ID   DKK1_HUMAN              Reviewed;         266 AA.
AC   O94907; B2RC19;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 197.
DE   RecName: Full=Dickkopf-related protein 1;
DE            Short=Dickkopf-1;
DE            Short=Dkk-1;
DE            Short=hDkk-1;
DE   AltName: Full=SK;
DE   Flags: Precursor;
GN   Name=DKK1; ORFNames=UNQ492/PRO1008;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leiomyosarcoma;
RX   PubMed=10383463; DOI=10.1074/jbc.274.27.19465;
RA   Fedi P., Bafico A., Nieto Soria A., Burgess W.H., Miki T., Bottaro D.P.,
RA   Kraus M.H., Aaronson S.A.;
RT   "Isolation and biochemical characterization of the human Dkk-1 homologue, a
RT   novel inhibitor of mammalian Wnt signaling.";
RL   J. Biol. Chem. 274:19465-19472(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Fetal kidney;
RX   PubMed=10570958; DOI=10.1016/s0378-1119(99)00365-0;
RA   Krupnik V.E., Sharp J.D., Jiang C., Robison K., Chickering T.W.,
RA   Amaravadi L., Brown D.E., Guyot D., Mays G., Leiby K., Chang B., Duong T.,
RA   Goodearl A.D.J., Gearing D.P., Sokol S.Y., McCarthy S.A.;
RT   "Functional and structural diversity of the human Dickkopf gene family.";
RL   Gene 238:301-313(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Tate G., Suzuki T., Mitsuya T.;
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10965128; DOI=10.1159/000015618;
RA   Roessler E., Du Y., Glinka A., Dutra A., Niehrs C., Muenke M.;
RT   "The genomic structure, chromosome location, and analysis of the human DKK1
RT   head inducer gene as a candidate for holoprosencephaly.";
RL   Cytogenet. Cell Genet. 89:220-224(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Cerebellum;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   PROTEIN SEQUENCE OF 32-46.
RX   PubMed=15340161; DOI=10.1110/ps.04682504;
RA   Zhang Z., Henzel W.J.;
RT   "Signal peptide prediction based on analysis of experimentally verified
RT   cleavage sites.";
RL   Protein Sci. 13:2819-2824(2004).
RN   [10]
RP   INTERACTION WITH LRP6.
RX   PubMed=11448771; DOI=10.1016/s0960-9822(01)00290-1;
RA   Semenov M.V., Tamai K., Brott B.K., Kuhl M., Sokol S., He X.;
RT   "Head inducer Dickkopf-1 is a ligand for Wnt coreceptor LRP6.";
RL   Curr. Biol. 11:951-961(2001).
RN   [11]
RP   REVIEW OF THE DKK FAMILY, AND FUNCTION.
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).
RN   [12]
RP   INTERACTION WITH LRP6 AND KREM1.
RX   PubMed=17804805; DOI=10.1073/pnas.0702305104;
RA   Binnerts M.E., Kim K.A., Bright J.M., Patel S.M., Tran K., Zhou M.,
RA   Leung J.M., Liu Y., Lomas W.E. III, Dixon M., Hazell S.A., Wagle M.,
RA   Nie W.S., Tomasevic N., Williams J., Zhan X., Levy M.D., Funk W.D., Abo A.;
RT   "R-Spondin1 regulates Wnt signaling by inhibiting internalization of
RT   LRP6.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:14700-14705(2007).
RN   [13]
RP   INTERACTION WITH LRP5.
RX   PubMed=19746449; DOI=10.1002/jcb.22335;
RA   Murrills R.J., Matteo J.J., Bhat B.M., Coleburn V.E., Allen K.M., Chen W.,
RA   Damagnez V., Bhat R.A., Bex F.J., Bodine P.V.;
RT   "A cell-based Dkk1 binding assay reveals roles for extracellular domains of
RT   LRP5 in Dkk1 interaction and highlights differences between wild-type and
RT   the high bone mass mutant LRP5(G171V).";
RL   J. Cell. Biochem. 108:1066-1075(2009).
