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Protein

Amyloid-like protein 1

Gene

Aplp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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

Miscellaneous

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei166Required for Cu(2+) reductionBy similarity1

GO - Molecular functioni

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • cell adhesion Source: UniProtKB-KW
  • cellular response to norepinephrine stimulus Source: MGI
  • endocytosis Source: UniProtKB-KW
  • extracellular matrix organization Source: MGI
  • forebrain development Source: MGI
  • mRNA polyadenylation Source: MGI
  • negative regulation of adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: MGI
  • regulation of translation Source: MGI

Keywordsi

Molecular functionHeparin-binding
Biological processApoptosis, Cell adhesion, Endocytosis
LigandCopper, 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:88046 Aplp1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini38 – 583ExtracellularSequence analysisAdd BLAST546
Transmembranei584 – 606HelicalSequence analysisAdd BLAST23
Topological domaini607 – 653CytoplasmicSequence analysisAdd BLAST47

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi641Y → G: Reduced binding of APBB1. 1 Publication1

Keywords - Diseasei

Neurodegeneration

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 37Sequence analysisAdd BLAST37
ChainiPRO_000000020538 – 653Amyloid-like protein 1Add BLAST616
PeptideiPRO_0000000206624 – 653C30By similarityAdd BLAST30

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi464N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi554N-linked (GlcNAc...) asparagineSequence analysis1

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei623 – 624Cleavage; by caspase-3By similarity2

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ03157
PaxDbiQ03157
PeptideAtlasiQ03157
PRIDEiQ03157

PTM databases

iPTMnetiQ03157
PhosphoSitePlusiQ03157

Expressioni

Gene expression databases

CleanExiMM_APLP1

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

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198153, 1 interactor
IntActiQ03157, 11 interactors
MINTiQ03157
STRINGi10090.ENSMUSP00000006828

Structurei

3D structure databases

ProteinModelPortaliQ03157
SMRiQ03157
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni157 – 177Copper-bindingAdd BLAST21
Regioni203 – 210Zinc-bindingBy similarity8
Regioni313 – 345Heparin-bindingBy similarityAdd BLAST33
Regioni413 – 444Heparin-bindingBy similarityAdd BLAST32
Regioni445 – 462Collagen-bindingBy similarityAdd BLAST18
Regioni635 – 651Interaction with DAB1Add BLAST17
Regioni639 – 653Interaction with DAB21 PublicationAdd BLAST15

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi607 – 618Basolateral sorting signalBy similarityAdd BLAST12
Motifi643 – 646NPXY motif; contains endocytosis signal4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi263 – 271Poly-Glu9
Compositional biasi535 – 538Poly-Ser4
Compositional biasi601 – 606Poly-Leu6

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

eggNOGiENOG410KDN8 Eukaryota
ENOG4111MXY LUCA
HOVERGENiHBG000051
InParanoidiQ03157
KOiK05639
PhylomeDBiQ03157
TreeFamiTF317274

Family and domain databases

Gene3Di1.20.120.770, 1 hit
3.30.1490.140, 1 hit
3.90.570.10, 1 hit
InterProiView protein in InterPro
IPR036669 Amyloid_Cu-bd_sf
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
IPR036454 Amyloid_glyco_heparin-bd_sf
IPR019745 Amyloid_glyco_intracell_CS
IPR019543 APP_amyloid_C
IPR036176 E2_sf
PANTHERiPTHR23103 PTHR23103, 1 hit
PfamiView protein in Pfam
PF10515 APP_amyloid, 1 hit
PF12924 APP_Cu_bd, 1 hit
PF12925 APP_E2, 1 hit
PF02177 APP_N, 1 hit
PRINTSiPR00203 AMYLOIDA4
SMARTiView protein in SMART
SM00006 A4_EXTRA, 1 hit
SUPFAMiSSF109843 SSF109843, 1 hit
SSF56491 SSF56491, 1 hit
SSF89811 SSF89811, 1 hit
PROSITEiView protein in PROSITE
PS00319 A4_EXTRA, 1 hit
PS00320 A4_INTRA, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q03157-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPTSPAARG QGRRWRPPLP LLLPLSLLLL RAQLAVGNLA VGSPSAAEAP
60 70 80 90 100
GSAQVAGLCG RLTLHRDLRT GRWEPDPQRS RRCLLDPQRV LEYCRQMYPE
110 120 130 140 150
LHIARVEQAA QAIPMERWCG GTRSGRCAHP HHEVVPFHCL PGEFVSEALL
160 170 180 190 200
VPEGCRFLHQ ERMDQCESST RRHQEAQEAC SSQGLILHGS GMLLPCGSDR
210 220 230 240 250
FRGVEYVCCP PPATPNPSGM AAGDPSTRSW PLGGRAEGGE DEEEVESFPQ
260 270 280 290 300
PVDDYFVEPP QAEEEEEEEE ERAPPPSSHT PVMVSRVTPT PRPTDGVDVY
310 320 330 340 350
FGMPGEIGEH EGFLRAKMDL EERRMRQINE VMREWAMADS QSKNLPKADR
360 370 380 390 400
QALNEHFQSI LQTLEEQVSG ERQRLVETHA TRVIALINDQ RRAALEGFLA
410 420 430 440 450
ALQGDPPQAE RVLMALRRYL RAEQKEQRHT LRHYQHVAAV DPEKAQQMRF
460 470 480 490 500
QVQTHLQVIE ERMNQSLGLL DQNPHLAQEL RPQIQELLLA EHLGPSELDA
510 520 530 540 550
SVPGSSSEDK GSLQPPESKD DPPVTLPKGS TDQESSSSGR EKLTPLEQYE
560 570 580 590 600
QKVNASAPRG FPFHSSDIQR DELAPSGTGV SREALSGLLI MGAGGGSLIV
610 620 630 640 650
LSLLLLRKKK PYGTISHGVV EVDPMLTLEE QQLRELQRHG YENPTYRFLE

ERP
Length:653
Mass (Da):72,751
Last modified:October 1, 1993 - v1
Checksum:i56516DC3EA40E4B0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti18P → PP in AAH21877 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04538 mRNA Translation: AAA37247.1
BC021877 mRNA Translation: AAH21877.1
PIRiA46362
RefSeqiNP_031493.2, NM_007467.3
UniGeneiMm.2381

Genome annotation databases

GeneIDi11803
KEGGimmu:11803
UCSCiuc009gek.2 mouse

Similar proteinsi

Entry informationi

Entry nameiAPLP1_MOUSE
AccessioniPrimary (citable) accession number: Q03157
Secondary accession number(s): Q8VC38
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: March 28, 2018
This is version 158 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health