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Q03157

- APLP1_MOUSE

UniProt

Q03157 - APLP1_MOUSE

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Protein

Amyloid-like protein 1

Gene
Aplp1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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+) reduction By similarity
Sitei623 – 6242Cleavage; by caspase-3 By 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
Complete GO annotation...

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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini38 – 583546Extracellular Reviewed predictionAdd
BLAST
Transmembranei584 – 60623Helical; Reviewed predictionAdd
BLAST
Topological domaini607 – 65347Cytoplasmic Reviewed predictionAdd
BLAST

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
Complete GO annotation...

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 – 3737 Reviewed predictionAdd
BLAST
Chaini38 – 653616Amyloid-like protein 1PRO_0000000205Add
BLAST
Peptidei624 – 65330C30 By similarityPRO_0000000206Add
BLAST

Amino acid modifications

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

Post-translational modificationi

Proteolytically cleaved by caspases during neuronal apoptosis. Cleaved, in vitro, at Asp-623 by caspase-3 By similarity.1 Publication
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 DAB1.6 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.

Family & Domainsi

Region

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi607 – 61812Basolateral sorting signal By 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.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181P → PP in AAH21877. 1 Publication

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

« Hide 'large scale' publications
  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: June 11, 2014
This is version 130 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

Similar proteinsi