FZD5_RAT
ID FZD5_RAT Reviewed; 585 AA.
AC Q8CHL0;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Frizzled-5;
DE Short=Fz-5;
DE Flags: Precursor;
GN Name=Fzd5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ito S., Imamura T., Shiota K.;
RT "Molecular cloning and characterization of a gene encoding for rat Frizzled
RT 5.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20530549; DOI=10.1242/dev.046722;
RA Sahores M., Gibb A., Salinas P.C.;
RT "Frizzled-5, a receptor for the synaptic organizer Wnt7a, regulates
RT activity-mediated synaptogenesis.";
RL Development 137:2215-2225(2010).
CC -!- FUNCTION: Receptor for Wnt proteins (PubMed:20530549). Can activate
CC WNT2, WNT10B, WNT5A, but not WNT2B or WNT4 (in vitro); the in vivo
CC situation may be different since not all of these are known to be
CC coexpressed (By similarity). In neurons, activation of WNT7A promotes
CC formation of synapses (PubMed:20530549). Functions in the canonical
CC Wnt/beta-catenin signaling pathway. The canonical Wnt/beta-catenin
CC signaling pathway leads to the activation of disheveled proteins,
CC inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and
CC activation of Wnt target genes (By similarity). A second signaling
CC pathway involving PKC and calcium fluxes has been seen for some family
CC members, but it is not yet clear if it represents a distinct pathway or
CC if it can be integrated in the canonical pathway, as PKC seems to be
CC required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways
CC seem to involve interactions with G-proteins. May be involved in
CC transduction and intercellular transmission of polarity information
CC during tissue morphogenesis and/or in differentiated tissues
CC (Probable). Plays a role in yolk sac angiogenesis and in placental
CC vascularization (By similarity). {ECO:0000250|UniProtKB:Q9EQD0,
CC ECO:0000269|PubMed:20530549, ECO:0000305}.
CC -!- SUBUNIT: Binding of unsaturated fatty acid molecules (via FZ domain)
CC promotes homodimerization (via FZ domain). Interacts with WNT2B (By
CC similarity). Interacts with WNT7A. Interacts with GOPC (By similarity).
CC {ECO:0000250|UniProtKB:Q13467, ECO:0000250|UniProtKB:Q9EQD0}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20530549};
CC Multi-pass membrane protein {ECO:0000305}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9EQD0}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9EQD0}. Synapse {ECO:0000269|PubMed:20530549}.
CC Perikaryon {ECO:0000269|PubMed:20530549}. Cell projection, dendrite
CC {ECO:0000269|PubMed:20530549}. Cell projection, axon
CC {ECO:0000269|PubMed:20530549}. Note=Localized at the plasma membrane
CC and also found at the Golgi. {ECO:0000250|UniProtKB:Q9EQD0}.
CC -!- DOMAIN: The PDZ-binding motif mediates interaction with GOPC.
CC {ECO:0000250}.
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 RNF43 and ZNRF3, leading to its degradation by
CC the proteasome. {ECO:0000250|UniProtKB:Q13467}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family.
CC {ECO:0000305}.
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DR EMBL; AB052909; BAC53980.1; -; mRNA.
DR RefSeq; NP_776210.1; NM_173838.1.
DR AlphaFoldDB; Q8CHL0; -.
DR SMR; Q8CHL0; -.
DR GlyGen; Q8CHL0; 2 sites.
DR iPTMnet; Q8CHL0; -.
DR PhosphoSitePlus; Q8CHL0; -.
DR PRIDE; Q8CHL0; -.
DR GeneID; 317674; -.
DR KEGG; rno:317674; -.
DR UCSC; RGD:631406; rat.
DR CTD; 7855; -.
DR RGD; 631406; Fzd5.
DR InParanoid; Q8CHL0; -.
DR OrthoDB; 509772at2759; -.
DR PhylomeDB; Q8CHL0; -.
DR Reactome; R-RNO-4086398; Ca2+ pathway.
DR Reactome; R-RNO-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-RNO-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-RNO-4641263; Regulation of FZD by ubiquitination.
DR Reactome; R-RNO-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
DR PRO; PR:Q8CHL0; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005923; C:bicellular tight junction; ISO:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0001540; F:amyloid-beta binding; ISO:RGD.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0042813; F:Wnt receptor activity; ISO:RGD.
