APLP1
Amyloid beta precursor like protein 1
Also known as: APLP, APLP1_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P51693
- Gene
- APLP1
- Ensembl
- ENSG00000105290
- Chromosome
- 19
- Canonical length
- 650 aa
- Protein class
- Plasma proteins, Predicted intracellular proteins, Predicted membrane proteins
- Subcellular location
- Nucleoplasm,Golgi apparatus,Plasma membrane
- Quaternary structure
- Homodimer
OverviewNCBI Gene
This gene encodes a member of the highly conserved amyloid precursor protein gene family. The encoded protein is a membrane-associated glycoprotein that is cleaved by secretases in a manner similar to amyloid beta A4 precursor protein cleavage. This cleavage liberates an intracellular cytoplasmic fragment that may act as a transcriptional activator. The encoded protein may also play a role in synaptic maturation during cortical development. Alternatively spliced transcript variants encoding different isoforms have been described. [provided by RefSeq, Jul 2008]
Canonical amino-acid sequenceUniProt
650 residues, UniProt reviewed canonical sequence.
>P51693|APLP1
1 MGPASPAARG LSRRPGQPPL PLLLPLLLLL LRAQPAIGSL AGGSPGAAEA PGSAQVAGLC
61 GRLTLHRDLR TGRWEPDPQR SRRCLRDPQR VLEYCRQMYP ELQIARVEQA TQAIPMERWC
121 GGSRSGSCAH PHHQVVPFRC LPGEFVSEAL LVPEGCRFLH QERMDQCESS TRRHQEAQEA
181 CSSQGLILHG SGMLLPCGSD RFRGVEYVCC PPPGTPDPSG TAVGDPSTRS WPPGSRVEGA
241 EDEEEEESFP QPVDDYFVEP PQAEEEEETV PPPSSHTLAV VGKVTPTPRP TDGVDIYFGM
301 PGEISEHEGF LRAKMDLEER RMRQINEVMR EWAMADNQSK NLPKADRQAL NEHFQSILQT
361 LEEQVSGERQ RLVETHATRV IALINDQRRA ALEGFLAALQ ADPPQAERVL LALRRYLRAE
421 QKEQRHTLRH YQHVAAVDPE KAQQMRFQVH THLQVIEERV NQSLGLLDQN PHLAQELRPQ
481 IQELLHSEHL GPSELEAPAP GGSSEDKGGL QPPDSKDDTP MTLPKGSTEQ DAASPEKEKM
541 NPLEQYERKV NASVPRGFPF HSSEIQRDEL APAGTGVSRE AVSGLLIMGA GGGSLIVLSM
601 LLLRRKKPYG AISHGVVEVD PMLTLEEQQL RELQRHGYEN PTYRFLEERPLocalizationUniProt · AlphaFold · HPA
Whether an antibody against APLP1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Cell surface
- Secreted
- No
- Transmembrane segments
- 1
- Mean surface accessibility (rSASA)
- 0.47
- Highest tissue expression
- 1,120 nTPM
Expression across tissuesHPA
Tissue
- spinal cord: 1,120 nTPM
- midbrain: 493 nTPM
- hippocampal formation: 448 nTPM
- basal ganglia: 372 nTPM
- hypothalamus: 314 nTPM
- cerebral cortex: 289 nTPM
Single-cell type
- oligodendrocytes: 626 nCPM
- pancreatic islet cells: 176 nCPM
- retinal pigment epithelial cells: 175 nCPM
- adrenal medulla cells: 160 nCPM
- retinal bipolar cells: 111 nCPM
- other brain neurons: 99 nCPM
Immune cell
- basophil: 0.6 nTPM
- NK-cell: 0.4 nTPM
- neutrophil: 0.3 nTPM
- naive B-cell: 0.1 nTPM
- classical monocyte: 0 nTPM
- eosinophil: 0 nTPM
Brain region
- white matter: 2,101 nTPM
- medulla oblongata: 1,317 nTPM
- basal ganglia: 1,146 nTPM
- cerebellum: 1,100 nTPM
- pons: 1,043 nTPM
- midbrain: 982 nTPM
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 0.44
- gnomAD pLI
- 0.12
- gnomAD missense Z
- 1.21
- DepMap mean gene effect
- -0.14
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- animal organ morphogenesis
- apoptotic process
- axonogenesis
- cell adhesion
- cellular response to norepinephrine stimulus
- central nervous system development
- cytosolic mRNA polyadenylation
- endocytosis
- extracellular matrix organization
- forebrain development
- negative regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway
- nervous system development
- regulation of translation
Molecular functions
- alpha-2A adrenergic receptor binding
- alpha-2C adrenergic receptor binding
- heparin binding
- identical protein binding
- transition metal ion binding
- alpha-2B adrenergic receptor binding
Cellular components
Protein domainsUniProt · Pfam · InterPro
- Amyloidogenic glycoprotein, extracellular
- Amyloidogenic glycoprotein
- Amyloidogenic glycoprotein, copper-binding
- Amyloidogenic glycoprotein, heparin-binding
- Beta-amyloid precursor protein C-terminal
- Amyloidogenic glycoprotein, copper-binding domain conserved site
- Amyloidogenic glycoprotein, intracellular domain, conserved site
- Amyloidogenic glycoprotein, E2 domain
- E2 domain superfamily
- Amyloidogenic glycoprotein, heparin-binding domain superfamily
- Amyloidogenic glycoprotein, copper-binding domain superfamily
- Amyloid A4 N-terminal heparin-binding
- Beta-amyloid precursor protein C-terminus
- Copper-binding of amyloid precursor, CuBD
- E2 domain of amyloid precursor protein
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of APLP1 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads APLP1 as an antibody target. Whether an autoantibody or antibody against APLP1 could matter depends on whether native APLP1 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
APLP1 is annotated at the cell surface, where native APLP1 is exposed to circulating antibodies and is a prime autoantibody target that could block, deplete, or overstimulate it.
Annotation status
The present source text does not explicitly label APLP1 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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