RN   [14]
RP   INTERACTION WITH LRP6.
RX   PubMed=20093360; DOI=10.1074/jbc.m109.092130;
RA   Bourhis E., Tam C., Franke Y., Bazan J.F., Ernst J., Hwang J., Costa M.,
RA   Cochran A.G., Hannoush R.N.;
RT   "Reconstitution of a frizzled8.Wnt3a.LRP6 signaling complex reveals
RT   multiple Wnt and Dkk1 binding sites on LRP6.";
RL   J. Biol. Chem. 285:9172-9179(2010).
RN   [15]
RP   GLYCOSYLATION AT SER-61 AND ASN-256, AND DISULFIDE BONDS.
RX   PubMed=21805521; DOI=10.1002/pro.705;
RA   Haniu M., Horan T., Spahr C., Hui J., Fan W., Chen C., Richards W.G.,
RA   Lu H.S.;
RT   "Human Dickkopf-1 (huDKK1) protein: characterization of glycosylation and
RT   determination of disulfide linkages in the two cysteine-rich domains.";
RL   Protein Sci. 20:1802-1813(2011).
RN   [16]
RP   IDENTIFICATION IN A TERNARY COMPLEX WITH KREM1 AND LRP6.
RX   PubMed=27524201; DOI=10.1016/j.str.2016.06.020;
RA   Zebisch M., Jackson V.A., Zhao Y., Jones E.Y.;
RT   "Structure of the dual-mode wnt regulator Kremen1 and insight into ternary
RT   complex formation with LRP6 and Dickkopf.";
RL   Structure 24:1599-1605(2016).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 178-266 IN COMPLEX WITH LRP6,
RP   FUNCTION, AND DISULFIDE BONDS.
RX   PubMed=22000856; DOI=10.1016/j.devcel.2011.09.003;
RA   Ahn V.E., Chu M.L., Choi H.J., Tran D., Abo A., Weis W.I.;
RT   "Structural basis of Wnt signaling inhibition by Dickkopf binding to
RT   LRP5/6.";
RL   Dev. Cell 21:862-873(2011).
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       (PubMed:22000856). DKKs play an important role in vertebrate
CC       development, where they locally inhibit Wnt regulated processes such as
CC       antero-posterior axial patterning, limb development, somitogenesis and
CC       eye formation. In the adult, Dkks are implicated in bone formation and
CC       bone disease, cancer and Alzheimer disease (PubMed:17143291). Inhibits
CC       the pro-apoptotic function of KREMEN1 in a Wnt-independent manner, and
CC       has anti-apoptotic activity (By similarity).
CC       {ECO:0000250|UniProtKB:O54908, ECO:0000269|PubMed:22000856,
CC       ECO:0000303|PubMed:17143291}.
CC   -!- SUBUNIT: Interacts with LRP6 (PubMed:11448771, PubMed:17804805,
CC       PubMed:20093360, PubMed:22000856). Interacts (via the C-termianl Cys-
CC       rich domain) with LRP5 (via beta-propeller regions 3 and 4); the
CC       interaction, enhanced by MESD and or KREMEN, antagonizes Wnt-mediated
CC       signaling (PubMed:19746449). Forms a ternary complex with LRP6 and
CC       KREM1 (PubMed:27524201). Interacts with KREM1 (PubMed:17804805).
CC       {ECO:0000269|PubMed:11448771, ECO:0000269|PubMed:17804805,
CC       ECO:0000269|PubMed:19746449, ECO:0000269|PubMed:20093360,
CC       ECO:0000269|PubMed:22000856, ECO:0000269|PubMed:27524201}.
CC   -!- INTERACTION:
CC       O94907; Q96MU8: KREMEN1; NbExp=3; IntAct=EBI-742864, EBI-15656184;
CC       O94907; O75581: LRP6; NbExp=16; IntAct=EBI-742864, EBI-910915;
CC       O94907; Q99750: MDFI; NbExp=4; IntAct=EBI-742864, EBI-724076;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Placenta.
