Q03157 · APLP1_MOUSE
- ProteinAmyloid beta precursor like protein 1
- GeneAplp1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids654 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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.
Miscellaneous
Binds zinc and copper in the extracellular domain. Zinc-binding increases heparin binding. No Cu2+ reducing activity with copper-binding.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 174 | Cu2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 206 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 209 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 210 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 565 | Cu2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 565 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Site | 624-625 | Cleavage; by caspase-3 | ||||
Sequence: DP |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | Golgi apparatus | |
Cellular Component | membrane | |
Cellular Component | nucleoplasm | |
Cellular Component | perinuclear region of cytoplasm | |
Cellular Component | plasma membrane | |
Molecular Function | alpha-2A adrenergic receptor binding | |
Molecular Function | alpha-2B adrenergic receptor binding | |
Molecular Function | alpha-2C adrenergic receptor binding | |
Molecular Function | heparin binding | |
Molecular Function | identical protein binding | |
Molecular Function | transition metal ion binding | |
Biological Process | apoptotic process | |
Biological Process | axonogenesis | |
Biological Process | cell adhesion | |
Biological Process | cellular response to norepinephrine stimulus | |
Biological Process | central nervous system development | |
Biological Process | cytosolic mRNA polyadenylation | |
Biological Process | endocytosis | |
Biological Process | extracellular matrix organization | |
Biological Process | forebrain development | |
Biological Process | negative regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway | |
Biological Process | regulation of translation |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameAmyloid beta precursor like protein 1
- Alternative names
- Cleaved into 1 chains
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ03157
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
C30
Note: C-terminally processed in the Golgi complex.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 39-584 | Extracellular | ||||
Sequence: NLAVGSPSAAEAPGSAQVAGLCGRLTLHRDLRTGRWEPDPQRSRRCLLDPQRVLEYCRQMYPELHIARVEQAAQAIPMERWCGGTRSGRCAHPHHEVVPFHCLPGEFVSEALLVPEGCRFLHQERMDQCESSTRRHQEAQEACSSQGLILHGSGMLLPCGSDRFRGVEYVCCPPPATPNPSGMAAGDPSTRSWPLGGRAEGGEDEEEVESFPQPVDDYFVEPPQAEEEEEEEEERAPPPSSHTPVMVSRVTPTPRPTDGVDVYFGMPGEIGEHEGFLRAKMDLEERRMRQINEVMREWAMADSQSKNLPKADRQALNEHFQSILQTLEEQVSGERQRLVETHATRVIALINDQRRAALEGFLAALQGDPPQAERVLMALRRYLRAEQKEQRHTLRHYQHVAAVDPEKAQQMRFQVQTHLQVIEERMNQSLGLLDQNPHLAQELRPQIQELLLAEHLGPSELDASVPGSSSEDKGSLQPPESKDDPPVTLPKGSTDQESSSSGREKLTPLEQYEQKVNASAPRGFPFHSSDIQRDELAPSGTGVSRE | ||||||
Transmembrane | 585-607 | Helical | ||||
Sequence: ALSGLLIMGAGGGSLIVLSLLLL | ||||||
Topological domain | 608-654 | Cytoplasmic | ||||
Sequence: RKKKPYGTISHGVVEVDPMLTLEEQQLRELQRHGYENPTYRFLEERP |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 642 | Reduced binding of APBB1. | ||||
Sequence: Y → G |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 32 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, peptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-38 | |||||
Sequence: MGPTSPAARGQGRRWRPPPLPLLLPLSLLLLRAQLAVG | ||||||
Chain | PRO_0000000205 | 39-654 | Amyloid beta precursor like protein 1 | |||
Sequence: NLAVGSPSAAEAPGSAQVAGLCGRLTLHRDLRTGRWEPDPQRSRRCLLDPQRVLEYCRQMYPELHIARVEQAAQAIPMERWCGGTRSGRCAHPHHEVVPFHCLPGEFVSEALLVPEGCRFLHQERMDQCESSTRRHQEAQEACSSQGLILHGSGMLLPCGSDRFRGVEYVCCPPPATPNPSGMAAGDPSTRSWPLGGRAEGGEDEEEVESFPQPVDDYFVEPPQAEEEEEEEEERAPPPSSHTPVMVSRVTPTPRPTDGVDVYFGMPGEIGEHEGFLRAKMDLEERRMRQINEVMREWAMADSQSKNLPKADRQALNEHFQSILQTLEEQVSGERQRLVETHATRVIALINDQRRAALEGFLAALQGDPPQAERVLMALRRYLRAEQKEQRHTLRHYQHVAAVDPEKAQQMRFQVQTHLQVIEERMNQSLGLLDQNPHLAQELRPQIQELLLAEHLGPSELDASVPGSSSEDKGSLQPPESKDDPPVTLPKGSTDQESSSSGREKLTPLEQYEQKVNASAPRGFPFHSSDIQRDELAPSGTGVSREALSGLLIMGAGGGSLIVLSLLLLRKKKPYGTISHGVVEVDPMLTLEEQQLRELQRHGYENPTYRFLEERP | ||||||
Disulfide bond | 60↔84 | |||||
Sequence: CGRLTLHRDLRTGRWEPDPQRSRRC | ||||||
Disulfide bond | 95↔140 | |||||
Sequence: CRQMYPELHIARVEQAAQAIPMERWCGGTRSGRCAHPHHEVVPFHC | ||||||
Disulfide bond | 120↔128 | |||||
Sequence: CGGTRSGRC | ||||||
Disulfide bond | 156↔210 | |||||
Sequence: CRFLHQERMDQCESSTRRHQEAQEACSSQGLILHGSGMLLPCGSDRFRGVEYVCC | ||||||
Disulfide bond | 167↔197 | |||||
Sequence: CESSTRRHQEAQEACSSQGLILHGSGMLLPC | ||||||
Disulfide bond | 181↔209 | |||||
Sequence: CSSQGLILHGSGMLLPCGSDRFRGVEYVC | ||||||
Glycosylation | 465 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 555 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Peptide | PRO_0000000206 | 625-654 | C30 | |||
Sequence: PMLTLEEQQLRELQRHGYENPTYRFLEERP |
Post-translational modification
Proteolytically cleaved by caspases during neuronal apoptosis. Cleaved, in vitro, at Asp-624 by caspase-3 (By similarity).
