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Q03157

- APLP1_MOUSE

UniProt

Q03157 - APLP1_MOUSE

Protein

Amyloid-like protein 1

Gene

Aplp1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    Functioni

    May play a role in postsynaptic function. The C-terminal gamma-secretase processed fragment, ALID1, activates transcription activation through APBB1 (Fe65) binding. Couples to JIP signal transduction through C-terminal binding. May interact with cellular G-protein signaling pathways. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I.
    The gamma-CTF peptide, C30, is a potent enhancer of neuronal apoptosis.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei166 – 1661Required for Cu(2+) reductionBy similarity
    Sitei623 – 6242Cleavage; by caspase-3By similarity

    GO - Molecular functioni

    1. heparin binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. transition metal ion binding Source: InterPro

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. cell adhesion Source: UniProtKB-KW
    3. cellular response to norepinephrine stimulus Source: Ensembl
    4. endocytosis Source: UniProtKB-KW
    5. extracellular matrix organization Source: MGI
    6. forebrain development Source: MGI
    7. mRNA polyadenylation Source: MGI
    8. negative regulation of cAMP biosynthetic process Source: Ensembl
    9. regulation of translation Source: MGI

    Keywords - Biological processi

    Apoptosis, Cell adhesion, Endocytosis

    Keywords - Ligandi

    Copper, Heparin-binding, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Amyloid-like protein 1
    Short name:
    APLP
    Short name:
    APLP-1
    Cleaved into the following chain:
    Gene namesi
    Name:Aplp1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:88046. Aplp1.

    Subcellular locationi

    Peptide C30 : Cytoplasm
    Note: C-terminally processed in the Golgi complex.

    GO - Cellular componenti

    1. Golgi apparatus Source: UniProtKB
    2. integral component of membrane Source: UniProtKB
    3. membrane Source: MGI
    4. perinuclear region of cytoplasm Source: Ensembl
    5. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi641 – 6411Y → G: Reduced binding of APBB1. 1 Publication

    Keywords - Diseasei

    Neurodegeneration

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3737Sequence AnalysisAdd
    BLAST
    Chaini38 – 653616Amyloid-like protein 1PRO_0000000205Add
    BLAST
    Peptidei624 – 65330C30By similarityPRO_0000000206Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi464 – 4641N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi554 – 5541N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Proteolytically cleaved by caspases during neuronal apoptosis. Cleaved, in vitro, at Asp-623 by caspase-3 By similarity.By similarity
    N- and O-glycosylated.

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ03157.
    PRIDEiQ03157.

    PTM databases

    PhosphoSiteiQ03157.

    Expressioni

    Gene expression databases

    BgeeiQ03157.
    CleanExiMM_APLP1.
    GenevestigatoriQ03157.

    Interactioni

    Subunit structurei

    Monomer and homodimer. Heparin binding promotes homodimerization. Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB and APBA family members, MAPK8IP1 and Dab1 By similarity. Binding to Dab1 inhibits its serine phosphorylation. Interacts with CPEB1. Interacts (via NPXY motif) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif. Interacts (via NPXY motif) with DAB1.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AppP120234EBI-399929,EBI-78814
    Dab1P973184EBI-399929,EBI-81680

    Protein-protein interaction databases

    BioGridi198153. 1 interaction.
    IntActiQ03157. 10 interactions.
    MINTiMINT-1177110.

    Structurei

    3D structure databases

    ProteinModelPortaliQ03157.
    SMRiQ03157. Positions 54-145, 148-210, 295-488.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini38 – 583546ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini607 – 65347CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei584 – 60623HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni157 – 17721Copper-bindingAdd
    BLAST
    Regioni203 – 2108Zinc-bindingBy similarity
    Regioni313 – 34533Heparin-bindingBy similarityAdd
    BLAST
    Regioni413 – 44432Heparin-bindingBy similarityAdd
    BLAST
    Regioni445 – 46218Collagen-bindingBy similarityAdd
    BLAST
    Regioni635 – 65117Interaction with DAB1Add
    BLAST
    Regioni639 – 65315Interaction with DAB2Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi607 – 61812Basolateral sorting signalBy similarityAdd
    BLAST
    Motifi643 – 6464NPXY motif; contains endocytosis signal

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi263 – 2719Poly-Glu
    Compositional biasi535 – 5384Poly-Ser
    Compositional biasi601 – 6066Poly-Leu

    Domaini

    The NPXY sequence motif found in many tyrosine-phosphorylated proteins is required for the specific binding of the PID domain. However, additional amino acids either N- or C-terminal to the NPXY motif are often required for complete interaction. The NPXY site is also involved in clathrin-mediated endocytosis.

