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 A4_MOUSE                Reviewed;         770 AA.
P12023; P97487; P97942; Q99K32;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
09-MAY-2003, sequence version 3.
30-AUG-2017, entry version 214.
RecName: Full=Amyloid beta A4 protein;
AltName: Full=ABPP;
Short=APP;
AltName: Full=Alzheimer disease amyloid A4 protein homolog;
AltName: Full=Amyloid precursor protein {ECO:0000305};
AltName: Full=Amyloidogenic glycoprotein;
Short=AG;
AltName: Full=Beta-amyloid precursor protein {ECO:0000305};
Contains:
RecName: Full=N-APP;
Contains:
RecName: Full=Soluble APP-alpha;
Short=S-APP-alpha;
Contains:
RecName: Full=Soluble APP-beta;
Short=S-APP-beta;
Contains:
RecName: Full=C99;
AltName: Full=APP-C99;
Contains:
RecName: Full=Beta-amyloid protein 42;
AltName: Full=Beta-APP42;
Contains:
RecName: Full=Beta-amyloid protein 40;
AltName: Full=Beta-APP40;
Contains:
RecName: Full=C83;
Contains:
RecName: Full=P3(42);
Contains:
RecName: Full=P3(40);
Contains:
RecName: Full=C80;
Contains:
RecName: Full=Gamma-secretase C-terminal fragment 59;
AltName: Full=APP-C59;
AltName: Full=Amyloid intracellular domain 59;
Short=AID(59);
AltName: Full=Gamma-CTF(59);
Contains:
RecName: Full=Gamma-secretase C-terminal fragment 57;
AltName: Full=APP-C57;
AltName: Full=Amyloid intracellular domain 57;
Short=AID(57);
AltName: Full=Gamma-CTF(57);
Contains:
RecName: Full=Gamma-secretase C-terminal fragment 50;
AltName: Full=Amyloid intracellular domain 50;
Short=AID(50);
AltName: Full=Gamma-CTF(50);
Contains:
RecName: Full=C31;
Flags: Precursor;
Name=App;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM APP695).
TISSUE=Brain;
PubMed=3322280; DOI=10.1016/0006-291X(87)90419-0;
Yamada T., Sasaki H., Furuya H., Miyata T., Goto I., Sakaki Y.;
"Complementary DNA for the mouse homolog of the human amyloid beta
protein precursor.";
Biochem. Biophys. Res. Commun. 149:665-671(1987).
[2]
SEQUENCE REVISION.
Yamada T.;
Submitted (MAR-1988) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM APP695).
STRAIN=BALB/cJ; TISSUE=Brain;
PubMed=1756177; DOI=10.1016/0167-4781(91)90231-A;
de Strooper B., van Leuven F., van den Berghe H.;
"The amyloid beta protein precursor or proteinase nexin II from mouse
is closer related to its human homolog than previously reported.";
Biochim. Biophys. Acta 1129:141-143(1991).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM APP695).
STRAIN=SAMP8; TISSUE=Hippocampus;
PubMed=11235921; DOI=10.1139/o00-094;
Kumar V.B., Vyas K., Franko M., Choudhary V., Buddhiraju C.,
Alvarez J., Morley J.E.;
"Molecular cloning, expression, and regulation of hippocampal amyloid
precursor protein of senescence accelerated mouse (SAMP8).";
Biochem. Cell Biol. 79:57-67(2001).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
PubMed=1555768; DOI=10.1016/0378-1119(92)90375-Y;
Izumi R., Yamada T., Yoshikai S., Sasaki H., Hattori M., Sakai Y.;
"Positive and negative regulatory elements for the expression of the
Alzheimer's disease amyloid precursor-encoding gene in mouse.";
Gene 112:189-195(1992).
[6]
PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM APP770).
TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 281-380, AND ALTERNATIVE SPLICING.
TISSUE=Brain, and Kidney;
PubMed=2493250; DOI=10.1016/0006-291X(89)92808-8;
Yamada T., Sasaki H., Dohura K., Goto I., Sakaki Y.;
"Structure and expression of the alternatively-spliced forms of mRNA
for the mouse homolog of Alzheimer's disease amyloid beta protein
precursor.";
Biochem. Biophys. Res. Commun. 158:906-912(1989).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 289-364.
