FZD9_RAT
ID FZD9_RAT Reviewed; 592 AA.
AC Q8K4C8;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Frizzled-9 {ECO:0000303|PubMed:12138115};
DE AltName: Full=Frizzled-like protein 9 {ECO:0000303|PubMed:16670314};
DE Short=rFz9 {ECO:0000303|PubMed:12138115};
DE Flags: Precursor;
GN Name=Fzd9 {ECO:0000312|RGD:628817};
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], SUBCELLULAR LOCATION, FUNCTION, AND REGION.
RC STRAIN=Sprague-Dawley;
RX PubMed=12138115; DOI=10.1074/jbc.m205658200;
RA Karasawa T., Yokokura H., Kitajewski J., Lombroso P.J.;
RT "Frizzled-9 is activated by Wnt-2 and functions in Wnt/beta -catenin
RT signaling.";
RL J. Biol. Chem. 277:37479-37486(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=16670314; DOI=10.4049/jimmunol.176.10.6055;
RA Becanovic K., Jagodic M., Sheng J.R., Dahlman I., Aboul-Enein F.,
RA Wallstrom E., Olofsson P., Holmdahl R., Lassmann H., Olsson T.;
RT "Advanced intercross line mapping of Eae5 reveals Ncf-1 and CLDN4 as
RT candidate genes for experimental autoimmune encephalomyelitis.";
RL J. Immunol. 176:6055-6064(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for WNT2 that is coupled to the beta-catenin
CC canonical signaling pathway, which leads to the activation of
CC disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation
CC of beta-catenin and activation of Wnt target genes (PubMed:12138115).
CC Plays a role in neuromuscular junction (NMJ) assembly by negatively
CC regulating the clustering of acetylcholine receptors (AChR) through the
CC beta-catenin canonical signaling pathway (By similarity). May play a
CC role in neural progenitor cells (NPCs) viability through the beta-
CC catenin canonical signaling pathway by negatively regulating cell cycle
CC arrest leading to inhibition of neuron apoptotic process (By
CC similarity). During hippocampal development, regulates neuroblast
CC proliferation and apoptotic cell death. Controls bone formation through
CC non canonical Wnt signaling mediated via ISG15. Positively regulates
CC bone regeneration through non canonical Wnt signaling (By similarity).
CC {ECO:0000250|UniProtKB:O00144, ECO:0000250|UniProtKB:Q9R216,
CC ECO:0000269|PubMed:12138115}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12138115};
CC Multi-pass membrane protein {ECO:0000255}. Note=Relocalizes DVL1 to the
CC cell membrane leading to phosphorylation of DVL1 and AXIN1
CC relocalization to the cell membrane. {ECO:0000269|PubMed:12138115}.
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 ZNRF3, leading to its degradation by the
CC proteasome. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family.
CC {ECO:0000305}.
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DR EMBL; AF455054; AAN03014.1; -; mRNA.
DR EMBL; DQ211688; ABB20593.1; -; mRNA.
DR EMBL; DQ211689; ABB20594.1; -; mRNA.
DR EMBL; AABR07035836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473973; EDM13380.1; -; Genomic_DNA.
DR RefSeq; NP_695217.1; NM_153305.1.
DR AlphaFoldDB; Q8K4C8; -.
DR SMR; Q8K4C8; -.
DR STRING; 10116.ENSRNOP00000001973; -.
DR PaxDb; Q8K4C8; -.
DR PRIDE; Q8K4C8; -.
DR Ensembl; ENSRNOT00000001973; ENSRNOP00000001973; ENSRNOG00000001452.
DR GeneID; 266608; -.
DR KEGG; rno:266608; -.
DR UCSC; RGD:628817; rat.
DR CTD; 8326; -.
DR RGD; 628817; Fzd9.
DR eggNOG; KOG3577; Eukaryota.
DR GeneTree; ENSGT00940000161226; -.
DR HOGENOM; CLU_007873_2_1_1; -.
DR InParanoid; Q8K4C8; -.