    Sequence similaritiesi

    Belongs to the APP family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG289770.
    GeneTreeiENSGT00530000063252.
    HOVERGENiHBG000051.
    InParanoidiQ03157.
    KOiK05639.
    OrthoDBiEOG7RNJZP.
    PhylomeDBiQ03157.
    TreeFamiTF317274.

    Family and domain databases

    Gene3Di3.30.1490.140. 1 hit.
    3.90.570.10. 1 hit.
    InterProiIPR008155. Amyloid_glyco.
    IPR011178. Amyloid_glyco_Cu-bd.
    IPR024329. Amyloid_glyco_E2_domain.
    IPR008154. Amyloid_glyco_extra.
    IPR019744. Amyloid_glyco_extracell_CS.
    IPR015849. Amyloid_glyco_heparin-bd.
    IPR019745. Amyloid_glyco_intracell_CS.
    IPR019543. APP_amyloid_C.
    [Graphical view]
    PfamiPF10515. APP_amyloid. 1 hit.
    PF12924. APP_Cu_bd. 1 hit.
    PF12925. APP_E2. 1 hit.
    PF02177. APP_N. 1 hit.
    [Graphical view]
    PRINTSiPR00203. AMYLOIDA4.
    SMARTiSM00006. A4_EXTRA. 1 hit.
    [Graphical view]
    SUPFAMiSSF109843. SSF109843. 1 hit.
    SSF56491. SSF56491. 1 hit.
    SSF89811. SSF89811. 1 hit.
    PROSITEiPS00319. A4_EXTRA. 1 hit.
    PS00320. A4_INTRA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q03157-1 [UniParc]FASTAAdd to Basket

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    MGPTSPAARG QGRRWRPPLP LLLPLSLLLL RAQLAVGNLA VGSPSAAEAP    50
    GSAQVAGLCG RLTLHRDLRT GRWEPDPQRS RRCLLDPQRV LEYCRQMYPE 100
    LHIARVEQAA QAIPMERWCG GTRSGRCAHP HHEVVPFHCL PGEFVSEALL 150
    VPEGCRFLHQ ERMDQCESST RRHQEAQEAC SSQGLILHGS GMLLPCGSDR 200
    FRGVEYVCCP PPATPNPSGM AAGDPSTRSW PLGGRAEGGE DEEEVESFPQ 250
    PVDDYFVEPP QAEEEEEEEE ERAPPPSSHT PVMVSRVTPT PRPTDGVDVY 300
    FGMPGEIGEH EGFLRAKMDL EERRMRQINE VMREWAMADS QSKNLPKADR 350
    QALNEHFQSI LQTLEEQVSG ERQRLVETHA TRVIALINDQ RRAALEGFLA 400
    ALQGDPPQAE RVLMALRRYL RAEQKEQRHT LRHYQHVAAV DPEKAQQMRF 450
    QVQTHLQVIE ERMNQSLGLL DQNPHLAQEL RPQIQELLLA EHLGPSELDA 500
    SVPGSSSEDK GSLQPPESKD DPPVTLPKGS TDQESSSSGR EKLTPLEQYE 550
    QKVNASAPRG FPFHSSDIQR DELAPSGTGV SREALSGLLI MGAGGGSLIV 600
    LSLLLLRKKK PYGTISHGVV EVDPMLTLEE QQLRELQRHG YENPTYRFLE 650
    ERP 653
    Length:653
    Mass (Da):72,751
    Last modified:October 1, 1993 - v1
    Checksum:i56516DC3EA40E4B0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti18 – 181P → PP in AAH21877. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L04538 mRNA. Translation: AAA37247.1.
    BC021877 mRNA. Translation: AAH21877.1.
    PIRiA46362.
    RefSeqiNP_031493.2. NM_007467.3.
    UniGeneiMm.2381.

    Genome annotation databases

    EnsembliENSMUST00000006828; ENSMUSP00000006828; ENSMUSG00000006651.
    GeneIDi11803.
    KEGGimmu:11803.
    UCSCiuc009gek.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L04538 mRNA. Translation: AAA37247.1 .
    BC021877 mRNA. Translation: AAH21877.1 .
    PIRi A46362.
    RefSeqi NP_031493.2. NM_007467.3.
    UniGenei Mm.2381.

    3D structure databases

    ProteinModelPortali Q03157.
    SMRi Q03157. Positions 54-145, 148-210, 295-488.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198153. 1 interaction.
    IntActi Q03157. 10 interactions.
    MINTi MINT-1177110.

    PTM databases

    PhosphoSitei Q03157.

    Proteomic databases

    PaxDbi Q03157.
    PRIDEi Q03157.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000006828 ; ENSMUSP00000006828 ; ENSMUSG00000006651 .
    GeneIDi 11803.
    KEGGi mmu:11803.
    UCSCi uc009gek.2. mouse.