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}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/44007/DKK1";
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DR   EMBL; AF127563; AAD21087.1; -; mRNA.
DR   EMBL; AF177394; AAF02674.1; -; mRNA.
DR   EMBL; AB020315; BAA34651.1; -; Genomic_DNA.
DR   EMBL; AF261158; AAG15544.1; -; Genomic_DNA.
DR   EMBL; AF261157; AAG15544.1; JOINED; Genomic_DNA.
DR   EMBL; AY359005; AAQ89364.1; -; mRNA.
DR   EMBL; AK314902; BAG37416.1; -; mRNA.
DR   EMBL; CH471083; EAW54144.1; -; Genomic_DNA.
DR   EMBL; BC001539; AAH01539.1; -; mRNA.
DR   CCDS; CCDS7246.1; -.
DR   RefSeq; NP_036374.1; NM_012242.2.
DR   PDB; 3S2K; X-ray; 2.80 A; C=178-266.
DR   PDB; 3S8V; X-ray; 3.10 A; X=183-266.
DR   PDB; 3SOQ; X-ray; 1.90 A; Z=38-44.
DR   PDB; 5FWW; X-ray; 3.50 A; C=182-266.
DR   PDB; 5GJE; EM; 21.00 A; C=182-266.
DR   PDBsum; 3S2K; -.
DR   PDBsum; 3S8V; -.
DR   PDBsum; 3SOQ; -.
DR   PDBsum; 5FWW; -.
DR   PDBsum; 5GJE; -.
DR   AlphaFoldDB; O94907; -.
DR   EMDB; EMD-9501; -.
DR   SMR; O94907; -.
DR   BioGRID; 116599; 24.
DR   CORUM; O94907; -.
DR   DIP; DIP-46461N; -.
DR   ELM; O94907; -.
DR   IntAct; O94907; 13.
DR   MINT; O94907; -.
DR   STRING; 9606.ENSP00000363081; -.
DR   BindingDB; O94907; -.
DR   ChEMBL; CHEMBL6024; -.
DR   GlyCosmos; O94907; 2 sites, No reported glycans.
DR   GlyGen; O94907; 18 sites, 1 O-linked glycan (13 sites).
DR   iPTMnet; O94907; -.
DR   PhosphoSitePlus; O94907; -.
DR   BioMuta; DKK1; -.
DR   EPD; O94907; -.
DR   jPOST; O94907; -.
DR   MassIVE; O94907; -.
DR   MaxQB; O94907; -.
DR   PaxDb; 9606-ENSP00000363081; -.
DR   PeptideAtlas; O94907; -.
DR   ProteomicsDB; 50543; -.
DR   ABCD; O94907; 269 sequenced antibodies.
DR   Antibodypedia; 4049; 1102 antibodies from 48 providers.
DR   DNASU; 22943; -.
DR   Ensembl; ENST00000373970.4; ENSP00000363081.3; ENSG00000107984.10.
DR   GeneID; 22943; -.
DR   KEGG; hsa:22943; -.
DR   MANE-Select; ENST00000373970.4; ENSP00000363081.3; NM_012242.4; NP_036374.1.
DR   UCSC; uc001jjr.4; human.
DR   AGR; HGNC:2891; -.
DR   CTD; 22943; -.
DR   DisGeNET; 22943; -.
DR   GeneCards; DKK1; -.
DR   HGNC; HGNC:2891; DKK1.
DR   HPA; ENSG00000107984; Tissue enhanced (cervix, placenta).
DR   MalaCards; DKK1; -.
DR   MIM; 605189; gene.
DR   neXtProt; NX_O94907; -.
DR   OpenTargets; ENSG00000107984; -.
DR   Orphanet; 268882; Arnold-Chiari malformation type I.
DR   Orphanet; 85193; Idiopathic juvenile osteoporosis.
DR   PharmGKB; PA27345; -.
DR   VEuPathDB; HostDB:ENSG00000107984; -.
DR   eggNOG; KOG1218; Eukaryota.
DR   GeneTree; ENSGT00940000161319; -.
DR   HOGENOM; CLU_080459_0_0_1; -.