DR OMA; CEGIGYN; -.
DR OrthoDB; 509772at2759; -.
DR PhylomeDB; Q8K4C8; -.
DR TreeFam; TF317907; -.
DR PRO; PR:Q8K4C8; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Proteomes; UP000234681; Chromosome 12.
DR Bgee; ENSRNOG00000001452; Expressed in skeletal muscle tissue and 14 other tissues.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031527; C:filopodium membrane; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0042813; F:Wnt receptor activity; IDA:RGD.
DR GO; GO:0017147; F:Wnt-protein binding; ISO:RGD.
DR GO; GO:0030183; P:B cell differentiation; ISO:RGD.
DR GO; GO:1990523; P:bone regeneration; ISS:UniProtKB.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0007611; P:learning or memory; ISO:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:1904394; P:negative regulation of skeletal muscle acetylcholine-gated channel clustering; ISS:UniProtKB.
DR GO; GO:0007405; P:neuroblast proliferation; ISO:RGD.
DR GO; GO:0001503; P:ossification; ISS:UniProtKB.
DR GO; GO:0030501; P:positive regulation of bone mineralization; ISS:UniProtKB.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; ISS:UniProtKB.
DR GO; GO:0099173; P:postsynapse organization; IDA:SynGO.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0099566; P:regulation of postsynaptic cytosolic calcium ion concentration; IDA:SynGO.
DR GO; GO:1904393; P:regulation of skeletal muscle acetylcholine-gated channel clustering; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IDA:RGD.
DR CDD; cd07463; CRD_FZ9; 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; IPR041777; FZ9_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; Developmental protein; Disulfide bond;
KW G-protein coupled receptor; Membrane; Receptor; Reference proteome; Signal;
KW Transducer; Transmembrane; Transmembrane helix; Ubl conjugation;
KW Wnt signaling pathway.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..592
FT /note="Frizzled-9"
FT /id="PRO_5008178514"
FT TOPO_DOM 24..230
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..267
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..314
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 336..356
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 378..401
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..448
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..469
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 470..509
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 510..530
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 531..592
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..156
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT REGION 59..173
FT /note="Required for Wnt-activated receptor activity"
FT /evidence="ECO:0000269|PubMed:12138115"
FT REGION 555..592
FT /note="Required for CTNNB1 accumulation and TCF
FT transcription factor activity"
FT /evidence="ECO:0000269|PubMed:12138115"
FT MOTIF 533..538
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 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..140
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 592 AA; 64965 MW; 71B2D4F8DF3234CE CRC64;
MAVPPLLRGA LLLWQLLATG GAALEIGRFD PERGRGPAPC QAMEIPMCRG IGYNLTRMPN
LLGHTSQGEA AAQLAEFSPL VQYGCHSHLR FFLCSLYAPM CTDQVSTPIP ACRPMCEQAR
LRCAPIMEQF NFGWPDSLDC ARLPTRNDPH ALCMEAPENA TAGPTEPHKG LGMLPVAPRP
ARPPGDSAPG PGSGGTCDNP EKFQYVEKSR SCAPRCGPGV EVFWSRRDKD FALVWMAVWS
ALCFFSTAFT VFTFLLEPHR FQYPERPIIF LSMCYNVYSL AFLIRAVAGA QSVACDQEAG
ALYVIQEGLE NTGCTLVFLL LYYFGMASSL WWVVLTLTWF LAAGKKWGHE AIEAHGSYFH
MAAWGLPALK TIVVLTLRKV AGDELTGLCY VASMDPAALT GFVLVPLSCY LVLGTSFLLT
GFVALFHIRK IMKTGGTNTE KLEKLMVKIG VFSILYTVPA TCVIVCYVYE RLNMDFWRLR
ATEQPCTAAA VPGGRRDCSL PGGSVPTVAV FMLKIFMSLV VGITSGVWVW SSKTFQTWQS
LCYRKMAAGR ARAKACRTPG GYGRGTHCHY KAPTVVLHMT KTDPSLENPT HL
