Q09163 (DLK1_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 16, 2012.
Version 114.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Protein delta homolog 1 Short name=DLK-1 Alternative name(s): Adipocyte differentiation inhibitor protein Preadipocyte factor 1 Short name=Pref-1 Cleaved into the following chain:
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| Gene names |
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| Organism | Mus musculus (Mouse) | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus |
Protein attributes
| Sequence length | 385 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | May have a role in neuroendocrine differentiation. Inhibits adipocyte differentiation. Ref.1 Ref.2 |
| Subunit structure | Monomer. |
| Subcellular location | |
| Tissue specificity | Highly expressed in fetal liver, placenta, adult adrenal gland, brain, testis and ovary and, to a lesser degree, in adult kidney, muscle, thymus and heart. Ref.7 |
| Developmental stage | Expression is elevated in liver after birth but starts to decline around postnatal day 16. Ref.7 |
| Post-translational modification | N- and O-glycosylated. Ref.6 |
| Sequence similarities | Contains 6 EGF-like domains. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Membrane |
| Coding sequence diversity | Alternative splicing |
| Domain | EGF-like domain Repeat Signal Transmembrane Transmembrane helix |
| PTM | Disulfide bond Glycoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | embryonic skeletal system development Inferred from direct assay PubMed 19247431. Source: MGI negative regulation of Notch signaling pathwayInferred from genetic interaction PubMed 21419176. Source: MGI post-embryonic developmentInferred from direct assay PubMed 19247431. Source: MGI |
| Cellular component | external side of plasma membrane Inferred from direct assay PubMed 18988804. Source: MGI integral to membraneInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | calcium ion binding Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Alternative products
| This entry describes 6 isoforms produced by alternative splicing. [Align] [Select] Note: Additional isoforms seem to exist. | ||||||
| Isoform A (identifier: Q09163-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform B (identifier: Q09163-2) The sequence of this isoform differs from the canonical sequence as follows: 231-281: Missing. | ||||||
| Isoform C (identifier: Q09163-3) The sequence of this isoform differs from the canonical sequence as follows: 231-303: Missing. | ||||||
| Isoform C2 (identifier: Q09163-4) The sequence of this isoform differs from the canonical sequence as follows: 231-305: Missing. | ||||||
| Isoform D (identifier: Q09163-5) The sequence of this isoform differs from the canonical sequence as follows: 211-303: Missing. | ||||||
| Isoform D2 (identifier: Q09163-6) The sequence of this isoform differs from the canonical sequence as follows: 211-305: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 23 | 23 | By similarity | ||||||||
| Chain | 24 – 385 | 362 | Protein delta homolog 1 | PRO_0000007520 | |||||||
| Chain | 24 – 305 | 282 | Fetal antigen 1 | PRO_0000007521 | |||||||
Regions | |||||||||||
| Topological domain | 24 – 305 | 282 | Extracellular Potential | ||||||||
| Transmembrane | 306 – 329 | 24 | Helical; Potential | ||||||||
| Topological domain | 330 – 385 | 56 | Cytoplasmic Potential | ||||||||
| Domain | 24 – 55 | 32 | EGF-like 1 | ||||||||
| Domain | 53 – 86 | 34 | EGF-like 2 | ||||||||
