Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Amyloid-beta A4 protein (ABPP) (APP) (Alzheimer disease amyloid A4 protein homolog) (Amyloid precursor protein) (Amyloid-beta precursor protein) [Cleaved into: N-APP; Soluble APP-alpha (S-APP-alpha); Soluble APP-beta (S-APP-beta); C99 (Beta-secretase C-terminal fragment) (Beta-CTF); Amyloid-beta protein 42 (Abeta42) (Beta-APP42); amyloid-beta protein 40 (Abeta40) (Beta-APP40); C83 (Alpha-secretase C-terminal fragment) (Alpha-CTF); P3(42); P3(40); C80; Gamma-secretase C-terminal fragment 59 (Gamma-CTF(59)); Gamma-secretase C-terminal fragment 57 (Gamma-CTF(57)); Gamma-secretase C-terminal fragment 50 (Gamma-CTF(50)); C31]

 A4_PIG                  Reviewed;         770 AA.
P79307; Q29023; Q9TUI0;
23-APR-2003, integrated into UniProtKB/Swiss-Prot.
23-APR-2003, sequence version 2.
05-DEC-2018, entry version 143.
RecName: Full=Amyloid-beta A4 protein;
AltName: Full=ABPP;
AltName: Full=Alzheimer disease amyloid A4 protein homolog;
AltName: Full=Amyloid precursor protein {ECO:0000305};
AltName: Full=Amyloid-beta precursor protein {ECO:0000305};
RecName: Full=N-APP;
RecName: Full=Soluble APP-alpha;
RecName: Full=Soluble APP-beta;
RecName: Full=C99;
AltName: Full=Beta-secretase C-terminal fragment;
RecName: Full=Amyloid-beta protein 42;
AltName: Full=Beta-APP42;
RecName: Full=amyloid-beta protein 40;
AltName: Full=Beta-APP40;
RecName: Full=C83;
AltName: Full=Alpha-secretase C-terminal fragment;
RecName: Full=P3(42);
RecName: Full=P3(40);
RecName: Full=C80;
RecName: Full=Gamma-secretase C-terminal fragment 59;
AltName: Full=Gamma-CTF(59);
RecName: Full=Gamma-secretase C-terminal fragment 57;
AltName: Full=Gamma-CTF(57);
RecName: Full=Gamma-secretase C-terminal fragment 50;
AltName: Full=Gamma-CTF(50);
RecName: Full=C31;
Flags: Precursor;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Kimura A., Takahashi T.;
"Amyloid precursor protein 770.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
TISSUE=Small intestine;
Winteroe A.K., Fredholm M.;
"Evaluation and characterization of a porcine small intestine cDNA
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
PubMed=1656157; DOI=10.1016/0169-328X(91)90088-F;
Johnstone E.M., Chaney M.O., Norris F.H., Pascual R., Little S.P.;
"Conservation of the sequence of the Alzheimer's disease amyloid
peptide in dog, polar bear and five other mammals by cross-species
polymerase chain reaction analysis.";
Brain Res. Mol. Brain Res. 10:299-305(1991).
-!- FUNCTION: Functions as a cell surface receptor and performs
physiological functions on the surface of neurons relevant to
neurite growth, neuronal adhesion and axonogenesis. Interaction
between APP molecules on neighboring cells promotes
synaptogenesis. Involved in cell mobility and transcription
regulation through protein-protein interactions (By similarity).
Can promote transcription activation through binding to APBB1-KAT5
and inhibit Notch signaling through interaction with Numb (By
similarity). Couples to apoptosis-inducing pathways such as those
mediated by G(O) and JIP (By similarity). Inhibits G(o) alpha
ATPase activity (By similarity). Acts as a kinesin I membrane
receptor, mediating the axonal transport of beta-secretase and
presenilin 1 (By similarity). May be involved in copper
homeostasis/oxidative stress through copper ion reduction (By
similarity). In vitro, copper-metallated APP induces neuronal
death directly or is potentiated through Cu(2+)-mediated low-
density lipoprotein oxidation (By similarity). Can regulate
neurite outgrowth through binding to components of the
extracellular matrix such as heparin and collagen I and IV.