STRAIN=CD-1; TISSUE=Placenta;
PubMed=2569710; DOI=10.1093/nar/17.13.5396;
Fukuchi K., Martin G.M., Deeb S.S.;
"Sequence of the protease inhibitor domain of the A4 amyloid protein
precursor of Mus domesticus.";
Nucleic Acids Res. 17:5396-5396(1989).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 656-737.
STRAIN=129/Sv;
Wragg M.A., Busfield F., Duff K., Korenblat K., Capecchi M.,
Loring J.F., Goate A.M.;
"Introduction of six mutations into the mouse genome using 'Hit and
Run' gene-targeting: introduction of familial Alzheimer's disease
mutations into the mouse amyloid precursor protein gene and
humanization of the A-beta fragment.";
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
[10]
TISSUE SPECIFICITY OF ALTERNATIVE SPLICED FORMS.
PubMed=8510506; DOI=10.1016/0169-328X(93)90020-P;
Sola C., Mengod G., Ghetti B., Palacios J.M., Triarhou L.C.;
"Regional distribution of the alternatively spliced isoforms of beta
APP RNA transcript in the brain of normal, heterozygous and homozygous
weaver mutant mice as revealed by in situ hybridization
histochemistry.";
Brain Res. Mol. Brain Res. 17:340-346(1993).
[11]
INTERACTION WITH KNS2.
PubMed=11144355; DOI=10.1016/S0896-6273(00)00124-0;
Kamal A., Stokin G.B., Yang Z., Xia C.-H., Goldstein L.S.;
"Axonal transport of amyloid precursor protein is mediated by direct
binding to the kinesin light chain subunit of kinesin-I.";
Neuron 28:449-459(2000).
[12]
PHOSPHORYLATION AT TYR-757.
PubMed=11279131; DOI=10.1074/jbc.M100792200;
Zambrano N., Bruni P., Minopoli G., Mosca R., Molino D., Russo C.,
Schettini G., Sudol M., Russo T.;
"The beta-amyloid precursor protein APP is tyrosine-phosphorylated in
cells expressing a constitutively active form of the Abl
protoncogene.";
J. Biol. Chem. 276:19787-19792(2001).
[13]
C-TERMINAL PROTEIN-PROTEIN INTERACTION, AND MUTAGENESIS OF TYR-728;
THR-743; TYR-757; ASN-759 AND TYR-762.
PubMed=11517249;
Matsuda S., Yasukawa T., Homma Y., Ito Y., Niikura T., Hiraki T.,
Hirai S., Ohno S., Kita Y., Kawasumi M., Kouyama K., Yamamoto T.,
Kyriakis J.M., Nishimoto I.;
"C-jun N-terminal kinase (JNK)-interacting protein-1b/islet-brain-1
scaffolds Alzheimer's amyloid precursor protein with JNK.";
J. Neurosci. 21:6597-6607(2001).
[14]
INTERACTION WITH DAB2, AND MUTAGENESIS OF GLY-756; TYR-757; ASN-759;
PRO-760 AND TYR-762.
PubMed=11247302; DOI=10.1034/j.1600-0854.2001.020206.x;
Morris S.M., Cooper J.A.;
"Disabled-2 colocalizes with the LDLR in clathrin-coated pits and
interacts with AP-2.";
Traffic 2:111-123(2001).
[15]
INTERACTION WITH MAPK8IP1, AND PHOSPHORYLATION.
PubMed=11912189; DOI=10.1074/jbc.M108372200;
Taru H., Iijima K., Hase M., Kirino Y., Yagi Y., Suzuki T.;
"Interaction of Alzheimer's beta-amyloid precursor family proteins
with scaffold proteins of the JNK signaling cascade.";
J. Biol. Chem. 277:20070-20078(2002).
[16]
INTERACTION OF CTF PEPTIDES WITH NUMB.
