gr.145100; RA Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M., RA Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.; RT "Normalization and subtraction of cap-trapper-selected cDNAs to prepare RT full-length cDNA libraries for rapid discovery of new genes."; RL Genome Res. 10:1617-1630(2000). RN [3] {ECO:0000313|EMBL:BAC40329.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAC40329.1}; RC TISSUE=Thymus {ECO:0000313|EMBL:BAC40329.1}; RX PubMed=11076861; DOI=10.1101/gr.152600; RA Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P., RA Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N., RA Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R., RA Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S., RA Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y., RA Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y., RA Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.; RT "RIKEN integrated sequence analysis (RISA) system--384-format sequencing RT pipeline with 384 multicapillary sequencer."; RL Genome Res. 10:1757-1771(2000). RN [4] {ECO:0000313|EMBL:BAC40329.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAC40329.1}; RC TISSUE=Thymus {ECO:0000313|EMBL:BAC40329.1}; RX PubMed=11217851; DOI=10.1038/35055500; RG The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium; RT "Functional annotation of a full-length mouse cDNA collection."; RL Nature 409:685-690(2001). RN [5] {ECO:0000313|EMBL:BAC40329.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAC40329.1}; RC TISSUE=Thymus {ECO:0000313|EMBL:BAC40329.1}; RX PubMed=12466851; DOI=10.1038/nature01266; RG The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team; RT "Analysis of the mouse transcriptome based on functional annotation of RT 60,770 full-length cDNAs."; RL Nature 420:563-573(2002). RN [6] {ECO:0000313|EMBL:BAC40329.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAC40329.1}; RC TISSUE=Thymus {ECO:0000313|EMBL:BAC40329.1}; RA Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P., RA Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W., Hayashida K., RA Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T., Hori F., Imotani K., RA Ishii Y., Itoh M., Kagawa I., Kasukawa T., Katoh H., Kawai J., Kojima Y., RA Kondo S., Konno H., Kouda M., Koya S., Kurihara C., Matsuyama T., RA Miyazaki A., Murata M., Nakamura M., Nishi K., Nomura K., Numazaki R., RA Ohno M., Ohsato N., Okazaki Y., Saito R., Saitoh H., Sakai C., Sakai K., RA Sakazume N., Sano H., Sasaki D., Shibata K., Shinagawa A., Shiraki T., RA Sogabe Y., Tagami M., Tagawa A., Takahashi F., Takaku-Akahira S., RA Takeda Y., Tanaka T., Tomaru A., Toya T., Yasunishi A., Muramatsu M., RA Hayashizaki Y.; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|EMBL:BAC40329.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAC40329.1}; RC TISSUE=Thymus {ECO:0000313|EMBL:BAC40329.1}; RG The FANTOM Consortium; RG Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group); RT "The Transcriptional Landscape of the Mammalian Genome."; RL Science 309:1559-1563(2005). RN [8] {ECO:0000313|EMBL:BAC40329.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAC40329.1}; RC TISSUE=Thymus {ECO:0000313|EMBL:BAC40329.1}; RX PubMed=16141073; DOI=10.1126/science.1112009; RG RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium; RT "Antisense Transcription in the Mammalian Transcriptome."; RL Science 309:1564-1566(2005). RN [9] {ECO:0007829|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). CC -!- SUBCELLULAR LOCATION: Apical cell membrane CC {ECO:0000256|ARBA:ARBA00004424}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004424}. Cell membrane CC {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004651}. Cell surface CC {ECO:0000256|ARBA:ARBA00004241}. Cytoplasmic vesicle membrane CC {ECO:0000256|ARBA:ARBA00004439}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004439}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family. CC {ECO:0000256|ARBA:ARBA00008077}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00090}. 