| Domain | 88 – 125 | 38 | EGF-like 3 | ||||||||
| Domain | 127 – 168 | 42 | EGF-like 4 | ||||||||
| Domain | 172 – 208 | 37 | EGF-like 5 | ||||||||
| Domain | 210 – 247 | 38 | EGF-like 6 | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 94 | 1 | O-linked (GalNAc...) Ref.6 | CAR_000160 | |||||||
| Glycosylation | 100 | 1 | N-linked (GlcNAc...) Ref.6 | CAR_000183 | |||||||
| Glycosylation | 165 | 1 | N-linked (GlcNAc...); partial; atypical Ref.6 | ||||||||
| Glycosylation | 174 | 1 | N-linked (GlcNAc...); atypical Ref.6 | ||||||||
| Glycosylation | 216 | 1 | O-linked (GalNAc...) Ref.6 | CAR_000161 | |||||||
| Glycosylation | 224 | 1 | O-linked (GalNAc...) Ref.6 | CAR_000162 | |||||||
| Glycosylation | 258 | 1 | O-linked (GalNAc...) Ref.6 | ||||||||
| Glycosylation | 267 | 1 | O-linked (GalNAc...); partial Ref.6 | ||||||||
| Glycosylation | 271 | 1 | O-linked (GalNAc...) Ref.6 | ||||||||
| Glycosylation | 295 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 26 ↔ 37 | By similarity | |||||||||
| Disulfide bond | 30 ↔ 43 | By similarity | |||||||||
| Disulfide bond | 45 ↔ 54 | By similarity | |||||||||
| Disulfide bond | 57 ↔ 68 | By similarity | |||||||||
| Disulfide bond | 63 ↔ 74 | By similarity | |||||||||
| Disulfide bond | 76 ↔ 85 | By similarity | |||||||||
| Disulfide bond | 92 ↔ 103 | By similarity | |||||||||
| Disulfide bond | 97 ↔ 113 | By similarity | |||||||||
| Disulfide bond | 115 ↔ 124 | By similarity | |||||||||
| Disulfide bond | 131 ↔ 144 | By similarity | |||||||||
| Disulfide bond | 138 ↔ 156 | By similarity | |||||||||
| Disulfide bond | 158 ↔ 167 | By similarity | |||||||||
| Disulfide bond | 176 ↔ 187 | By similarity | |||||||||
| Disulfide bond | 181 ↔ 196 | By similarity | |||||||||
| Disulfide bond | 198 ↔ 207 | By similarity | |||||||||
| Disulfide bond | 214 ↔ 225 | By similarity | |||||||||
| Disulfide bond | 219 ↔ 235 | By similarity | |||||||||
| Disulfide bond | 237 ↔ 246 | By similarity | |||||||||
Natural variations | |||||||||||
| Alternative sequence | 211 – 305 | 95 | Missing in isoform D2. | VSP_001379 | |||||||
| Alternative sequence | 211 – 303 | 93 | Missing in isoform D. | VSP_001378 | |||||||
| Alternative sequence | 231 – 305 | 75 | Missing in isoform C2. | VSP_001382 | |||||||
| Alternative sequence | 231 – 303 | 73 | Missing in isoform C. | VSP_001381 | |||||||
| Alternative sequence | 231 – 281 | 51 | Missing in isoform B. | VSP_001380 | |||||||
| Natural variant | 347 | 1 | Missing. Ref.3 | ||||||||
Experimental info | |||||||||||
| Sequence conflict | 250 | 1 | R → P in AAA37175. Ref.2 | ||||||||
| Sequence conflict | 320 – 385 | 66 | VLGTV…GDEEI → CWAPWPSSFSTSAKPGCPTC ATTTCFARRRTSCCSITAAR SWRSISSSPRRLT in AAA37175. Ref.2 | ||||||||
| Sequence conflict | 344 – 345 | 2 | TF → ML in BAA04121. Ref.4 | ||||||||
Sequences
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References
| [1] | "dlk, a putative mammalian homeotic gene differentially expressed in small cell lung carcinoma and neuroendocrine tumor cell line." Laborda J., Sausville E.A., Hoffman T., Notario V. J. Biol. Chem. 268:3817-3820(1993) [PubMed: 8095043] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION. Strain: Swiss. Tissue: Fibroblast. |
| [2] | "Pref-1, a protein containing EGF-like repeats, inhibits adipocyte differentiation." Smas C.M., Sul H.S. Cell 73:725-734(1993) [PubMed: 8500166] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION. |