PubMed=12011466; DOI=10.1073/pnas.102192599;
Roncarati R., Sestan N., Scheinfeld M.H., Berechid B.E., Lopez P.A.,
Meucci O., McGlade J.C., Rakic P., D'Adamio L.;
"The gamma-secretase-generated intracellular domain of beta-amyloid
precursor protein binds Numb and inhibits Notch signaling.";
Proc. Natl. Acad. Sci. U.S.A. 99:7102-7107(2002).
[17]
PROTEOLYTIC PROCESSING BY GAMMA SECRETASE, AND INTERACTION WITH APBB1.
PubMed=11553691; DOI=10.1046/j.1471-4159.2001.00516.x;
Cupers P., Orlans I., Craessaerts K., Annaert W., De Strooper B.;
"The amyloid precursor protein (APP)-cytoplasmic fragment generated by
gamma-secretase is rapidly degraded but distributes partially in a
nuclear fraction of neurons in culture.";
J. Neurochem. 78:1168-1178(2001).
[18]
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=15677459; DOI=10.1074/jbc.M409179200;
Cappai R., Cheng F., Ciccotosto G.D., Needham B.E., Masters C.L.,
Multhaup G., Fransson L.A., Mani K.;
"The amyloid precursor protein (APP) of Alzheimer disease and its
paralog, APLP2, modulate the Cu/Zn-nitric oxide-catalyzed degradation
of glypican-1 heparan sulfate in vivo.";
J. Biol. Chem. 280:13913-13920(2005).
[19]
INTERACTION WITH CPEB1.
PubMed=16314516; DOI=10.1128/MCB.25.24.10930-10939.2005;
Cao Q., Huang Y.-S., Kan M.-C., Richter J.D.;
"Amyloid precursor proteins anchor CPEB to membranes and promote
polyadenylation-induced translation.";
Mol. Cell. Biol. 25:10930-10939(2005).
[20]
INTERACTION WITH APP.
PubMed=16174740; DOI=10.1073/pnas.0503689102;
Andersen O.M., Reiche J., Schmidt V., Gotthardt M., Spoelgen R.,
Behlke J., von Arnim C.A., Breiderhoff T., Jansen P., Wu X.,
Bales K.R., Cappai R., Masters C.L., Gliemann J., Mufson E.J.,
Hyman B.T., Paul S.M., Nykjaer A., Willnow T.E.;
"Neuronal sorting protein-related receptor sorLA/LR11 regulates
processing of the amyloid precursor protein.";
Proc. Natl. Acad. Sci. U.S.A. 102:13461-13466(2005).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-441, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Kidney, Lung, Pancreas, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[22]
INTERACTION WITH VDAC1.
PubMed=25168729; DOI=10.1016/j.neuroscience.2014.07.079;
Fernandez-Echevarria C., Diaz M., Ferrer I., Canerina-Amaro A.,
Marin R.;
"Abeta promotes VDAC1 channel dephosphorylation in neuronal lipid
rafts. Relevance to the mechanisms of neurotoxicity in Alzheimer's
disease.";
Neuroscience 278:354-366(2014).
-!- FUNCTION: Functions as a cell surface receptor and performs
physiological functions on the surface of neurons relevant to
neurite growth, neuronal adhesion and axonogenesis. Involved in
cell mobility and transcription regulation through protein-protein
interactions. Can promote transcription activation through binding
to APBB1-KAT5 and inhibit Notch signaling through interaction with
Numb. Couples to apoptosis-inducing pathways such as those
mediated by G(O) and JIP. 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. May be
involved in copper homeostasis/oxidative stress through copper ion
reduction. Can regulate neurite outgrowth through binding to
components of the extracellular matrix such as heparin and
collagen I and IV (By similarity). The splice isoforms that
contain the BPTI domain possess protease inhibitor activity.
Induces a AGER-dependent pathway that involves activation of p38
MAPK, resulting in internalization of amyloid-beta peptide and
leading to mitochondrial dysfunction in cultured cortical neurons
(By similarity). 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. {ECO:0000250,
ECO:0000269|PubMed:15677459}.