Induces a AGER-dependent pathway that involves activation of p38
MAPK, resulting in internalization of amyloid-beta peptide and
mitochondrial dysfunction in cultured cortical neurons. Provides
Cu(2+) ions for GPC1 which are required for release of nitric
oxide (NO) and subsequent degradation of the heparan sulfate
chains on GPC1 (By similarity). {ECO:0000250,
-!- FUNCTION: Amyloid-beta peptides are lipophilic metal chelators
with metal-reducing activity. Binds transient metals such as
copper, zinc and iron (By similarity). {ECO:0000250}.
-!- FUNCTION: The gamma-CTF peptides as well as the caspase-cleaved
peptides, including C31, are potent enhancers of neuronal
apoptosis. {ECO:0000250}.
-!- FUNCTION: N-APP binds TNFRSF21 triggering caspase activation and
degeneration of both neuronal cell bodies (via caspase-3) and
axons (via caspase-6). {ECO:0000250}.
-!- SUBUNIT: Binds, via its C-terminus, to the PID domain of several
cytoplasmic proteins, including APBB family members, the APBA
family, MAPK8IP1, SHC1 and NUMB and DAB1 (By similarity). Binding
to DAB1 inhibits its serine phosphorylation (By similarity).
Interacts (via NPXY motif) with DAB2 (via PID domain); the
interaction is impaired by tyrosine phosphorylation of the NPXY
motif. Also interacts with GPCR-like protein BPP, FPRL1, APPBP1,
IB1, KNS2 (via its TPR domains), APPBP2 (via BaSS) and DDB1. In
vitro, it binds MAPT via the MT-binding domains (By similarity).
Associates with microtubules in the presence of ATP and in a
kinesin-dependent manner (By similarity). Interacts, through a C-
terminal domain, with GNAO1. Amyloid-beta protein 42 binds CHRNA7
in hippocampal neurons (By similarity). Amyloid-beta associates
with HADH2 (By similarity). Interacts with CPEB1, ANKS1B, TNFRSF21
and AGER (By similarity). Interacts with ITM2B. Interacts with
ITM2C. Interacts with IDE. Can form homodimers; dimerization is
enhanced in the presence of Cu(2+) ions. Can form homodimers; this
is promoted by heparin binding (By similarity). Amyloid-beta
protein 40 interacts with S100A9 (By similarity). CTF-alpha
product of APP interacts with GSAP (By similarity). Interacts with
SORL1 (By similarity). Interacts with PLD3 (By similarity).
Interacts with VDAC1 (By similarity). Interacts with NSG1; could
regulate APP processing (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:P05067, ECO:0000250|UniProtKB:P12023}.
{ECO:0000250|UniProtKB:P05067}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P05067}. Membrane
{ECO:0000250|UniProtKB:P05067}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P05067}. Perikaryon
{ECO:0000250|UniProtKB:P05067}. Cell projection, growth cone
{ECO:0000250|UniProtKB:P05067}. Membrane, clathrin-coated pit
{ECO:0000250|UniProtKB:P05067}. Early endosome
{ECO:0000250|UniProtKB:P05067}. Cytoplasmic vesicle
{ECO:0000250|UniProtKB:P05067}. Note=Cell surface protein that
rapidly becomes internalized via clathrin-coated pits. Only a
minor proportion is present at the cell membrane; most of the
protein is present in intracellular vesicles. During maturation,
the immature APP (N-glycosylated in the endoplasmic reticulum)
moves to the Golgi complex where complete maturation occurs (O-
glycosylated and sulfated). After alpha-secretase cleavage,
soluble APP is released into the extracellular space and the C-
terminal is internalized to endosomes and lysosomes. Some APP
accumulates in secretory transport vesicles leaving the late Golgi
compartment and returns to the cell surface. Gamma-CTF(59) peptide
is located to both the cytoplasm and nuclei of neurons. It can be
translocated to the nucleus through association with APBB1 (Fe65).
