Q98931 (LRP8_CHICK) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 96.
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: Low-density lipoprotein receptor-related protein 8 Short name=LRP-8 Alternative name(s): Apolipoprotein E receptor 2 Protein LR8B | ||||
| Gene names |
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| Organism | Gallus gallus (Chicken) [Reference proteome] | ||||
| Taxonomic identifier | 9031 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus![]() |
Protein attributes
| Sequence length | 917 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 | Cell surface receptor for Reelin (RELN) and apolipoprotein E (apoE)-containing ligands. Also binds alpha2-macroglobulin. LRP8 participates in transmitting the extracellular Reelin signal to intracellular signaling processes, by binding to DAB1 on its cytoplasmic tail. Reelin acts via both the VLDL receptor (VLDLR) and LRP8 to regulate DAB1 tyrosine phosphorylation and microtubule function in neurons. LRP8 has higher affinity for Reelin than VLDLR. LRP8 is thus a key component of the Reelin pathway which governs neuronal layering of the forebrain during embryonic brain development By similarity. |
| Subunit structure | Reelin associates with two or more receptor molecules. Interacts with DAB1 and JNK-interacting proteins By similarity. Ref.2 |
| Subcellular location | Membrane; Single-pass type I membrane protein Potential. |
| Tissue specificity | Mainly in brain. |
| Post-translational modification | O-glycosylated By similarity. Tyrosine phosphorylated upon apoE binding By similarity. |
| Sequence similarities | Belongs to the LDLR family. Contains 2 EGF-like domains. Contains 7 LDL-receptor class A domains. Contains 5 LDL-receptor class B repeats. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Endocytosis |
| Cellular component | Membrane |
| Coding sequence diversity | Alternative splicing |
| Domain | EGF-like domain Repeat Signal Transmembrane Transmembrane helix |
| Ligand | Calcium |
| Molecular function | Receptor |
| PTM | Disulfide bond Glycoprotein Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | endocytosis Inferred from electronic annotation. Source: UniProtKB-KW ventral spinal cord developmentInferred from expression pattern PubMed 20711475. Source: UniProtKB |
| Cellular_component | integral to membrane Inferred 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 1 isoform produced by alternative splicing. [Select] Note: A number of isoforms are produced. | ||||||
| Isoform 1 (identifier: Q98931-1) 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. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 24 | 24 | Potential | ||||||||
| Chain | 25 – 917 | 893 | Low-density lipoprotein receptor-related protein 8 | PRO_0000017334 | |||||||
Regions | |||||||||||
| Topological domain | 25 – 838 | 814 | Extracellular Potential | ||||||||
| Transmembrane | 839 – 861 | 23 | Helical; Potential | ||||||||
| Topological domain | 862 – 917 | 56 | Cytoplasmic Potential | ||||||||
| Domain | 28 – 64 | 37 | LDL-receptor class A 1 | ||||||||
| Domain | 67 – 105 | 39 | LDL-receptor class A 2 | ||||||||
| Domain | 108 – 146 | 39 | LDL-receptor class A 3 | ||||||||
| Domain | 148 – 184 | 37 | LDL-receptor class A 4 | ||||||||
| Domain | 187 – 225 | 39 | LDL-receptor class A 5 | ||||||||
| Domain | 272 – 308 | 37 | LDL-receptor class A 6 | ||||||||
| Domain | 312 – 351 | 40 | LDL-receptor class A 7 | ||||||||
| Domain | 346 – 390 | 45 | EGF-like 1 | ||||||||
| Domain | 391 – 430 | 40 | EGF-like 2; calcium-binding Potential | ||||||||
| Repeat | 476 – 522 | 47 | LDL-receptor class B 1 | ||||||||
| Repeat | 523 – 565 | 43 | LDL-receptor class B 2 | ||||||||
| Repeat | 566 – 609 | 44 | LDL-receptor class B 3 | ||||||||
| Repeat | 610 – 652 | 43 | LDL-receptor class B 4 | ||||||||
| Repeat | 653 – 695 | 43 | LDL-receptor class B 5 | ||||||||
| Region | 754 – 813 | 60 | Clustered O-linked oligosaccharides | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 158 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 196 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 532 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 628 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 782 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 820 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 29 ↔ 41 | By similarity | |||||||||