-!- FUNCTION: Beta-amyloid peptides are lipophilic metal chelators
with metal-reducing activity. Binds transient metals such as
copper, zinc and iron. Rat and mouse beta-amyloid peptides bind
only weakly transient metals and have little reducing activity due
to substitutions of transient metal chelating residues. Beta-APP42
may activate mononuclear phagocytes in the brain and elicit
inflammatory responses. Promotes both tau aggregation and TPK II-
mediated phosphorylation. Also binds GPC1 in lipid rafts (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:0000269|PubMed:15677459}.
-!- 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, NUMB and DAB1. Binding to DAB1 inhibits
its serine phosphorylation. 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 (By similarity). 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 (By similarity). Amyloid beta-42 binds CHRNA7 in
hippocampal neurons (By similarity). Beta-amyloid associates with
HADH2 (By similarity). Interacts with ANKS1B, TNFRSF21 and AGER
(By similarity). Interacts with CPEB1. Interacts with ITM2B.
Interacts with ITM2C. Interacts with IDE. Can form homodimers;
this is promoted by heparin binding (By similarity). Beta-amyloid
protein 40 interacts with S100A9 (By similarity). CTF-alpha
product of APP interacts with GSAP (By similarity). Interacts with
SORL1. Interacts with PLD3 (By similarity). Interacts with VDAC1
(PubMed:25168729). {ECO:0000250, ECO:0000269|PubMed:25168729}.
-!- INTERACTION:
P98084:Apba2; NbExp=2; IntAct=EBI-78814, EBI-81669;
Q9QXJ1:Apbb1; NbExp=2; IntAct=EBI-78814, EBI-81338;
Q03157:Aplp1; NbExp=4; IntAct=EBI-78814, EBI-399929;
Q06335:Aplp2; NbExp=3; IntAct=EBI-78814, EBI-446708;
P15253:CALR (xeno); NbExp=2; IntAct=EBI-78814, EBI-9005200;
P14211:Calr; NbExp=4; IntAct=EBI-78814, EBI-644340;
P97318:Dab1; NbExp=3; IntAct=EBI-78814, EBI-81680;
Q62108:Dlg4; NbExp=4; IntAct=EBI-78814, EBI-300895;
Q9D1T0:Lingo1; NbExp=2; IntAct=EBI-78814, EBI-2012981;
Q9UQF2:MAPK8IP1 (xeno); NbExp=2; IntAct=EBI-78814, EBI-78404;
Q9WVI9-1:Mapk8ip1; NbExp=3; IntAct=EBI-78814, EBI-288461;
Q61120:Shc3; NbExp=2; IntAct=EBI-78814, EBI-79107;
Q9JHI9:Slc40a1; NbExp=2; IntAct=EBI-78814, EBI-2931424;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:15677459};
Single-pass type I membrane protein {ECO:0000269|PubMed:15677459}.
Membrane, clathrin-coated pit {ECO:0000269|PubMed:15677459}.
Note=Cell surface protein that rapidly becomes internalized via
clathrin-coated pits. 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). Beta-APP42
associates with FPRL1 at the cell surface and the complex is then
rapidly internalized (By similarity). APP sorts to the basolateral
surface in epithelial cells (By similarity). 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. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Comment=Additional isoforms seem to exist.;
Name=APP770;
IsoId=P12023-1; Sequence=Displayed;
Name=APP695;
IsoId=P12023-2; Sequence=VSP_000012, VSP_000013;
Name=APP751;
IsoId=P12023-3; Sequence=VSP_000014;
Name=APP714;
IsoId=P12023-4; Sequence=Not described;
-!- TISSUE SPECIFICITY: Isoform APP770 is expressed in kidney. Isoform
APP751 is widely expressed. Isoform APP695 is expressed in brain,
kidney and liver. Isoform APP695, isoform APP714 and isoform
APP751 are expressed in several different brain regions including
hippocampus, substania nigra pars compacta and cerebellum. In the
cerebellum, these isoforms are abundantly expressed in Purkinje
cells. {ECO:0000269|PubMed:8510506}.