    Organism-specific databases

    CTDi 333.
    MGIi MGI:88046. Aplp1.

    Phylogenomic databases

    eggNOGi NOG289770.
    GeneTreei ENSGT00530000063252.
    HOVERGENi HBG000051.
    InParanoidi Q03157.
    KOi K05639.
    OrthoDBi EOG7RNJZP.
    PhylomeDBi Q03157.
    TreeFami TF317274.

    Miscellaneous databases

    ChiTaRSi APLP1. mouse.
    NextBioi 279655.
    PROi Q03157.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q03157.
    CleanExi MM_APLP1.
    Genevestigatori Q03157.

    Family and domain databases

    Gene3Di 3.30.1490.140. 1 hit.
    3.90.570.10. 1 hit.
    InterProi IPR008155. Amyloid_glyco.
    IPR011178. Amyloid_glyco_Cu-bd.
    IPR024329. Amyloid_glyco_E2_domain.
    IPR008154. Amyloid_glyco_extra.
    IPR019744. Amyloid_glyco_extracell_CS.
    IPR015849. Amyloid_glyco_heparin-bd.
    IPR019745. Amyloid_glyco_intracell_CS.
    IPR019543. APP_amyloid_C.
    [Graphical view ]
    Pfami PF10515. APP_amyloid. 1 hit.
    PF12924. APP_Cu_bd. 1 hit.
    PF12925. APP_E2. 1 hit.
    PF02177. APP_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00203. AMYLOIDA4.
    SMARTi SM00006. A4_EXTRA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF109843. SSF109843. 1 hit.
    SSF56491. SSF56491. 1 hit.
    SSF89811. SSF89811. 1 hit.
    PROSITEi PS00319. A4_EXTRA. 1 hit.
    PS00320. A4_INTRA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a mouse brain cDNA that encodes a protein related to the Alzheimer disease-associated amyloid beta protein precursor."
      Wasco W., Bupp K., Magendantz M., Gusella J.F., Tanzi R.E., Solomon F.
      Proc. Natl. Acad. Sci. U.S.A. 89:10758-10762(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Retina.
    3. "Regulation of amyloid protein precursor (APP) binding to collagen and mapping of the binding sites on APP and collagen type I."
      Beher D., Hesse L., Masters C.L., Multhaup G.
      J. Biol. Chem. 271:1613-1620(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: COLLAGEN-BINDING.
    4. "Disabled-1 binds to the cytoplasmic domain of amyloid precursor-like protein 1."
      Homayouni R., Rice D.S., Sheldon M., Curran T.
      J. Neurosci. 19:7507-7515(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DAB1.
    5. "C-jun N-terminal kinase (JNK)-interacting protein-1b/islet-brain-1 scaffolds Alzheimer's amyloid precursor protein with JNK."
      Matsuda S., Yasukawa T., Homma Y., Ito Y., Niikura T., Hiraki T., Hirai S., Ohno S., Kita Y., Kawasumi M., Kouyama K., Yamamoto T., Kyriakis J.M., Nishimoto I.
      J. Neurosci. 21:6597-6607(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAPK8IP1.
    6. "Disabled-2 colocalizes with the LDLR in clathrin-coated pits and interacts with AP-2."
      Morris S.M., Cooper J.A.
      Traffic 2:111-123(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DAB2.
    7. "Processing of beta-amyloid precursor-like protein-1 and -2 by gamma-secretase regulates transcription."
      Scheinfeld M.H., Ghersi E., Laky K., Fowlkes B.J., D'Adamio L.
      J. Biol. Chem. 277:44195-44201(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING BY GAMMA SECRETASE, INTERACTION WITH APBB1, MUTAGENESIS OF TYR-641.
    8. "Crystal structures of the Dab homology domains of mouse disabled 1 and 2."
      Yun M., Keshvara L., Park C.G., Zhang Y.M., Dickerson J.B., Zheng J., Rock C.O., Curran T., Park H.W.
      J. Biol. Chem. 278:36572-36581(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DAB1.
    9. "Amyloid precursor proteins anchor CPEB to membranes and promote polyadenylation-induced translation."
      Cao Q., Huang Y.-S., Kan M.-C., Richter J.D.
      Mol. Cell. Biol. 25:10930-10939(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CPEB1.

    Entry informationi

    Entry nameiAPLP1_MOUSE
    AccessioniPrimary (citable) accession number: Q03157
    Secondary accession number(s): Q8VC38
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 131 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Binds zinc and copper in the extracellular domain. Zinc-binding increases heparin binding. No Cu2+ reducing activity with copper-binding.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3