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Protein

Amyloid-like protein 1

Gene

Aplp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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)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 cAMP biosynthetic process Source: MGI
  • 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
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:88046. Aplp1.

Subcellular locationi

C30 :
  • Cytoplasm

  • Note: C-terminally processed in the Golgi complex.

Topology

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

GO - Cellular componenti

  • Golgi apparatus Source: UniProtKB
  • integral component of membrane Source: UniProtKB
  • membrane Source: MGI
  • perinuclear region of cytoplasm Source: MGI
  • plasma membrane Source: MGI
Complete GO annotation...

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...)Sequence analysis1
Glycosylationi554N-linked (GlcNAc...)Sequence 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

BgeeiENSMUSG00000006651.
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

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198153. 1 interactor.
IntActiQ03157. 10 interactors.
MINTiMINT-1177110.
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

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

« 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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliQ03157.
SMRiQ03157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198153. 1 interactor.
IntActiQ03157. 10 interactors.
MINTiMINT-1177110.
STRINGi10090.ENSMUSP00000006828.

PTM databases

iPTMnetiQ03157.
PhosphoSitePlusiQ03157.

Proteomic databases

MaxQBiQ03157.
PaxDbiQ03157.
PeptideAtlasiQ03157.
PRIDEiQ03157.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi11803.
KEGGimmu:11803.
UCSCiuc009gek.2. mouse.

Organism-specific databases

CTDi333.
MGIiMGI:88046. Aplp1.

Phylogenomic databases

eggNOGiENOG410KDN8. Eukaryota.
ENOG4111MXY. LUCA.
HOVERGENiHBG000051.
InParanoidiQ03157.
KOiK05639.
PhylomeDBiQ03157.
TreeFamiTF317274.

Miscellaneous databases

ChiTaRSiAplp1. mouse.
PROiQ03157.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000006651.
CleanExiMM_APLP1.

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]
ProtoNetiSearch...

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: November 30, 2016
This is version 150 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.