DR   InParanoid; O94907; -.
DR   OMA; LDNYQPY; -.
DR   OrthoDB; 4329885at2759; -.
DR   PhylomeDB; O94907; -.
DR   TreeFam; TF330916; -.
DR   PathwayCommons; O94907; -.
DR   Reactome; R-HSA-201681; TCF dependent signaling in response to WNT.
DR   Reactome; R-HSA-3772470; Negative regulation of TCF-dependent signaling by WNT ligand antagonists.
DR   Reactome; R-HSA-5339717; Signaling by LRP5 mutants.
DR   SignaLink; O94907; -.
DR   SIGNOR; O94907; -.
DR   BioGRID-ORCS; 22943; 14 hits in 1150 CRISPR screens.
DR   ChiTaRS; DKK1; human.
DR   GeneWiki; DKK1; -.
DR   GenomeRNAi; 22943; -.
DR   Pharos; O94907; Tchem.
DR   PRO; PR:O94907; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; O94907; Protein.
DR   Bgee; ENSG00000107984; Expressed in decidua and 125 other cell types or tissues.
DR   ExpressionAtlas; O94907; baseline and differential.
DR   GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0039706; F:co-receptor binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0008083; F:growth factor activity; TAS:ProtInc.
DR   GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IDA:MGI.
DR   GO; GO:0048019; F:receptor antagonist activity; IDA:BHF-UCL.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR   GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR   GO; GO:0030326; P:embryonic limb morphogenesis; IEA:Ensembl.
DR   GO; GO:0003197; P:endocardial cushion development; ISS:BHF-UCL.
DR   GO; GO:0001706; P:endoderm formation; IEA:Ensembl.
DR   GO; GO:0060325; P:face morphogenesis; IEA:Ensembl.
DR   GO; GO:0030900; P:forebrain development; IEA:Ensembl.
DR   GO; GO:0001942; P:hair follicle development; IEA:Ensembl.
DR   GO; GO:0003129; P:heart induction; ISS:BHF-UCL.
DR   GO; GO:0003170; P:heart valve development; ISS:BHF-UCL.
DR   GO; GO:0007611; P:learning or memory; ISS:ARUK-UCL.
DR   GO; GO:0060173; P:limb development; ISS:UniProtKB.
DR   GO; GO:0001707; P:mesoderm formation; IEA:Ensembl.
DR   GO; GO:0061743; P:motor learning; IEA:Ensembl.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0030514; P:negative regulation of BMP signaling pathway; IEA:Ensembl.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:ParkinsonsUK-UCL.
DR   GO; GO:2000726; P:negative regulation of cardiac muscle cell differentiation; IDA:BHF-UCL.
DR   GO; GO:0042662; P:negative regulation of mesodermal cell fate specification; IDA:BHF-UCL.
DR   GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
DR   GO; GO:0030279; P:negative regulation of ossification; ISS:UniProtKB.
DR   GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IDA:BHF-UCL.
DR   GO; GO:1905607; P:negative regulation of presynapse assembly; IEA:Ensembl.
DR   GO; GO:0032091; P:negative regulation of protein binding; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0060392; P:negative regulation of SMAD protein signal transduction; IDA:BHF-UCL.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR   GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IDA:UniProtKB.
DR   GO; GO:1904723; P:negative regulation of Wnt-Frizzled-LRP5/6 complex assembly; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0010628; P:positive regulation of gene expression; IGI:ARUK-UCL.
DR   GO; GO:0046330; P:positive regulation of JNK cascade; IDA:ARUK-UCL.
DR   GO; GO:1904958; P:positive regulation of midbrain dopaminergic neuron differentiation; IEA:Ensembl.
DR   GO; GO:0045813; P:positive regulation of Wnt signaling pathway, calcium modulating pathway; TAS:ARUK-UCL.
DR   GO; GO:2000096; P:positive regulation of Wnt signaling pathway, planar cell polarity pathway; TAS:ARUK-UCL.