Amyloid-beta protein 42 associates with FRPL1 at the cell surface
and the complex is then rapidly internalized. APP sorts to the
basolateral surface in epithelial cells. During neuronal
differentiation, the Thr-743 phosphorylated form is located mainly
in growth cones, moderately in neurites and sparingly in the cell
body. Casein kinase phosphorylation can occur either at the cell
surface or within a post-Golgi compartment. Associates with GPC1
in perinuclear compartments. Colocalizes with SORL1 in a vesicular
pattern in cytoplasm and perinuclear regions.
-!- DOMAIN: The basolateral sorting signal (BaSS) is required for
sorting of membrane proteins to the basolateral surface of
epithelial cells. {ECO:0000250|UniProtKB:P05067}.
-!- DOMAIN: The GFLD subdomain binds Cu(2+) ions; this promotes
homodimerization. {ECO:0000250|UniProtKB:P05067}.
-!- 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 PID domain-containing proteins which bind APP
require the YENPTY motif for full interaction. These interactions
are independent of phosphorylation on the terminal tyrosine
residue. The YENPXY site is also involved in clathrin-mediated
endocytosis. {ECO:0000250|UniProtKB:P05067}.
-!- DOMAIN: The C-terminal region can bind zinc ions; this favors
dimerization and formation of higher oligomers.
-!- PTM: Proteolytically processed under normal cellular conditions.
Cleavage either by alpha-secretase, beta-secretase or theta-
secretase leads to generation and extracellular release of soluble
APP peptides, S-APP-alpha and S-APP-beta, and the retention of
corresponding membrane-anchored C-terminal fragments, C80, C83 and
C99. Subsequent processing of C80 and C83 by gamma-secretase
yields P3 peptides. This is the major secretory pathway and is
non-amyloidogenic. Alternatively, presenilin/nicastrin-mediated
gamma-secretase processing of C99 releases the amyloid-beta
proteins, amyloid-beta protein 40 and amyloid-beta protein 42,
major components of amyloid plaques, and the cytotoxic C-terminal
fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59) (By
similarity). {ECO:0000250}.
-!- PTM: Proteolytically cleaved by caspases during neuronal
apoptosis. Cleavage at Asp-739 by either caspase-3, -8 or -9
results in the production of the neurotoxic C31 peptide and the
increased production of amyloid-beta peptides. {ECO:0000250}.
-!- PTM: N- and O-glycosylated. {ECO:0000250}.
-!- PTM: Phosphorylation in the C-terminal on tyrosine, threonine and
serine residues is neuron-specific. Phosphorylation can affect APP
processing, neuronal differentiation and interaction with other
proteins (By similarity). {ECO:0000250}.
-!- PTM: Extracellular binding and reduction of copper, results in a
corresponding oxidation of Cys-144 and Cys-158, and the formation
of a disulfide bond. {ECO:0000250}.
-!- PTM: Trophic-factor deprivation triggers the cleavage of surface
APP by beta-secretase to release sAPP-beta which is further
cleaved to release an N-terminal fragment of APP (N-APP).
-!- PTM: Amyloid-beta peptides are degraded by IDE. {ECO:0000250}.
-!- MISCELLANEOUS: Chelation of metal ions, notably copper, iron and
zinc, can induce histidine-bridging between amyloid-beta molecules
resulting in amyloid-beta-metal aggregates. Extracellular zinc-
binding increases binding of heparin to APP and inhibits collagen-
binding. {ECO:0000250}.
-!- SIMILARITY: Belongs to the APP family. {ECO:0000255|PROSITE-
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
EMBL; AB032550; BAA84580.1; -; mRNA.
EMBL; Z84022; CAB06313.1; -; mRNA.
EMBL; X56127; CAA39592.1; -; mRNA.
PIR; F60045; F60045.
RefSeq; NP_999537.1; NM_214372.1.
UniGene; Ssc.14258; -.
UniGene; Ssc.59825; -.
UniGene; Ssc.83894; -.
ProteinModelPortal; P79307; -.
SMR; P79307; -.
STRING; 9823.ENSSSCP00000012805; -.
