DKK1_HUMAN
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 03-AUG-2022, entry version 188.
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; O75581: LRP6; NbExp=15; 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="http://atlasgeneticsoncology.org/Genes/DKK1ID44007ch10q11.html";
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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 SMR; O94907; -.
DR BioGRID; 116599; 21.
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 GlyGen; O94907; 6 sites.
DR iPTMnet; O94907; -.
DR PhosphoSitePlus; O94907; -.
DR BioMuta; DKK1; -.
DR EPD; O94907; -.
DR jPOST; O94907; -.
DR MassIVE; O94907; -.
DR MaxQB; O94907; -.
DR PaxDb; O94907; -.
DR PeptideAtlas; O94907; -.
DR PRIDE; O94907; -.
DR ProteomicsDB; 50543; -.
DR ABCD; O94907; 269 sequenced antibodies.
DR Antibodypedia; 4049; 971 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 CTD; 22943; -.
DR DisGeNET; 22943; -.
DR GeneCards; DKK1; -.
DR HGNC; HGNC:2891; DKK1.
DR HPA; ENSG00000107984; Tissue enhanced (cervix, placenta, urinary bladder).
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; 1139517at2759; -.
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 1072 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 124 other tissues.
DR ExpressionAtlas; O94907; baseline and differential.
DR Genevisible; O94907; HS.
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:0000904; P:cell morphogenesis involved in differentiation; IEA:Ensembl.
DR GO; GO:0030326; P:embryonic limb morphogenesis; IEA:Ensembl.
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: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:1901296; P:negative regulation of canonical Wnt signaling pathway involved in cardiac muscle cell fate commitment; IDA:BHF-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:0060394; P:negative regulation of pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
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: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:0010942; P:positive regulation of cell death; TAS:ARUK-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:ARUK-UCL.
DR GO; GO:0090082; P:positive regulation of heart induction by negative regulation of canonical Wnt signaling pathway; ISS:BHF-UCL.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; IDA:ARUK-UCL.
DR GO; GO:1904958; P:positive regulation of midbrain dopaminergic neuron differentiation; IEA:Ensembl.
DR GO; GO:1901216; P:positive regulation of neuron death; ISS:ARUK-UCL.
DR GO; GO:1902949; P:positive regulation of tau-protein kinase activity; ISS:ARUK-UCL.
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: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 DisProt; DP01335; -.
DR IDEAL; IID00532; -.
DR InterPro; IPR006796; Dickkopf_N.
DR InterPro; IPR039863; DKK-like.
DR PANTHER; PTHR12113; PTHR12113; 1.
DR Pfam; PF04706; Dickkopf_N; 1.
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
