Alpha-2-macroglobulin receptor-associated protein

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• amyloid-beta binding Source: ARUK-UCL <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementⁱ
  • "Low-density lipoprotein receptor represents an apolipoprotein E-independent pathway of Abeta uptake and degradation by astrocytes."
    Basak J.M., Verghese P.B., Yoon H., Kim J., Holtzman D.M.
    J. Biol. Chem. 287:13959-13971(2012) [PubMed] [Europe PMC] [Abstract]
• heparin binding Source: UniProtKB-KW
• lipase binding Source: Ensembl
• low-density lipoprotein particle receptor binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • Ref.9

    "39 kDa receptor-associated protein is an ER resident protein and molecular chaperone for LDL receptor-related protein."
    Bu G., Geuze H.J., Strous G.J., Schwartz A.L.
    EMBO J. 14:2269-2280(1995) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LRP1, MOTIF, GLYCOSYLATION.
• receptor antagonist activity Source: BHF-UCLInferred from direct assayⁱ
  • "The 39-kDa receptor-associated protein regulates ligand binding by the very low density lipoprotein receptor."
    Battey F.D., Gafvels M.E., FitzGerald D.J., Argraves W.S., Chappell D.A., Strauss J.F., Strickland D.K.
    J. Biol. Chem. 269:23268-23273(1994) [PubMed] [Europe PMC] [Abstract]
• signaling receptor binding Source: ParkinsonsUK-UCLTraceable author statementⁱ
  • "The low density lipoprotein receptor-related protein LRP is regulated by membrane type-1 matrix metalloproteinase (MT1-MMP) proteolysis in malignant cells."
    Rozanov D.V., Hahn-Dantona E., Strickland D.K., Strongin A.Y.
    J. Biol. Chem. 279:4260-4268(2004) [PubMed] [Europe PMC] [Abstract]
• very-low-density lipoprotein particle receptor binding Source: BHF-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "The 39-kDa receptor-associated protein regulates ligand binding by the very low density lipoprotein receptor."
    Battey F.D., Gafvels M.E., FitzGerald D.J., Argraves W.S., Chappell D.A., Strauss J.F., Strickland D.K.
    J. Biol. Chem. 269:23268-23273(1994) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• amyloid-beta clearance by transcytosis Source: ARUK-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Central role for PICALM in amyloid-beta blood-brain barrier transcytosis and clearance."
    Zhao Z., Sagare A.P., Ma Q., Halliday M.R., Kong P., Kisler K., Winkler E.A., Ramanathan A., Kanekiyo T., Bu G., Owens N.C., Rege S.V., Si G., Ahuja A., Zhu D., Miller C.A., Schneider J.A., Maeda M.

    , Maeda T., Sugawara T., Ichida J.K., Zlokovic B.V.
    Nat. Neurosci. 18:978-987(2015) [PubMed] [Europe PMC] [Abstract]
• extracellular negative regulation of signal transduction Source: ParkinsonsUK-UCLTraceable author statementⁱ
  • "The low density lipoprotein receptor-related protein LRP is regulated by membrane type-1 matrix metalloproteinase (MT1-MMP) proteolysis in malignant cells."
    Rozanov D.V., Hahn-Dantona E., Strickland D.K., Strongin A.Y.
    J. Biol. Chem. 279:4260-4268(2004) [PubMed] [Europe PMC] [Abstract]
• negative regulation of amyloid-beta clearance Source: BHF-UCL <p>Inferred from Genetic Interaction</p> <p>Used to describe “traditional” genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactionⁱ
  • "SRF and myocardin regulate LRP-mediated amyloid-beta clearance in brain vascular cells."
    Bell R.D., Deane R., Chow N., Long X., Sagare A., Singh I., Streb J.W., Guo H., Rubio A., Van Nostrand W., Miano J.M., Zlokovic B.V.
    Nat. Cell Biol. 11:143-153(2009) [PubMed] [Europe PMC] [Abstract]
• negative regulation of cell death Source: ARUK-UCLInferred from genetic interactionⁱ
  • "Prion protein-mediated toxicity of amyloid-beta oligomers requires lipid rafts and the transmembrane LRP1."
    Rushworth J.V., Griffiths H.H., Watt N.T., Hooper N.M.
    J. Biol. Chem. 288:8935-8951(2013) [PubMed] [Europe PMC] [Abstract]
• negative regulation of protein binding Source: BHF-UCLInferred from direct assayⁱ
  • "The 39-kDa receptor-associated protein regulates ligand binding by the very low density lipoprotein receptor."
    Battey F.D., Gafvels M.E., FitzGerald D.J., Argraves W.S., Chappell D.A., Strauss J.F., Strickland D.K.
    J. Biol. Chem. 269:23268-23273(1994) [PubMed] [Europe PMC] [Abstract]
• negative regulation of receptor internalization Source: ARUK-UCLInferred from genetic interactionⁱ
  • "Prion protein-mediated toxicity of amyloid-beta oligomers requires lipid rafts and the transmembrane LRP1."
    Rushworth J.V., Griffiths H.H., Watt N.T., Hooper N.M.
    J. Biol. Chem. 288:8935-8951(2013) [PubMed] [Europe PMC] [Abstract]
• negative regulation of very-low-density lipoprotein particle clearance Source: BHF-UCLInferred from direct assayⁱ
  • "The 39-kDa receptor-associated protein regulates ligand binding by the very low density lipoprotein receptor."
    Battey F.D., Gafvels M.E., FitzGerald D.J., Argraves W.S., Chappell D.A., Strauss J.F., Strickland D.K.
    J. Biol. Chem. 269:23268-23273(1994) [PubMed] [Europe PMC] [Abstract]
• positive regulation of amyloid-beta clearance Source: ARUK-UCLTraceable author statementⁱ
  • "Low-density lipoprotein receptor represents an apolipoprotein E-independent pathway of Abeta uptake and degradation by astrocytes."
    Basak J.M., Verghese P.B., Yoon H., Kim J., Holtzman D.M.
    J. Biol. Chem. 287:13959-13971(2012) [PubMed] [Europe PMC] [Abstract]
• regulation of receptor-mediated endocytosis Source: UniProtKBInferred from direct assayⁱ
  • Ref.9