DR GO; GO:0017147; F:Wnt-protein binding; IPI:RGD.
DR GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR GO; GO:0008595; P:anterior/posterior axis specification, embryo; ISO:RGD.
DR GO; GO:0060561; P:apoptotic process involved in morphogenesis; ISO:RGD.
DR GO; GO:0060670; P:branching involved in labyrinthine layer morphogenesis; ISO:RGD.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:0048469; P:cell maturation; ISO:RGD.
DR GO; GO:0071219; P:cellular response to molecule of bacterial origin; ISO:RGD.
DR GO; GO:0060718; P:chorionic trophoblast cell differentiation; ISO:RGD.
DR GO; GO:0000578; P:embryonic axis specification; ISO:RGD.
DR GO; GO:0031076; P:embryonic camera-type eye development; ISO:RGD.
DR GO; GO:0048596; P:embryonic camera-type eye morphogenesis; ISO:RGD.
DR GO; GO:0060716; P:labyrinthine layer blood vessel development; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; ISO:RGD.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISO:RGD.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; ISO:RGD.
DR GO; GO:0002726; P:positive regulation of T cell cytokine production; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:RGD.
DR GO; GO:0031077; P:post-embryonic camera-type eye development; ISO:RGD.
DR GO; GO:0099054; P:presynapse assembly; IDA:SynGO.
DR GO; GO:2000810; P:regulation of bicellular tight junction assembly; ISO:RGD.
DR GO; GO:1901382; P:regulation of chorionic trophoblast cell proliferation; ISO:RGD.
DR GO; GO:0060061; P:Spemann organizer formation; ISO:RGD.
DR GO; GO:0060715; P:syncytiotrophoblast cell differentiation involved in labyrinthine layer development; ISO:RGD.
DR GO; GO:0033077; P:T cell differentiation in thymus; ISO:RGD.
DR GO; GO:0001944; P:vasculature development; ISO:RGD.
DR GO; GO:0016055; P:Wnt signaling pathway; ISO:RGD.
DR CDD; cd07460; CRD_FZ5; 1.
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; IPR037441; FZ5_CRD.
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 Cell membrane; Cell projection; Developmental protein; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Golgi apparatus; Lipid-binding;
KW Membrane; Receptor; Reference proteome; Signal; Synapse; Transducer;
KW Transmembrane; Transmembrane helix; Ubl conjugation; Wnt signaling pathway.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..585
FT /note="Frizzled-5"
FT /id="PRO_0000243937"
FT TOPO_DOM 27..238
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..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..315
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 337..358
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 380..402
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..449
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 471..500
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 501..521
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 522..585
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..150
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT REGION 156..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 525..530
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 MOTIF 583..585
FT /note="PDZ-binding"
FT /evidence="ECO:0000250"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 41..87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 78..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 105..147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 109..133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 585 AA; 64112 MW; BF26772B29FA12C8 CRC64;
MARPDPSAPP SLLLLLLAQL VGRAAAASKA PVCQEITVPM CRGIGYNLTH MPNQFNHDTQ
DEAGLEVHQF WPLVEIHCSP DLRFFLCSMY TPICLPDYHK PLPPCRSVCE RAKAGCSPLM
RQYGFAWPER MSCDRLPVLG GDAEVLCMDY NRSEATTASP KSFPAKPTLP GPPGAPSSGG
ECPSGGPSVC TCREPFVPIL KESHPLYNKV RTGQVPNCAV PCYQPSFSPD ERTFATFWIG
LWSVLCFIST STTVATFLID MERFRYPERP IIFLSACYLC VSLGFLVRLV VGHASVACSR
EHSHIHYETT GPALCTVVFL LVYFFGMASS IWWVILSLTW FLAAGMKWGN EAIAGYAQYF
HLAAWLIPSV KSITALALSS VDGDPVAGVC YVGNQNLNSL RGFVLGPLVL YLLVGTLFLL
AGFVSLFRIR SVIKQGGTKT DKLEKLMIRI GIFTLLYTVP ASIVVACYLY EQHYRESWEA
ALTCACPGSD AGQPRAKPEY WVLMLKYFMC LVVGITSGVW IWSGKTLESW RRFTSRCCCS
SRRGHKSGGA MVAGDYAEAS AALTGRTGPP GPAAAYHKQV SLSHV