MEROPS; I02.015; -.
PaxDb; P79307; -.
PeptideAtlas; P79307; -.
PRIDE; P79307; -.
Ensembl; ENSSSCT00000041749; ENSSSCP00000034553; ENSSSCG00000012022.
GeneID; 397663; -.
KEGG; ssc:397663; -.
CTD; 351; -.
eggNOG; KOG3540; Eukaryota.
GeneTree; ENSGT00530000063252; -.
HOGENOM; HOG000232190; -.
HOVERGEN; HBG000051; -.
InParanoid; P79307; -.
KO; K04520; -.
Reactome; R-SSC-114608; Platelet degranulation.
Reactome; R-SSC-1810476; RIP-mediated NFkB activation via ZBP1.
Reactome; R-SSC-3000178; ECM proteoglycans.
Reactome; R-SSC-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
Reactome; R-SSC-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-SSC-416476; G alpha (q) signalling events.
Reactome; R-SSC-418594; G alpha (i) signalling events.
Reactome; R-SSC-432720; Lysosome Vesicle Biogenesis.
Reactome; R-SSC-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-SSC-879415; Advanced glycosylation endproduct receptor signaling.
Reactome; R-SSC-8957275; Post-translational protein phosphorylation.
Reactome; R-SSC-933542; TRAF6 mediated NF-kB activation.
ChiTaRS; APP; pig.
Proteomes; UP000008227; Chromosome 13.
ExpressionAtlas; P79307; baseline and differential.
GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
GO; GO:0035253; C:ciliary rootlet; IEA:Ensembl.
GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0043198; C:dendritic shaft; IEA:Ensembl.
GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
GO; GO:0005769; C:early endosome; ISS:UniProtKB.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0005798; C:Golgi-associated vesicle; ISS:UniProtKB.
GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
GO; GO:0005641; C:nuclear envelope lumen; IEA:Ensembl.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0048786; C:presynaptic active zone; IEA:Ensembl.
GO; GO:0043235; C:receptor complex; IEA:Ensembl.
GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
GO; GO:0005790; C:smooth endoplasmic reticulum; IEA:GOC.
GO; GO:0051233; C:spindle midzone; IEA:Ensembl.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0051425; F:PTB domain binding; IEA:Ensembl.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
GO; GO:0008344; P:adult locomotory behavior; ISS:UniProtKB.
GO; GO:1990000; P:amyloid fibril formation; IEA:Ensembl.
GO; GO:0002265; P:astrocyte activation involved in immune response; IEA:Ensembl.
GO; GO:0008088; P:axo-dendritic transport; ISS:UniProtKB.
GO; GO:0016199; P:axon midline choice point recognition; ISS:UniProtKB.
GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0006878; P:cellular copper ion homeostasis; ISS:UniProtKB.
GO; GO:1904646; P:cellular response to amyloid-beta; IEA:Ensembl.
GO; GO:0008203; P:cholesterol metabolic process; IEA:Ensembl.
GO; GO:0050890; P:cognition; ISS:UniProtKB.
GO; GO:0048669; P:collateral sprouting in absence of injury; ISS:UniProtKB.
GO; GO:0016358; P:dendrite development; ISS:UniProtKB.
GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
GO; GO:0030198; P:extracellular matrix organization; ISS:UniProtKB.
GO; GO:0030900; P:forebrain development; IEA:Ensembl.
GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007626; P:locomotory behavior; ISS:UniProtKB.
GO; GO:0007617; P:mating behavior; ISS:UniProtKB.
GO; GO:0014005; P:microglia development; IEA:Ensembl.
GO; GO:0090647; P:modulation of age-related behavioral decline; IEA:Ensembl.
GO; GO:0098815; P:modulation of excitatory postsynaptic potential; IEA:Ensembl.
GO; GO:0006378; P:mRNA polyadenylation; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; IEA:Ensembl.
GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl.
GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
GO; GO:1990535; P:neuron projection maintenance; IEA:Ensembl.
GO; GO:0016322; P:neuron remodeling; ISS:UniProtKB.
GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
GO; GO:1905908; P:positive regulation of amyloid fibril formation; IEA:Ensembl.
GO; GO:1902004; P:positive regulation of amyloid-beta formation; IEA:Ensembl.
GO; GO:0061890; P:positive regulation of astrocyte activation; IEA:Ensembl.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IEA:Ensembl.
GO; GO:0046330; P:positive regulation of JNK cascade; IEA:Ensembl.
GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IEA:Ensembl.
GO; GO:1903980; P:positive regulation of microglial cell activation; IEA:Ensembl.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISS:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IEA:Ensembl.
GO; GO:0032092; P:positive regulation of protein binding; IEA:Ensembl.
GO; GO:2000406; P:positive regulation of T cell migration; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
GO; GO:0007176; P:regulation of epidermal growth factor-activated receptor activity; ISS:UniProtKB.
GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IEA:Ensembl.
GO; GO:0040014; P:regulation of multicellular organism growth; ISS:UniProtKB.
GO; GO:1905606; P:regulation of presynapse assembly; IEA:Ensembl.
GO; GO:0150003; P:regulation of spontaneous synaptic transmission; IEA:Ensembl.
GO; GO:0050803; P:regulation of synapse structure or activity; ISS:UniProtKB.
GO; GO:0006417; P:regulation of translation; ISS:UniProtKB.
GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
GO; GO:0051563; P:smooth endoplasmic reticulum calcium ion homeostasis; IEA:Ensembl.
GO; GO:0001967; P:suckling behavior; IEA:Ensembl.
GO; GO:0051124; P:synaptic growth at neuromuscular junction; IEA:Ensembl.
GO; GO:0032640; P:tumor necrosis factor production; IEA:Ensembl.
GO; GO:0008542; P:visual learning; ISS:UniProtKB.
CDD; cd00109; KU; 1.
Gene3D;; -; 1.
Gene3D;; -; 1.
Gene3D; 3.30.1490.140; -; 1.
Gene3D; 3.90.570.10; -; 1.
Gene3D;; -; 1.
Gene3D; 4.10.410.10; -; 1.
InterPro; IPR036669; Amyloid_Cu-bd_sf.
InterPro; IPR008155; Amyloid_glyco.
InterPro; IPR013803; Amyloid_glyco_Abeta.
InterPro; IPR037071; Amyloid_glyco_Abeta_sf.
InterPro; IPR011178; Amyloid_glyco_Cu-bd.
InterPro; IPR024329; Amyloid_glyco_E2_domain.
InterPro; IPR008154; Amyloid_glyco_extra.
InterPro; IPR019744; Amyloid_glyco_extracell_CS.
InterPro; IPR015849; Amyloid_glyco_heparin-bd.
InterPro; IPR036454; Amyloid_glyco_heparin-bd_sf.
InterPro; IPR019745; Amyloid_glyco_intracell_CS.
InterPro; IPR028866; APP.
InterPro; IPR019543; APP_amyloid_C.
InterPro; IPR036176; E2_sf.
InterPro; IPR002223; Kunitz_BPTI.
InterPro; IPR036880; Kunitz_BPTI_sf.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR020901; Prtase_inh_Kunz-CS.
PANTHER; PTHR23103; PTHR23103; 1.
PANTHER; PTHR23103:SF7; PTHR23103:SF7; 1.
Pfam; PF10515; APP_amyloid; 1.
Pfam; PF12924; APP_Cu_bd; 1.
Pfam; PF12925; APP_E2; 1.
Pfam; PF02177; APP_N; 1.
Pfam; PF03494; Beta-APP; 1.
Pfam; PF00014; Kunitz_BPTI; 1.
SMART; SM00006; A4_EXTRA; 1.
SMART; SM00131; KU; 1.
SUPFAM; SSF109843; SSF109843; 1.
SUPFAM; SSF56491; SSF56491; 1.
SUPFAM; SSF57362; SSF57362; 1.
SUPFAM; SSF89811; SSF89811; 1.
PROSITE; PS51869; APP_E1; 1.
