ID   DKK3_CHICK              Reviewed;         350 AA.
AC   Q90839;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Dickkopf-related protein 3;
DE            Short=Dickkopf-3;
DE            Short=Dkk-3;
DE   AltName: Full=Lens fiber protein CLFEST4;
DE   Flags: Precursor;
GN   Name=DKK3;
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=Lens fibers;
RX   PubMed=8840185;
RA   Sawada K., Agata K., Eguchi G.;
RT   "Characterization of terminally differentiated cell state by categorizing
RT   cDNA clones derived from chicken lens fibers.";
RL   Int. J. Dev. Biol. 40:531-535(1996).
RN   [2]
RP   REVIEW OF THE DKK FAMILY.
RX   PubMed=17143291; DOI=10.1038/sj.onc.1210054;
RA   Niehrs C.;
RT   "Function and biological roles of the Dickkopf family of Wnt modulators.";
RL   Oncogene 25:7469-7481(2006).
CC   -!- FUNCTION: Antagonizes canonical Wnt signaling by inhibiting LRP5/6
CC       interaction with Wnt and by forming a ternary complex with the
CC       transmembrane protein KREMEN that promotes internalization of LRP5/6.
CC       DKKs play an important role in vertebrate development, where they
CC       locally inhibit Wnt regulated processes such as antero-posterior axial
CC       patterning, limb development, somitogenesis and eye formation. In the
CC       adult, Dkks are implicated in bone formation and bone disease, cancer
CC       and Alzheimer disease (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with LRP5 and LRP6. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in eye lens.
CC   -!- DOMAIN: The C-terminal cysteine-rich domain mediates interaction with
CC       LRP5 and LRP6. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the dickkopf family. {ECO:0000305}.
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DR   EMBL; D26311; BAA05373.1; -; mRNA.
DR   RefSeq; NP_990456.1; NM_205125.1.
DR   AlphaFoldDB; Q90839; -.
DR   SMR; Q90839; -.
DR   STRING; 9031.ENSGALP00000008890; -.
DR   PaxDb; Q90839; -.
DR   PRIDE; Q90839; -.
DR   GeneID; 396023; -.
DR   KEGG; gga:396023; -.
DR   CTD; 27122; -.
DR   VEuPathDB; HostDB:geneid_396023; -.
DR   eggNOG; KOG1218; Eukaryota.
DR   InParanoid; Q90839; -.
DR   OrthoDB; 1139517at2759; -.
DR   PhylomeDB; Q90839; -.
DR   PRO; PR:Q90839; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IEA:InterPro.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR006796; Dickkopf_N.
DR   InterPro; IPR039863; DKK-like.
DR   InterPro; IPR023569; Prokineticin_domain.
DR   PANTHER; PTHR12113; PTHR12113; 1.
DR   Pfam; PF04706; Dickkopf_N; 1.
DR   Pfam; PF06607; Prokineticin; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Developmental protein; Disulfide bond; Glycoprotein;
KW   Reference proteome; Secreted; Signal; Wnt signaling pathway.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..350
FT                   /note="Dickkopf-related protein 3"
FT                   /id="PRO_0000007224"
FT   REGION          139..187
FT                   /note="DKK-type Cys-1"
FT   REGION          200..277
FT                   /note="DKK-type Cys-2"
FT   REGION          329..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          33..78
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        196
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        282
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        200..212
FT                   /evidence="ECO:0000250"
FT   DISULFID        206..223
FT                   /evidence="ECO:0000250"
FT   DISULFID        211..257
FT                   /evidence="ECO:0000250"
FT   DISULFID        233..265
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   350 AA;  39209 MW;  57BE7ED850089DAE CRC64;
     MRRGEGPAPR RRWLLLLAVL AALCCAAAGS GGRRRAASLG EMLREVEALM EDTQHKLRNA
     VQEMEAEEEG AKKLSEVNFE NLPPTYHNES NTETRIGNKT VQTHQEIDKV TDNRTGSTIF
     SETIITSIKG GENKRNHECI IDEDCETGKY CQFSTFEYKC QPCKTQHTHC SRDVECCGDQ
     LCVWGECRKA TSRGENGTIC ENQHDCNPGT CCAFQKELLF PVCTPLPEEG EPCHDPSNRL
     LNLITWELEP DGVLERCPCA SGLICQPQSS HSTTSVCELS SNETRKNEKE DPLNMDEMPF
     ISLIPRDILS DYEESSVIQE VRKELESLED QAGVKSEHDP AHDLFLGDEI