    "39 kDa receptor-associated protein is an ER resident protein and molecular chaperone for LDL receptor-related protein."
    Bu G., Geuze H.J., Strous G.J., Schwartz A.L.
    EMBO J. 14:2269-2280(1995) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LRP1, MOTIF, GLYCOSYLATION.

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

Keywords - Cellular componentⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseaseⁱ

Mutagenesis

Organism-specific databases

Miscellaneous databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• lipase binding Source: Ensembl
• low-density lipoprotein particle receptor binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.9

    "39 kDa receptor-associated protein is an ER resident protein and molecular chaperone for LDL receptor-related protein."
    Bu G., Geuze H.J., Strous G.J., Schwartz A.L.
    EMBO J. 14:2269-2280(1995) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LRP1, MOTIF, GLYCOSYLATION.
• receptor antagonist activity Source: BHF-UCLInferred from direct assayⁱ
  • "The 39-kDa receptor-associated protein regulates ligand binding by the very low density lipoprotein receptor."
    Battey F.D., Gafvels M.E., FitzGerald D.J., Argraves W.S., Chappell D.A., Strauss J.F., Strickland D.K.
    J. Biol. Chem. 269:23268-23273(1994) [PubMed] [Europe PMC] [Abstract]
• signaling receptor binding Source: ParkinsonsUK-UCLTraceable author statementⁱ
  • "The low density lipoprotein receptor-related protein LRP is regulated by membrane type-1 matrix metalloproteinase (MT1-MMP) proteolysis in malignant cells."
    Rozanov D.V., Hahn-Dantona E., Strickland D.K., Strongin A.Y.
    J. Biol. Chem. 279:4260-4268(2004) [PubMed] [Europe PMC] [Abstract]
• very-low-density lipoprotein particle receptor binding Source: BHF-UCLInferred from physical interactionⁱ
  • "The 39-kDa receptor-associated protein regulates ligand binding by the very low density lipoprotein receptor."
    Battey F.D., Gafvels M.E., FitzGerald D.J., Argraves W.S., Chappell D.A., Strauss J.F., Strickland D.K.
    J. Biol. Chem. 269:23268-23273(1994) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Region

Coiled coil

Motif

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MAPRRVRSFL RGLPALLLLL LFLGPWPAAS HGGKYSREKN QPKPSPKRES 
        60         70         80         90        100
GEEFRMEKLN QLWEKAQRLH LPPVRLAELH ADLKIQERDE LAWKKLKLDG 
       110        120        130        140        150
LDEDGEKEAR LIRNLNVILA KYGLDGKKDA RQVTSNSLSG TQEDGLDDPR 
       160        170        180        190        200
LEKLWHKAKT SGKFSGEELD KLWREFLHHK EKVHEYNVLL ETLSRTEEIH 
       210        220        230        240        250
ENVISPSDLS DIKGSVLHSR HTELKEKLRS INQGLDRLRR VSHQGYSTEA 
       260        270        280        290        300
EFEEPRVIDL WDLAQSANLT DKELEAFREE LKHFEAKIEK HNHYQKQLEI 
       310        320        330        340        350
AHEKLRHAES VGDGERVSRS REKHALLEGR TKELGYTVKK HLQDLSGRIS 

RARHNEL                                                

Experimental Info

Natural variant

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityⁱ

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. Human entries with polymorphisms or disease mutations
   List of human entries with polymorphisms or disease mutations
2. SIMILARITY comments
   Index of protein domains and families
3. Human chromosome 4
   Human chromosome 4: entries, gene names and cross-references to MIM
4. Human polymorphisms and disease mutations
   Index of human polymorphisms and disease mutations
5. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
6. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references