PROSITE; PS51870; APP_E2; 1.
2: Evidence at transcript level;
Amyloid; Apoptosis; Cell adhesion; Cell membrane; Cell projection;
Coated pit; Complete proteome; Copper; Cytoplasmic vesicle;
Disulfide bond; Endocytosis; Endosome; Glycoprotein; Heparin-binding;
Iron; Isopeptide bond; Membrane; Metal-binding;
Notch signaling pathway; Phosphoprotein; Protease inhibitor;
Reference proteome; Serine protease inhibitor; Signal; Transmembrane;
Transmembrane helix; Ubl conjugation; Zinc.
SIGNAL 1 17 {ECO:0000250|UniProtKB:P05067}.
CHAIN 18 770 Amyloid-beta A4 protein.
CHAIN 18 687 Soluble APP-alpha. {ECO:0000255}.
CHAIN 18 671 Soluble APP-beta. {ECO:0000255}.
CHAIN 18 286 N-APP. {ECO:0000250}.
CHAIN 672 770 C99. {ECO:0000250}.
CHAIN 672 713 Amyloid-beta protein 42. {ECO:0000250}.
CHAIN 672 711 amyloid-beta protein 40. {ECO:0000250}.
CHAIN 688 770 C83. {ECO:0000250}.
PEPTIDE 688 713 P3(42). {ECO:0000250}.
PEPTIDE 688 711 P3(40). {ECO:0000250}.
CHAIN 691 770 C80.
CHAIN 712 770 Gamma-secretase C-terminal fragment 59.
CHAIN 714 770 Gamma-secretase C-terminal fragment 57.
CHAIN 721 770 Gamma-secretase C-terminal fragment 50.
CHAIN 740 770 C31. {ECO:0000250}.
TOPO_DOM 18 699 Extracellular. {ECO:0000255}.
TRANSMEM 700 723 Helical. {ECO:0000255}.
TOPO_DOM 724 770 Cytoplasmic. {ECO:0000255}.
DOMAIN 28 189 E1. {ECO:0000255|PROSITE-
DOMAIN 291 341 BPTI/Kunitz inhibitor.
DOMAIN 374 565 E2. {ECO:0000255|PROSITE-
REGION 28 123 GFLD subdomain. {ECO:0000255|PROSITE-
REGION 96 110 Heparin-binding. {ECO:0000250}.
REGION 131 189 CuBD subdomain. {ECO:0000255|PROSITE-
REGION 135 155 Copper-binding. {ECO:0000250}.
REGION 181 188 Zinc-binding. {ECO:0000250}.
REGION 391 423 Heparin-binding. {ECO:0000250}.
REGION 491 522 Heparin-binding. {ECO:0000250}.
REGION 523 540 Collagen-binding. {ECO:0000250}.
REGION 732 751 Interaction with G(o)-alpha.
MOTIF 724 734 Basolateral sorting signal.
MOTIF 757 762 YENPXY motif; contains endocytosis
signal. {ECO:0000250|UniProtKB:P05067}.
COMPBIAS 230 260 Asp/Glu-rich (acidic).
COMPBIAS 274 280 Poly-Thr.
METAL 147 147 Copper 1. {ECO:0000255|PROSITE-
METAL 151 151 Copper 1. {ECO:0000255|PROSITE-
METAL 168 168 Copper 1. {ECO:0000255|PROSITE-
METAL 677 677 Copper or zinc 2.
METAL 681 681 Copper or zinc 2.
METAL 684 684 Copper or zinc 2.
METAL 685 685 Copper or zinc 2.
SITE 170 170 Required for Cu(2+) reduction.
SITE 301 302 Reactive bond. {ECO:0000250}.
SITE 671 672 Cleavage; by beta-secretase.
SITE 672 673 Cleavage; by caspase-6. {ECO:0000250}.
SITE 687 688 Cleavage; by alpha-secretase.
SITE 690 691 Cleavage; by theta-secretase.
SITE 704 704 Implicated in free radical propagation.
SITE 711 712 Cleavage; by gamma-secretase; site 1.