| Disulfide bond | 36 ↔ 54 | By similarity | |||||||||
| Disulfide bond | 48 ↔ 63 | By similarity | |||||||||
| Disulfide bond | 68 ↔ 80 | By similarity | |||||||||
| Disulfide bond | 75 ↔ 93 | By similarity | |||||||||
| Disulfide bond | 87 ↔ 104 | By similarity | |||||||||
| Disulfide bond | 109 ↔ 123 | By similarity | |||||||||
| Disulfide bond | 116 ↔ 136 | By similarity | |||||||||
| Disulfide bond | 130 ↔ 145 | By similarity | |||||||||
| Disulfide bond | 149 ↔ 161 | By similarity | |||||||||
| Disulfide bond | 156 ↔ 174 | By similarity | |||||||||
| Disulfide bond | 168 ↔ 183 | By similarity | |||||||||
| Disulfide bond | 188 ↔ 200 | By similarity | |||||||||
| Disulfide bond | 195 ↔ 213 | By similarity | |||||||||
| Disulfide bond | 207 ↔ 224 | By similarity | |||||||||
| Disulfide bond | 234 ↔ 246 | By similarity | |||||||||
| Disulfide bond | 241 ↔ 259 | By similarity | |||||||||
| Disulfide bond | 253 ↔ 268 | By similarity | |||||||||
| Disulfide bond | 273 ↔ 285 | By similarity | |||||||||
| Disulfide bond | 280 ↔ 298 | By similarity | |||||||||
| Disulfide bond | 292 ↔ 307 | By similarity | |||||||||
| Disulfide bond | 313 ↔ 326 | By similarity | |||||||||
| Disulfide bond | 321 ↔ 339 | By similarity | |||||||||
| Disulfide bond | 333 ↔ 350 | By similarity | |||||||||
| Disulfide bond | 355 ↔ 366 | By similarity | |||||||||
| Disulfide bond | 362 ↔ 375 | By similarity | |||||||||
| Disulfide bond | 377 ↔ 389 | By similarity | |||||||||
| Disulfide bond | 395 ↔ 405 | By similarity | |||||||||
| Disulfide bond | 401 ↔ 414 | By similarity | |||||||||
| Disulfide bond | 416 ↔ 429 | By similarity | |||||||||
Sequences
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References
| [1] | "A new LDL receptor homologue with 8 ligand binding repeats in brain of chicken and mouse." Novak S., Hiesberger T., Schneider W.J., Nimpf J. J. Biol. Chem. 271:11732-11736(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: White leghorn. Tissue: Brain. |
| [2] | "Alternative splicing in the ligand binding domain of mouse ApoE receptor-2 produces receptor variants binding reelin but not alpha2-macroglobulin." Brandes C., Kahr L., Stockinger W., Hiesberger T., Schneider W.J., Nimpf J. J. Biol. Chem. 276:22160-22169(2001) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING, INTERACTION WITH ALPHA2-MACROGLOBULIN. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X97001 mRNA. Translation: CAA65729.1. |
| IPI | IPI00581287. |
| RefSeq | NP_990517.1. NM_205186.1. |
| UniGene | Gga.3461. |
3D structure databases | |
| ProteinModelPortal | Q98931. |
| SMR | Q98931. Positions 270-308, 351-432. |
| ModBase | Search... |
Proteomic databases | |
| PaxDb | Q98931. |
| PRIDE | Q98931. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 396102. |
| KEGG | gga:396102. |
Organism-specific databases | |
| CTD | 7804. |
Phylogenomic databases | |
| eggNOG | NOG255913. |
| HOGENOM | HOG000115656. |
| HOVERGEN | HBG006250. |
| InParanoid | Q98931. |
Family and domain databases | |
| Gene3D | 2.120.10.30. 1 hit. 4.10.400.10. 8 hits. |
| InterPro | IPR011042. 6-blade_b-propeller_TolB-like. IPR026823. cEGF. IPR000742. EG-like_dom. IPR001881. EGF-like_Ca-bd. IPR013032. EGF-like_CS. IPR000152. EGF-type_Asp/Asn_hydroxyl_site. IPR018097. EGF_Ca-bd_CS. IPR009030. Growth_fac_rcpt. IPR023415. LDLR_class-A_CS. IPR000033. LDLR_classB_rpt. IPR002172. LDrepeatLR_classA_rpt. [Graphical view] |
| Pfam | PF12662. cEGF. 1 hit. PF00057. Ldl_recept_a. 8 hits. PF00058. Ldl_recept_b. 5 hits. [Graphical view] |
| SMART | SM00181. EGF. 2 hits. SM00179. EGF_CA. 1 hit. SM00192. LDLa. 8 hits. SM00135. LY. 5 hits. [Graphical view] |
| SUPFAM | SSF57184. Grow_fac_recept. 1 hit. SSF57424. LDL_rcpt_classA_cys-rich. 8 hits. |
| PROSITE | PS00010. ASX_HYDROXYL. 2 hits. PS00022. EGF_1. False negative. PS01186. EGF_2. 2 hits. PS50026. EGF_3. 2 hits. PS01187. EGF_CA. 1 hit. PS01209. LDLRA_1. 7 hits. PS50068. LDLRA_2. 8 hits. PS51120. LDLRB. 5 hits. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 20816160. |
Entry information
| Entry name | LRP8_CHICK | ||||||||
| Accession | Primary (citable) accession number: Q98931 Secondary accession number(s): Q90883 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
