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 02-OCT-2024, entry version 200. 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=18; 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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 15. 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 jPOST; O94907; -. DR MassIVE; O94907; -. DR PaxDb; 9606-ENSP00000363081; -. DR PeptideAtlas; O94907; -. DR ProteomicsDB; 50543; -. DR ABCD; O94907; 269 sequenced antibodies. DR Antibodypedia; 4049; 1074 antibodies from 47 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 EvolutionaryTrace; O94907; -. 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. PE 1: Evidence at protein level; KW 3D-structure; Developmental protein; Direct protein sequencing; KW Disulfide bond; Glycoprotein; Proteomics identification; KW Reference proteome; Secreted; Signal; 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 //