SITE 713 714 Cleavage; by gamma-secretase; site 2.
SITE 720 721 Cleavage; by gamma-secretase; site 3.
SITE 739 740 Cleavage; by caspase-6, caspase-8 or
caspase-9. {ECO:0000250}.
MOD_RES 198 198 Phosphoserine; by CK2.
MOD_RES 206 206 Phosphoserine; by CK1.
MOD_RES 441 441 Phosphoserine.
MOD_RES 497 497 Phosphotyrosine.
MOD_RES 729 729 Phosphothreonine.
MOD_RES 730 730 Phosphoserine; by APP-kinase I.
MOD_RES 743 743 Phosphothreonine; by CDK5 and MAPK10.
MOD_RES 757 757 Phosphotyrosine; by ABL1.
CARBOHYD 542 542 N-linked (GlcNAc...) asparagine.
CARBOHYD 571 571 N-linked (GlcNAc...) asparagine.
DISULFID 38 62 {ECO:0000255|PROSITE-ProRule:PRU01217}.
DISULFID 73 117 {ECO:0000255|PROSITE-ProRule:PRU01217}.
DISULFID 98 105 {ECO:0000255|PROSITE-ProRule:PRU01217}.
DISULFID 133 187 {ECO:0000255|PROSITE-ProRule:PRU01217}.
DISULFID 144 174 {ECO:0000255|PROSITE-ProRule:PRU01217}.
DISULFID 158 186 {ECO:0000255|PROSITE-ProRule:PRU01217}.
DISULFID 291 341 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 300 324 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 316 337 {ECO:0000255|PROSITE-ProRule:PRU00031}.
CROSSLNK 763 763 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
CONFLICT 134 136 KFL -> SSY (in Ref. 2; CAB06313).
SEQUENCE 770 AA; 86961 MW; 5F7A1DCB2BCC583E CRC64;

Related products :

Catalog number Product name Quantity
orb60003 beta Amyloid Beta-amyloid 1-42 is known as a biomarker of manifest AD that is detectable in cerebrospinal fluid (CSF). It is the 42-amino acid fragment of amyloid precursor protein. For research use o 1 mg
Q2B910G Beta Amyloid Cleaving Enzyme (BACE) beta-Secretase, C-terminal host: Goat 1mL
Y051548 to BACE-1 Memapsin-2 Beta Secretase-1 β-Site Amyloid Precursor Protein-cleaving Enzyme-1 ASP-2; Stalk region antibody 250ug
Y051551 Anti-BACE-2 Memapsin-1 Beta Secretase-2 β-Site Amyloid Precursor Protein-cleaving Enzyme-2 ASP-1; Stalk region antibody 250ug
Y051551 Anti-BACE-2 (Memapsin-1, Beta Secretase-2, β-Site Amyloid Precursor Protein-cleaving Enzyme-2, ASP-1); Stalk region Antibody 100μg
Y051552 Anti-BACE-2 (Memapsin-1, Beta Secretase-2, β-Site Amyloid Precursor Protein-cleaving Enzyme-2, ASP-1); Cytoplacmic domain Antibody 100μg
Y051547 Anti-BACE-1 Memapsin-2 Beta Secretase-1 β-Site Amyloid Precursor Protein-cleaving Enzyme-1 ASP-2; Catalytic domain antibody 250ug
Y051550 Anti-BACE-2 (Memapsin-1, Beta Secretase-2, β-Site Amyloid Precursor Protein-cleaving Enzyme-2, ASP-1); Catalytic domain Antibody 100μg
Y051552 Anti-BACE-2 Memapsin-1 Beta Secretase-2 β-Site Amyloid Precursor Protein-cleaving Enzyme-2 ASP-1; Cytoplacmic domain antibody 250ug
Y051549 Anti-BACE-1 Memapsin-2 Beta Secretase-1 β-Site Amyloid Precursor Protein-cleaving Enzyme-1 ASP-2; Cytoplasmic domain antibody 250ug
Y051550 Anti-BACE-2 Memapsin-1 Beta Secretase-2 β-Site Amyloid Precursor Protein-cleaving Enzyme-2 ASP-1; Catalytic domain antibody 250ug
20-272-191484 beta amyloid 1-43 - Mouse monoclonal [4H309] to beta amyloid 1-43; APP; ABPP; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; Protease nexin-II; PN-II; APPI; PreA4 Monoclon 0.05 ml
20-272-191483 beta Amyloid 1-40 - Mouse monoclonal [4H308] to beta Amyloid 1-40; APP; ABPP; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; Protease nexin-II; PN-II; APPI; PreA4 Monoclon 0.05 ml