-!- DOMAIN: The basolateral sorting signal (BaSS) is required for
sorting of membrane proteins to the basolateral surface of
epithelial cells.
-!- 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 NPXY site is also involved in clathrin-mediated
endocytosis (By similarity). {ECO:0000250}.
-!- 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 40 (Abeta40) and amyloid-beta 42 (Abeta42),
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 beta-amyloid peptides (By similarity).
{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. The Thr-743 phosphorylated form causes a conformational
change which reduces binding of Fe65 family members (By
similarity). Phosphorylation on Tyr-757 is required for SHC
binding (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).
{ECO:0000250}.
-!- PTM: Beta-amyloid peptides are degraded by IDE. {ECO:0000250}.
-!- MISCELLANEOUS: Chelation of metal ions, notably copper, iron and
zinc, can induce histidine-bridging between beta-amyloid molecules
resulting in beta-amyloid-metal aggregates. Rat and mouse beta-
amyloid peptides have an arginine residue substituted for the
bridging histidine residue and are thus less capable of forming
amyloid aggregates. Extracellular zinc-binding increases binding
of heparin to APP and inhibits collagen-binding (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the APP family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M18373; AAA37139.1; -; mRNA.
EMBL; X59379; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; U84012; AAB41502.1; -; mRNA.
EMBL; D10603; BAA01456.1; -; Genomic_DNA.
EMBL; BC005490; AAH05490.1; -; mRNA.
EMBL; M24397; AAA39929.1; -; mRNA.
EMBL; X15210; CAA33280.1; -; mRNA.
EMBL; U82624; AAB40919.1; -; Genomic_DNA.
CCDS; CCDS28285.1; -. [P12023-2]
PIR; A27485; A27485.
PIR; A32282; A32282.
PIR; S04855; S04855.
RefSeq; NP_001185752.1; NM_001198823.1. [P12023-1]
UniGene; Mm.277585; -.
UniGene; Mm.489029; -.
UniGene; Mm.490986; -.
PDB; 2ROZ; NMR; -; A=739-770.
PDB; 2YSZ; NMR; -; A=739-770.
PDB; 2YT0; NMR; -; A=739-770.
PDB; 2YT1; NMR; -; A=739-770.
PDB; 4YN0; X-ray; 2.20 A; B=370-592.
PDBsum; 2ROZ; -.
PDBsum; 2YSZ; -.
PDBsum; 2YT0; -.
PDBsum; 2YT1; -.
PDBsum; 4YN0; -.
ProteinModelPortal; P12023; -.
SMR; P12023; -.
BioGrid; 198167; 8.
ELM; P12023; -.
IntAct; P12023; 79.
MINT; MINT-208509; -.
STRING; 10090.ENSMUSP00000005406; -.
MEROPS; I02.015; -.
iPTMnet; P12023; -.
PhosphoSitePlus; P12023; -.
PaxDb; P12023; -.
PeptideAtlas; P12023; -.
PRIDE; P12023; -.
Ensembl; ENSMUST00000005406; ENSMUSP00000005406; ENSMUSG00000022892. [P12023-2]
GeneID; 11820; -.
KEGG; mmu:11820; -.
UCSC; uc007ztn.2; mouse. [P12023-1]
CTD; 351; -.
MGI; MGI:88059; App.
eggNOG; KOG3540; Eukaryota.
eggNOG; ENOG410ZW2A; LUCA.
GeneTree; ENSGT00530000063252; -.
HOGENOM; HOG000232190; -.
HOVERGEN; HBG000051; -.
InParanoid; P12023; -.
KO; K04520; -.
OMA; REVCSEQ; -.
PhylomeDB; P12023; -.
TreeFam; TF317274; -.
Reactome; R-MMU-114608; Platelet degranulation.
Reactome; R-MMU-1810476; RIP-mediated NFkB activation via ZBP1.
Reactome; R-MMU-3000178; ECM proteoglycans.
Reactome; R-MMU-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-MMU-416476; G alpha (q) signalling events.
Reactome; R-MMU-418594; G alpha (i) signalling events.
