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 27-MAR-2024, entry version 109.
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 GlyCosmos; Q90839; 5 sites, No reported glycans.
DR PaxDb; 9031-ENSGALP00000008890; -.
DR GeneID; 396023; -.
DR KEGG; gga:396023; -.
DR CTD; 27122; -.
DR VEuPathDB; HostDB:geneid_396023; -.
DR eggNOG; KOG1218; Eukaryota.
DR InParanoid; Q90839; -.
DR PhylomeDB; Q90839; -.
DR PRO; PR:Q90839; -.
DR Proteomes; UP000000539; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0039706; F:co-receptor binding; IBA:GO_Central.
DR GO; GO:0048019; F:receptor antagonist activity; IBA:GO_Central.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd23274; Dkk3_Cys2; 1.
DR CDD; cd23014; Dkk3_N_Cys1; 1.
DR Gene3D; 2.10.80.10; Lipase, subunit A; 1.
DR InterPro; IPR006796; Dickkopf_N.
DR InterPro; IPR039863; DKK1-4.
DR InterPro; IPR047300; Dkk3_Cys2.
DR InterPro; IPR047301; Dkk3_N.
DR InterPro; IPR023569; Prokineticin_domain.
DR PANTHER; PTHR12113:SF8; DICKKOPF-RELATED PROTEIN 3; 1.
DR PANTHER; PTHR12113; DICKKOPF3-LIKE 3; 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
//