DR   GO; GO:1904338; P:regulation of dopaminergic neuron differentiation; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0042663; P:regulation of endodermal cell fate specification; IDA:BHF-UCL.
DR   GO; GO:0043523; P:regulation of neuron apoptotic process; ISS:ARUK-UCL.
DR   GO; GO:0002090; P:regulation of receptor internalization; IDA:BHF-UCL.
DR   GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IEA:Ensembl.
DR   GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
DR   GO; GO:0098883; P:synapse pruning; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0090244; P:Wnt signaling pathway involved in somitogenesis; IEA:Ensembl.
DR   CDD; cd23272; Dkk1_Cys2; 1.
DR   CDD; cd23026; Dkk1_N_Cys1; 1.
DR   DisProt; DP01335; -.
DR   Gene3D; 2.10.80.10; Lipase, subunit A; 1.
DR   IDEAL; IID00532; -.
DR   InterPro; IPR006796; Dickkopf_N.
DR   InterPro; IPR048500; DIKK1/2/4_C-subdom1.
DR   InterPro; IPR048499; DIKK1/2/4_C-subdom2.
DR   InterPro; IPR039863; DKK1-4.
DR   InterPro; IPR047304; Dkk1_Cys2.
DR   InterPro; IPR047305; Dkk1_N.
DR   PANTHER; PTHR12113:SF11; DICKKOPF-RELATED PROTEIN 1; 1.
DR   PANTHER; PTHR12113; DICKKOPF3-LIKE 3; 1.
DR   Pfam; PF04706; Dickkopf_N; 1.
DR   Pfam; PF21481; DIKK1-2-4_C-subdom1; 1.
DR   Pfam; PF21479; DIKK1-2-4_C-subdom2; 1.
DR   Genevisible; O94907; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Developmental protein; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Reference proteome; Secreted; Signal;
KW   Wnt signaling pathway.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000269|PubMed:15340161"
FT   CHAIN           32..266
FT                   /note="Dickkopf-related protein 1"
FT                   /id="PRO_0000007218"
FT   REGION          85..138
FT                   /note="DKK-type Cys-1"
FT   REGION          189..263
FT                   /note="DKK-type Cys-2"
FT   CARBOHYD        61
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000269|PubMed:21805521"
FT   CARBOHYD        256
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:21805521"
FT   DISULFID        85..97
FT   DISULFID        91..111
FT   DISULFID        114..128
FT   DISULFID        121..133
FT   DISULFID        127..138
FT   DISULFID        189..201
FT   DISULFID        195..210
FT   DISULFID        200..237
FT   DISULFID        220..245
FT   DISULFID        239..263
FT   HELIX           192..194
FT                   /evidence="ECO:0007829|PDB:3S2K"
FT   STRAND          199..204
FT                   /evidence="ECO:0007829|PDB:3S2K"
FT   STRAND          207..212
FT                   /evidence="ECO:0007829|PDB:3S2K"
FT   STRAND          218..220
FT                   /evidence="ECO:0007829|PDB:5FWW"
FT   HELIX           226..231
FT                   /evidence="ECO:0007829|PDB:3S2K"
FT   STRAND          243..247
FT                   /evidence="ECO:0007829|PDB:3S2K"
FT   STRAND          261..265
FT                   /evidence="ECO:0007829|PDB:3S2K"
SQ   SEQUENCE   266 AA;  28672 MW;  5E878B2CCE4236BA CRC64;
     MMALGAAGAT RVFVAMVAAA LGGHPLLGVS ATLNSVLNSN AIKNLPPPLG GAAGHPGSAV
     SAAPGILYPG GNKYQTIDNY QPYPCAEDEE CGTDEYCASP TRGGDAGVQI CLACRKRRKR
     CMRHAMCCPG NYCKNGICVS SDQNHFRGEI EETITESFGN DHSTLDGYSR RTTLSSKMYH
     TKGQEGSVCL RSSDCASGLC CARHFWSKIC KPVLKEGQVC TKHRRKGSHG LEIFQRCYCG
     EGLSCRIQKD HHQASNSSRL HTCQRH
//