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; AK088399; BAC40329.1; -; mRNA. DR RefSeq; NP_001155966.1; NM_001162494.1. DR RefSeq; NP_032082.3; NM_008056.3. DR RefSeq; XP_017171919.1; XM_017316430.1. DR AlphaFoldDB; Q542J1; -. DR SMR; Q542J1; -. DR Antibodypedia; 2906; 373 antibodies from 37 providers. DR DNASU; 14368; -. DR GeneID; 14368; -. DR KEGG; mmu:14368; -. DR AGR; MGI:108474; -. DR CTD; 8323; -. DR MGI; MGI:108474; Fzd6. DR VEuPathDB; HostDB:ENSMUSG00000022297; -. DR HOGENOM; CLU_007873_4_0_1; -. DR OMA; FLKHNNR; -. DR OrthoDB; 5483535at2759; -. DR PhylomeDB; Q542J1; -. DR BioGRID-ORCS; 14368; 2 hits in 77 CRISPR screens. DR ChiTaRS; Fzd6; mouse. DR ExpressionAtlas; Q542J1; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl. DR GO; GO:0042813; F:Wnt receptor activity; IEA:Ensembl. DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl. DR GO; GO:0035567; P:non-canonical Wnt signaling pathway; IEA:Ensembl. DR CDD; cd15032; 7tmF_FZD6; 1. DR CDD; cd07450; CRD_FZ6; 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; IPR041770; FZ6_CRD. DR InterPro; IPR026543; FZD6_7TM. DR InterPro; IPR017981; GPCR_2-like_7TM. DR PANTHER; PTHR11309; FRIZZLED; 1. DR PANTHER; PTHR11309:SF75; FRIZZLED-6; 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; Q542J1; MM. PE 1: Evidence at protein level; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329}; KW Developmental protein {ECO:0000256|ARBA:ARBA00022473}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE- KW ProRule:PRU00090}; KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Receptor {ECO:0000256|ARBA:ARBA00023170}; Signal {ECO:0000256|SAM:SignalP}; KW Transducer {ECO:0000256|ARBA:ARBA00023224}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687}. FT SIGNAL 1..18 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 19..709 FT /note="Frizzled-6" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5009971085" FT TRANSMEM 201..222 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 234..254 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 287..312 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 324..345 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 369..393 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 413..440 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 473..494 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 19..132 FT /note="FZ" FT /evidence="ECO:0000259|PROSITE:PS50038" FT DOMAIN 195..502 FT /note="G-protein coupled receptors family 2 profile 2" FT /evidence="ECO:0000259|PROSITE:PS50261" FT REGION 583..709 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 594..611 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 663..694 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT DISULFID 24..85 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090" FT DISULFID 32..78 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090" FT DISULFID 99..123 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090" SQ SEQUENCE 709 AA; 79082 MW; 01374A9EC9122484 CRC64; MERSPFLLAC ILLPLVRGHS LFTCEPITVP RCMKMTYNMT FFPNLMGHYD QGIAAVEMGH FLHLANLECS PNIEMFLCQA FIPTCTEQIH VVLPCRKLCE KIVSDCKKLM DTFGIRWPEE LECNRLPHCD DTVPVTSHPH TELSGPQKKS DQVPRDIGFW CPKHLRTSGD QGYRFLGIEQ CAPPCPNMYF KSDELDFAKS FIGIVSIFCL CATLFTFLTF LIDVRRFRYP ERPIIYYSVC YSIVSLMYFV GFLLGNSTAC NKADEKLELG DTVVLGSKNK ACSVVFMFLY FFTMAGTVWW VILTITWFLA AGRKWSCEAI EQKAVWFHAV AWGAPGFLTV MLLAMNKVEG DNISGVCFVG LYDLDASRYF VLLPLCLCVF VGLSLLLAGI ISLNHVRQVI QHDGRNQEKL KKFMIRIGVF SGLYLVPLVT LLGCYVYELV NRITWEMTWF SDHCHQYRIP CPYQANPKAR PELALFMIKY LMTLIVGISA VFWVGSKKTC TEWAGFFKRN RKRDPISESR RVLQESCEFF LKHNSKVKHK KKHGAPGPHR LKVISKSMGT STGATTNHGT SAMAIADHDY LGQETSTEVH TSPEASVKEG RADRANTPSA KDRDCGESAG PSSKLSGNRN GRESRAGGLK ERSNGSEGAP SEGRVSPKSS VPETGLIDCS TSQAASSPEP TSLKGSTSLP VHSASRARKE QGAGSHSDA //