FZD10_CHICK
ID FZD10_CHICK Reviewed; 585 AA.
AC Q9PWH2;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Frizzled-10;
DE Short=Fz-10;
DE Short=cFz-10;
DE Flags: Precursor;
GN Name=FZD10; Synonyms=FZ10;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Limb bud;
RX PubMed=10704868; DOI=10.1016/s0925-4773(99)00301-9;
RA Kawakami Y., Wada N., Nishimatsu S., Komaguchi C., Noji S., Nohno T.;
RT "Identification of chick frizzled-10 expressed in the developing limb and
RT the central nervous system.";
RL Mech. Dev. 91:375-378(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=10781956; DOI=10.1016/s0925-4773(00)00263-x;
RA Stark M.R., Biggs J.J., Schoenwolf G.C., Rao M.S.;
RT "Characterization of avian frizzled genes in cranial placode development.";
RL Mech. Dev. 93:195-200(2000).
RN [3]
RP FUNCTION, INTERACTION WITH WNT7A, AND SUBCELLULAR LOCATION.
RX PubMed=11142678; DOI=10.1046/j.1440-169x.2000.00545.x;
RA Kawakami Y., Wada N., Nishimatsu S., Nohno T.;
RT "Involvement of frizzled-10 in Wnt-7a signaling during chick limb
RT development.";
RL Dev. Growth Differ. 42:561-569(2000).
CC -!- FUNCTION: Receptor for Wnt proteins. Functions in the canonical
CC Wnt/beta-catenin signaling pathway. Activation by WNT7A induces
CC expression of beta-catenin target genes (PubMed:11142678). The
CC canonical Wnt/beta-catenin signaling pathway 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:11142678). A
CC second signaling pathway involving PKC and calcium fluxes has been seen
CC for some family members, but it is not yet clear if it represents a
CC distinct pathway or if it can be integrated in the canonical pathway,
CC as PKC seems to be required for Wnt-mediated inactivation of GSK-3
CC kinase. Both pathways seem to involve interactions with G-proteins. May
CC be involved in transduction and intercellular transmission of polarity
CC information during tissue morphogenesis and/or in differentiated
CC tissues (Probable). {ECO:0000269|PubMed:11142678, ECO:0000305}.
CC -!- SUBUNIT: Interacts with WNT7A. {ECO:0000269|PubMed:11142678}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:11142678};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the dorsal ectoderm overlying the
CC developing spinal cord.
CC -!- DEVELOPMENTAL STAGE: Expressed in the region posterior to the Hensen
CC node at stage 6. Detected in the dorsal domain of the neural tube and
CC the CNS of the developing embryo. In the developing limb, expression
CC starts at stage 18 in the posterior-dorsal region of the distal
CC mesenchyme, and gradually expands to the anterior-distal region. Also
CC found in the feather bud and branchial arch.
CC -!- INDUCTION: By Sonic hedgehog (Shh) in limb bud.
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 -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family.
CC {ECO:0000305}.
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DR EMBL; AB023806; BAA83742.1; -; mRNA.
DR EMBL; AF224320; AAF61100.1; -; mRNA.
DR RefSeq; NP_989429.1; NM_204098.2.
DR AlphaFoldDB; Q9PWH2; -.
DR SMR; Q9PWH2; -.
DR IntAct; Q9PWH2; 2.
DR STRING; 9031.ENSGALP00000038896; -.
DR PaxDb; Q9PWH2; -.
DR PRIDE; Q9PWH2; -.
DR GeneID; 373885; -.
DR KEGG; gga:373885; -.
DR CTD; 11211; -.
DR VEuPathDB; HostDB:geneid_373885; -.
DR eggNOG; KOG3577; Eukaryota.
DR InParanoid; Q9PWH2; -.
DR OrthoDB; 509772at2759; -.
DR PhylomeDB; Q9PWH2; -.
DR PRO; PR:Q9PWH2; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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; IBA:GO_Central.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0034260; P:negative regulation of GTPase activity; IEA:Ensembl.
DR GO; GO:0038031; P:non-canonical Wnt signaling pathway via JNK cascade; IEA:Ensembl.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:Ensembl.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; IEA:Ensembl.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IEA:Ensembl.
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; IPR026549; FZD10.
DR InterPro; IPR017981; GPCR_2-like.
DR PANTHER; PTHR11309; PTHR11309; 1.
DR PANTHER; PTHR11309:SF86; PTHR11309:SF86; 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 1: Evidence at protein level;
KW Cell membrane; Developmental protein; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix;
KW Wnt signaling pathway.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..585
FT /note="Frizzled-10"
FT /id="PRO_0000013007"
FT TOPO_DOM 25..229
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..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..355
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 377..397
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..418
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 419..447
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..468
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 469..506
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 507..527
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 528..585
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 33..154
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT REGION 155..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 530..535
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 CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 38..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 46..92
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 83..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 110..151
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 114..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 585 AA; 65945 MW; 3E2A7E747CF9EE4B CRC64;
MGPAAGNLVR AVLALCWLAE HCAGISSIDI ERPGDGRCQP IEIPMCKDIG YNMTRMPNLM
GHENQREAAI QLHEFAPLVE YGCHGHLKFF LCSLYAPMCT EQVSTPIPAC RVMCEQARLK
CSPIMEQFNF KWPDSLDCSK LPNKNDPNYL CMEAPNNGSD EPPRGSSMLP PMFRPQRPST
GHDLQQHKDS LSRTSCENPG KFHHVEKSAS CAPLCTPGVD VYWSKDDKQF AVIWIAIWSI
LCFFSSAFTV LTFLIDPQRF KYPERPIIFL SMCYCVYSVG YIIRLFSGAE SIACDRDSGQ
LYVIQEGLES TGCTIVFLVL YYFGMASSLW WVILTLTWFL AAGKKWGHEA IEANSSYFHL
AAWAIPAVKT IMILVMRRVA GDELTGLCYV GSMDVNALTG FVLIPLACYL IIGTSFILSG
FVALFHIRRV MKTGGENTDK LEKLMVRIGV FSVLYTVPAT CVIACYFYER LNMDYWKIVA
SQQKCKMNNQ TKNLDCMMNN SIPAVEIFMV KIFMLLVVGI TSGMWIWTSK TLQSWQNVCS
RRLKKRSRRK PASVITSSGI YKKPQHPQKT HLAKYESTLQ PPTCV