Reactome; R-MMU-432720; Lysosome Vesicle Biogenesis.
Reactome; R-MMU-444473; Formyl peptide receptors bind formyl peptides and many other ligands.
Reactome; R-MMU-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-MMU-879415; Advanced glycosylation endproduct receptor signaling.
Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
Reactome; R-MMU-933542; TRAF6 mediated NF-kB activation.
ChiTaRS; App; mouse.
EvolutionaryTrace; P12023; -.
PRO; PR:P12023; -.
Proteomes; UP000000589; Chromosome 16.
Bgee; ENSMUSG00000022892; -.
CleanEx; MM_APP; -.
ExpressionAtlas; P12023; baseline and differential.
Genevisible; P12023; MM.
GO; GO:0045177; C:apical part of cell; IDA:MGI.
GO; GO:0097449; C:astrocyte projection; IEA:Ensembl.
GO; GO:0030424; C:axon; IDA:MGI.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0035253; C:ciliary rootlet; IDA:MGI.
GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
GO; GO:0043198; C:dendritic shaft; IEA:Ensembl.
GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
GO; GO:0005768; C:endosome; ISO:MGI.
GO; GO:0030134; C:ER to Golgi transport vesicle; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
GO; GO:1990812; C:growth cone filopodium; IEA:Ensembl.
GO; GO:1990761; C:growth cone lamellipodium; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IDA:MGI.
GO; GO:0044304; C:main axon; IEA:Ensembl.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0045121; C:membrane raft; ISO:MGI.
GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
GO; GO:0043005; C:neuron projection; IDA:MGI.
GO; GO:0005641; C:nuclear envelope lumen; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0043235; C:receptor complex; ISO:MGI.
GO; GO:0005791; C:rough endoplasmic reticulum; IEA:Ensembl.
GO; GO:0005790; C:smooth endoplasmic reticulum; IEA:GOC.
GO; GO:0051233; C:spindle midzone; IDA:MGI.
GO; GO:0043195; C:terminal bouton; IEA:Ensembl.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0070851; F:growth factor receptor binding; IEA:Ensembl.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IPI:ARUK-UCL.
GO; GO:0016504; F:peptidase activator activity; IEA:Ensembl.
GO; GO:0051425; F:PTB domain binding; ISO:MGI.
GO; GO:0005102; F:receptor binding; ISO:MGI.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; ISO:MGI.
GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
GO; GO:1990000; P:amyloid fibril formation; ISO:MGI.
GO; GO:0002265; P:astrocyte activation involved in immune response; ISO:MGI.
GO; GO:0008088; P:axo-dendritic transport; IMP:MGI.
GO; GO:0016199; P:axon midline choice point recognition; IMP:MGI.
GO; GO:0007409; P:axonogenesis; IMP:MGI.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0006878; P:cellular copper ion homeostasis; IMP:MGI.
GO; GO:0009987; P:cellular process; ISO:MGI.
GO; GO:1904646; P:cellular response to amyloid-beta; ISO:MGI.
GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEA:Ensembl.
GO; GO:0071874; P:cellular response to norepinephrine stimulus; IEA:Ensembl.
GO; GO:0008203; P:cholesterol metabolic process; IMP:MGI.
GO; GO:0048669; P:collateral sprouting in absence of injury; IGI:MGI.
GO; GO:0016358; P:dendrite development; IMP:MGI.
GO; GO:0006897; P:endocytosis; IMP:MGI.
GO; GO:0030198; P:extracellular matrix organization; IGI:MGI.
GO; GO:0030900; P:forebrain development; IMP:MGI.
GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IMP:MGI.
GO; GO:0007611; P:learning or memory; ISO:MGI.
GO; GO:0007626; P:locomotory behavior; IGI:MGI.
GO; GO:0060291; P:long-term synaptic potentiation; TAS:ARUK-UCL.
GO; GO:0007617; P:mating behavior; IGI:MGI.
GO; GO:0007613; P:memory; TAS:ARUK-UCL.
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; ISO:MGI.
GO; GO:0006378; P:mRNA polyadenylation; IDA:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; ISO:MGI.
GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
GO; GO:0045665; P:negative regulation of neuron differentiation; IDA:MGI.
GO; GO:0050885; P:neuromuscular process controlling balance; IGI:MGI.
GO; GO:0051402; P:neuron apoptotic process; IGI:MGI.
GO; GO:0031175; P:neuron projection development; IDA:MGI.
GO; GO:0016322; P:neuron remodeling; IMP:MGI.
GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:MGI.
GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; ISO:MGI.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:MGI.
GO; GO:0051247; P:positive regulation of protein metabolic process; ISO:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0051260; P:protein homooligomerization; ISO:MGI.
GO; GO:0006468; P:protein phosphorylation; IMP:MGI.
GO; GO:0007176; P:regulation of epidermal growth factor-activated receptor activity; IGI:MGI.
GO; GO:0010468; P:regulation of gene expression; IDA:MGI.
GO; GO:0040014; P:regulation of multicellular organism growth; IMP:MGI.
GO; GO:0043393; P:regulation of protein binding; IMP:MGI.
GO; GO:0050803; P:regulation of synapse structure or activity; IMP:MGI.
GO; GO:0048167; P:regulation of synaptic plasticity; ISO:MGI.
GO; GO:0006417; P:regulation of translation; IDA:MGI.
GO; GO:0010288; P:response to lead ion; IEA:Ensembl.
GO; GO:0006979; P:response to oxidative stress; IGI:MGI.
GO; GO:0051563; P:smooth endoplasmic reticulum calcium ion homeostasis; IGI:MGI.
GO; GO:0001967; P:suckling behavior; IGI:MGI.
GO; GO:0050808; P:synapse organization; ISO:MGI.
GO; GO:0051124; P:synaptic growth at neuromuscular junction; IGI:MGI.
GO; GO:0032640; P:tumor necrosis factor production; IEA:Ensembl.
GO; GO:0008542; P:visual learning; IMP:MGI.
CDD; cd00109; KU; 1.
Gene3D; 3.30.1490.140; -; 1.
Gene3D; 3.90.570.10; -; 1.
Gene3D; 4.10.230.10; -; 1.
Gene3D; 4.10.410.10; -; 1.
InterPro; IPR008155; Amyloid_glyco.
InterPro; IPR013803; Amyloid_glyco_Abeta.
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; IPR019745; Amyloid_glyco_intracell_CS.
InterPro; IPR028866; APP.
InterPro; IPR019543; APP_amyloid_C.
InterPro; IPR002223; Kunitz_BPTI.
InterPro; IPR020901; Prtase_inh_Kunz-CS.
PANTHER; PTHR23103:SF17; PTHR23103:SF17; 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.
PRINTS; PR00203; AMYLOIDA4.
PRINTS; PR00759; BASICPTASE.
PRINTS; PR00204; BETAAMYLOID.
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; PS00319; A4_EXTRA; 1.
PROSITE; PS00320; A4_INTRA; 1.
PROSITE; PS00280; BPTI_KUNITZ_1; 1.
PROSITE; PS50279; BPTI_KUNITZ_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Amyloid; Apoptosis; Cell adhesion;
Coated pit; Complete proteome; Copper; Disulfide bond; Endocytosis;
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}.
CHAIN 18 770 Amyloid beta A4 protein.
/FTId=PRO_0000000114.
CHAIN 18 687 Soluble APP-alpha. {ECO:0000255}.
/FTId=PRO_0000000115.
CHAIN 18 671 Soluble APP-beta. {ECO:0000255}.
/FTId=PRO_0000000116.
CHAIN 18 286 N-APP. {ECO:0000250}.
/FTId=PRO_0000381968.
CHAIN 672 770 C99. {ECO:0000250}.
/FTId=PRO_0000000117.
CHAIN 672 713 Beta-amyloid protein 42. {ECO:0000250}.
/FTId=PRO_0000000118.
CHAIN 672 711 Beta-amyloid protein 40. {ECO:0000250}.
/FTId=PRO_0000000119.
CHAIN 688 770 C83. {ECO:0000250}.