| [3] | "dlk, pG2 and Pref-1 mRNAs encode similar proteins belonging to the EGF-like superfamily. Identification of polymorphic variants of this RNA." Lee Y.L., Helman L., Hoffman T., Laborda J. Biochim. Biophys. Acta 1261:223-232(1995) [PubMed: 7711066] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LYS-347 DEL. Tissue: Adrenal gland and Placenta. |
| [4] | Maruyama K., Nishijima S., Kuromitsu S., Ichikawa A., Masuda E., Takemoto T., Kodama H., Kawashima H. Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [5] | "Structural characterization and alternate splicing of the gene encoding the preadipocyte EGF-like protein pref-1." Smas C.M., Green D., Sul H.S. Biochemistry 33:9257-9265(1994) [PubMed: 7519443] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8, ALTERNATIVE SPLICING. |
| [6] | "Glycosylation analysis and protein structure determination of murine fetal antigen 1 (mFA1) -- the circulating gene product of the delta-like protein (dlk), preadipocyte factor 1 (Pref-1) and stromal-cell-derived protein 1 (SCP-1) cDNAs." Krogh T.N., Bachmann E., Teisner B., Skjoedt K., Hoejrup P. Eur. J. Biochem. 244:334-342(1997) [PubMed: 9118998] [Abstract] Cited for: GLYCOSYLATION AT SER-94; ASN-100; ASN-165; ASN-174; SER-216; THR-224; THR-258; THR-267 AND THR-271, STRUCTURE OF CARBOHYDRATE. |
| [7] | "The novel gene EGFL9/Dlk2, highly homologous to Dlk1, functions as a modulator of adipogenesis." Nueda M.L., Baladron V., Garcia-Ramirez J.J., Sanchez-Solana B., Ruvira M.D., Rivero S., Ballesteros M.A., Monsalve E.M., Diaz-Guerra M.J., Ruiz-Hidalgo M.J., Laborda J. J. Mol. Biol. 367:1270-1280(2007) [PubMed: 17320102] [Abstract] Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Z12171 mRNA. Translation: CAA78162.1. U15980 mRNA. Translation: AAB60495.1. L12721 mRNA. Translation: AAA37175.1. S71340 Genomic DNA. No translation available. D16847 mRNA. Translation: BAA04121.1. |
| IPI | IPI00121716. IPI00226664. IPI00226665. IPI00321359. IPI00918517. IPI01008291. |
| PIR | A54785. S53718. |
| RefSeq | NP_034182.2. NM_010052.5. |
| UniGene | Mm.157069. |
3D structure databases | |
| ProteinModelPortal | Q09163. |
| SMR | Q09163. Positions 28-251. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-6010N. |
| IntAct | Q09163. 1 interaction. |
| STRING | Q09163. |
PTM databases | |
| GlycoSuiteDB | Q09163. |
| PhosphoSite | Q09163. |
Proteomic databases | |
| PRIDE | Q09163. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 13386. |
| KEGG | mmu:13386. |
Organism-specific databases | |
| CTD | 8788. |
| MGI | MGI:94900. Dlk1. |
Phylogenomic databases | |
| eggNOG | NOG306005. |
| HOGENOM | HOG000072581. |
| HOVERGEN | HBG007065. |
| InParanoid | Q09163. |
| OrthoDB | EOG44MXS5. |
Gene expression databases | |
| ArrayExpress | Q09163. |
| CleanEx | MM_DLK1. |
| Genevestigator | Q09163. |
| GermOnline | ENSMUSG00000040856. Mus musculus. |
Family and domain databases | |
| InterPro | IPR000742. EG-like_dom. IPR006210. EGF-like. IPR001881. EGF-like_Ca-bd. IPR006209. EGF-like_dom. IPR013032. EGF-like_reg_CS. IPR000152. EGF-type_Asp/Asn_hydroxyl_site. [Graphical view] |
| Pfam | PF00008. EGF. 4 hits. [Graphical view] |
| SMART | SM00181. EGF. 5 hits. SM00179. EGF_CA. 1 hit. [Graphical view] |
| PROSITE | PS00010. ASX_HYDROXYL. 1 hit. PS00022. EGF_1. 5 hits. PS01186. EGF_2. 6 hits. PS50026. EGF_3. 6 hits. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 283744. |
| SOURCE | Search... |
Entry information
| Entry name | DLK1_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q09163 Secondary accession number(s): Q07645, Q62208 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with