18-783-75671 RABBIT ANTI AMYLOID BETA (N-TERMINAL) - APP; ABPP; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; Protease nexin-II; PN-II; APPI; PreA4 Polyclonal 0.1 ml
27-061 APBB2 may modulate the internalization of beta-amyloid precursor protein.The protein encoded by this gene interacts with the cytoplasmic domains of amyloid beta (A4) precursor protein and amyloid beta 0.05 mg
20-272-190774 beta Amyloid - Mouse monoclonal [2C8] to beta Amyloid; APP; ABPP; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; Protease nexin-II; PN-II; APPI; PreA4 Monoclonal 0.05 mg
20-272-191574 beta Amyloid - Mouse monoclonal [3G5] to beta Amyloid; APP; ABPP; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; Protease nexin-II; PN-II; APPI; PreA4 Monoclonal 0.05 mg
18-272-197116 beta Amyloid - Rabbit polyclonal to beta Amyloid; APP; ABPP; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; Protease nexin-II; PN-II; APPI; PreA4 Polyclonal 0.1 mg
20-272-190378 beta Amyloid - Mouse monoclonal [DE2B4] to beta Amyloid; APP; ABPP; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; Protease nexin-II; PN-II; APPI; PreA4 Monoclonal 0.05 mg
E0718b ELISA BACE1,Beta-secretase 1,Beta-site amyloid precursor protein cleaving enzyme 1,Beta-site APP cleaving enzyme 1,Bos taurus,Bovine,Memapsin-2,Membrane-associated aspartic protease 2 96T
E0718b ELISA kit BACE1,Beta-secretase 1,Beta-site amyloid precursor protein cleaving enzyme 1,Beta-site APP cleaving enzyme 1,Bos taurus,Bovine,Memapsin-2,Membrane-associated aspartic protease 2 96T
U0718b CLIA BACE1,Beta-secretase 1,Beta-site amyloid precursor protein cleaving enzyme 1,Beta-site APP cleaving enzyme 1,Bos taurus,Bovine,Memapsin-2,Membrane-associated aspartic protease 2 96T
E1812r ELISA kit Bace2,Beta-secretase 2,Beta-site amyloid precursor protein cleaving enzyme 2,Beta-site APP cleaving enzyme 2,Memapsin-1,Membrane-associated aspartic protease 1,Rat,Rattus norvegicus,Theta-s 96T
U1812r CLIA kit Bace2,Beta-secretase 2,Beta-site amyloid precursor protein cleaving enzyme 2,Beta-site APP cleaving enzyme 2,Memapsin-1,Membrane-associated aspartic protease 1,Rat,Rattus norvegicus,Theta-se 96T
E0718r ELISA kit Asp 2,ASP2,Aspartyl protease 2,Bace,Bace1,Beta-secretase 1,Beta-site amyloid precursor protein cleaving enzyme 1,Beta-site APP cleaving enzyme 1,Memapsin-2,Membrane-associated aspartic prot 96T


GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur | Gentaur

Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | Gentaur



9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017
RIB 30004 00187 00010092253 10
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: +49 0241 40 08 90 86, +49 0241 95 78 94 78, +49 0241 40 08 90 86
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur | Gentaur

Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123

GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U

spain@gentaur.com | Gentaur | Gentaur

ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur | Gentaur
IBAN: BG11FINV91501014771636

GENTAUR Poland Sp. z o.o.

ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556


Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur | Gentaur