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FZD6_CHICK
ID   FZD6_CHICK              Reviewed;         190 AA.
AC   Q9PTW1;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Frizzled-6;
DE            Short=Fz-6;
DE            Short=cFz-6;
DE   Flags: Fragment;
GN   Name=FZD6; Synonyms=FZ6;
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=10512196;
RA   Nohno T., Kawakami Y., Wada N., Komaguchi C., Nishimatsu S.;
RT   "Differential expression of the frizzled family involved in Wnt signaling
RT   during chick limb development.";
RL   Cell. Mol. Biol. 45:653-659(1999).
CC   -!- FUNCTION: Receptor for Wnt proteins. Most of frizzled receptors are
CC       coupled to the beta-catenin canonical signaling pathway, which leads to
CC       the activation of disheveled proteins, inhibition of GSK-3 kinase,
CC       nuclear accumulation of beta-catenin and activation of Wnt target
CC       genes. A second signaling pathway involving PKC and calcium fluxes has
CC       been seen for some family members, but it is not yet clear if it
CC       represents a distinct pathway or if it can be integrated in the
CC       canonical pathway, as PKC seems to be required for Wnt-mediated
CC       inactivation of GSK-3 kinase. Both pathways seem to involve
CC       interactions with G-proteins. Activation by Wnt5A stimulates PKC
CC       activity via a G-protein-dependent mechanism. Involved in transduction
CC       and intercellular transmission of polarity information during tissue
CC       morphogenesis and/or in differentiated tissues. Together with FZD3, may
CC       be involved in the neural tube closure and plays a role in the
CC       regulation of the establishment of planar cell polarity (PCP),
CC       particularly in the orientation of asymmetric bundles of stereocilia on
CC       the apical faces of a subset of auditory and vestibular sensory cells
CC       located in the inner ear (By similarity).
CC       {ECO:0000250|UniProtKB:Q61089}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q61089}; Multi-
CC       pass membrane protein {ECO:0000255}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q61089}; Multi-pass membrane protein
CC       {ECO:0000255}. Cell surface {ECO:0000250|UniProtKB:Q61089}. Apical cell
CC       membrane {ECO:0000250|UniProtKB:Q61089}; Multi-pass membrane protein
CC       {ECO:0000255}. Cytoplasmic vesicle membrane
CC       {ECO:0000250|UniProtKB:Q61089}; Multi-pass membrane protein
CC       {ECO:0000255}.
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; AB029452; BAA89402.1; -; mRNA.
DR   RefSeq; NP_001258860.1; NM_001271931.2.
DR   AlphaFoldDB; Q9PTW1; -.
DR   SMR; Q9PTW1; -.
DR   STRING; 9031.ENSGALP00000025843; -.
DR   PaxDb; Q9PTW1; -.
DR   GeneID; 378788; -.
DR   KEGG; gga:378788; -.
DR   CTD; 8323; -.
DR   VEuPathDB; HostDB:geneid_378788; -.
DR   eggNOG; KOG3577; Eukaryota.
DR   InParanoid; Q9PTW1; -.
DR   OrthoDB; 330751at2759; -.
DR   Proteomes; UP000000539; Unplaced.
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:0016021; C:integral component of membrane; IBA:GO_Central.
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:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   InterPro; IPR015526; Frizzled/SFRP.
DR   InterPro; IPR000539; Frizzled/Smoothened_TM.
DR   InterPro; IPR026543; FZD6.
DR   InterPro; IPR017981; GPCR_2-like.
DR   PANTHER; PTHR11309; PTHR11309; 1.
DR   PANTHER; PTHR11309:SF75; PTHR11309:SF75; 1.
DR   Pfam; PF01534; Frizzled; 1.
DR   PRINTS; PR00489; FRIZZLED.
DR   SMART; SM01330; Frizzled; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cytoplasmic vesicle; Developmental protein;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Neurogenesis; Receptor;
KW   Reference proteome; Transducer; Transmembrane; Transmembrane helix;
KW   Wnt signaling pathway.
FT   CHAIN           <1..>190
FT                   /note="Frizzled-6"
FT                   /id="PRO_0000205977"
FT   TOPO_DOM        <1..89
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        90..110
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        111..121
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        122..142
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        143..169
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..190
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          <1..20
FT                   /note="FZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   CARBOHYD        144
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
FT   NON_TER         190
SQ   SEQUENCE   190 AA;  21622 MW;  99C380C7712688D6 CRC64;
     FGFAWPEELE CSRLVNCDET APATAPVTTN AHGTQKTPGQ TRRDYGFWCP RHLHTSNGQG
     YKFLGIDQCA PPCPNMYFKN YELDVAKSFI GIVSIFCLCA TLFTFLTFLI DVKRFRYPER
     PIIYYSVCYS IVSLMYFIGF LLGNRTACNK ADDKLEIGET VVLGSQNKAC TVLFMVLYFF
     TMAGTIWWVI
 
 
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