N- and O-glycosylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
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
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
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q03157 | App P12023 | 4 | EBI-399929, EBI-78814 | |
BINARY | Q03157 | Dab1 P97318 | 4 | EBI-399929, EBI-81680 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 50-146 | GFLD subdomain | ||||
Sequence: APGSAQVAGLCGRLTLHRDLRTGRWEPDPQRSRRCLLDPQRVLEYCRQMYPELHIARVEQAAQAIPMERWCGGTRSGRCAHPHHEVVPFHCLPGEFV | ||||||
Domain | 50-212 | E1 | ||||
Sequence: APGSAQVAGLCGRLTLHRDLRTGRWEPDPQRSRRCLLDPQRVLEYCRQMYPELHIARVEQAAQAIPMERWCGGTRSGRCAHPHHEVVPFHCLPGEFVSEALLVPEGCRFLHQERMDQCESSTRRHQEAQEACSSQGLILHGSGMLLPCGSDRFRGVEYVCCPP | ||||||
Region | 154-212 | CuBD subdomain | ||||
Sequence: EGCRFLHQERMDQCESSTRRHQEAQEACSSQGLILHGSGMLLPCGSDRFRGVEYVCCPP | ||||||
Region | 214-297 | Disordered | ||||
Sequence: ATPNPSGMAAGDPSTRSWPLGGRAEGGEDEEEVESFPQPVDDYFVEPPQAEEEEEEEEERAPPPSSHTPVMVSRVTPTPRPTDG | ||||||
Domain | 297-488 | E2 | ||||
Sequence: GVDVYFGMPGEIGEHEGFLRAKMDLEERRMRQINEVMREWAMADSQSKNLPKADRQALNEHFQSILQTLEEQVSGERQRLVETHATRVIALINDQRRAALEGFLAALQGDPPQAERVLMALRRYLRAEQKEQRHTLRHYQHVAAVDPEKAQQMRFQVQTHLQVIEERMNQSLGLLDQNPHLAQELRPQIQEL | ||||||
Region | 314-346 | Heparin-binding | ||||
Sequence: FLRAKMDLEERRMRQINEVMREWAMADSQSKNL | ||||||
Region | 414-445 | Heparin-binding | ||||
Sequence: LMALRRYLRAEQKEQRHTLRHYQHVAAVDPEK | ||||||
Region | 446-463 | Collagen-binding | ||||
Sequence: AQQMRFQVQTHLQVIEER | ||||||
Region | 497-580 | Disordered | ||||
Sequence: SELDASVPGSSSEDKGSLQPPESKDDPPVTLPKGSTDQESSSSGREKLTPLEQYEQKVNASAPRGFPFHSSDIQRDELAPSGTG | ||||||
Compositional bias | 529-545 | Polar residues | ||||
Sequence: KGSTDQESSSSGREKLT | ||||||
Motif | 608-619 | Basolateral sorting signal | ||||
Sequence: RKKKPYGTISHG | ||||||
Region | 636-652 | Interaction with DAB1 | ||||
Sequence: ELQRHGYENPTYRFLEE | ||||||
Region | 640-654 | Interaction with DAB2 | ||||
Sequence: HGYENPTYRFLEERP | ||||||
Motif | 644-647 | NPXY motif; contains endocytosis signal | ||||
Sequence: NPTY |
Domain
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 similarities
Belongs to the APP family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length654
- Mass (Da)72,848
- Last updated2021-09-29 v2
- ChecksumD72A3065D8D95F68
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 19 | in Ref. 1; AAA37247 | ||||
Sequence: Missing | ||||||
Sequence conflict | 280 | in Ref. 2; BAE32979 | ||||
Sequence: H → P | ||||||
Compositional bias | 529-545 | Polar residues | ||||
Sequence: KGSTDQESSSSGREKLT |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L04538 EMBL· GenBank· DDBJ | AAA37247.1 EMBL· GenBank· DDBJ | mRNA | ||
AK154992 EMBL· GenBank· DDBJ | BAE32979.1 EMBL· GenBank· DDBJ | mRNA | ||
JH584274 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC021877 EMBL· GenBank· DDBJ | AAH21877.1 EMBL· GenBank· DDBJ | mRNA |