/FTId=PRO_0000000120.
PEPTIDE 688 713 P3(42). {ECO:0000250}.
/FTId=PRO_0000000121.
PEPTIDE 688 711 P3(40). {ECO:0000250}.
/FTId=PRO_0000000122.
CHAIN 691 770 C80.
/FTId=PRO_0000384576.
CHAIN 712 770 Gamma-secretase C-terminal fragment 59.
/FTId=PRO_0000000123.
CHAIN 714 770 Gamma-secretase C-terminal fragment 57.
/FTId=PRO_0000000124.
CHAIN 721 770 Gamma-secretase C-terminal fragment 50.
/FTId=PRO_0000000125.
CHAIN 740 770 C31. {ECO:0000250}.
/FTId=PRO_0000000126.
TOPO_DOM 18 699 Extracellular. {ECO:0000255}.
TRANSMEM 700 723 Helical. {ECO:0000255}.
TOPO_DOM 724 770 Cytoplasmic. {ECO:0000255}.
DOMAIN 291 341 BPTI/Kunitz inhibitor.
{ECO:0000255|PROSITE-ProRule:PRU00031}.
REGION 96 110 Heparin-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.
{ECO:0000250}.
REGION 756 770 Interaction with DAB2.
{ECO:0000269|PubMed:11247302}.
MOTIF 724 734 Basolateral sorting signal.
MOTIF 759 762 NPXY motif; contains endocytosis signal.
COMPBIAS 230 260 Asp/Glu-rich (acidic).
COMPBIAS 274 280 Poly-Thr.
METAL 147 147 Copper 1. {ECO:0000250}.
METAL 151 151 Copper 1. {ECO:0000250}.
METAL 168 168 Copper 1. {ECO:0000250}.
METAL 677 677 Copper or zinc 2. {ECO:0000250}.
METAL 685 685 Copper or zinc 2. {ECO:0000250}.
SITE 144 144 Required for Cu(2+) reduction.
{ECO:0000250}.
SITE 301 302 Reactive bond. {ECO:0000250}.
SITE 671 672 Cleavage; by beta-secretase.
{ECO:0000250}.
SITE 672 673 Cleavage; by caspase-6. {ECO:0000250}.
SITE 687 688 Cleavage; by alpha-secretase.
{ECO:0000250|UniProtKB:P08592}.
SITE 690 691 Cleavage; by theta-secretase.
{ECO:0000250|UniProtKB:P08592}.
SITE 704 704 Implicated in free radical propagation.
{ECO:0000250}.
SITE 711 712 Cleavage; by gamma-secretase; site 1.
{ECO:0000250|UniProtKB:P08592}.
SITE 713 714 Cleavage; by gamma-secretase; site 2.
{ECO:0000250}.
SITE 720 721 Cleavage; by gamma-secretase; site 3.
{ECO:0000250}.
SITE 739 740 Cleavage; by caspase-6, caspase-8 or
caspase-9. {ECO:0000250}.
MOD_RES 198 198 Phosphoserine; by CK2.
{ECO:0000250|UniProtKB:P05067}.
MOD_RES 206 206 Phosphoserine; by CK1.
{ECO:0000250|UniProtKB:P05067}.
MOD_RES 441 441 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 497 497 Phosphotyrosine.
{ECO:0000250|UniProtKB:P05067}.
MOD_RES 729 729 Phosphothreonine.
{ECO:0000250|UniProtKB:P08592}.
MOD_RES 730 730 Phosphoserine; by APP-kinase I.
{ECO:0000250|UniProtKB:P08592}.
MOD_RES 743 743 Phosphothreonine; by CDK5 and MAPK10.
{ECO:0000269|PubMed:11912189}.
MOD_RES 757 757 Phosphotyrosine; by ABL1.
{ECO:0000269|PubMed:11279131}.
CARBOHYD 542 542 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
CARBOHYD 571 571 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
DISULFID 38 62 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 73 117 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 98 105 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 133 187 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 144 174 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 158 186 {ECO:0000255|PROSITE-ProRule:PRU00031}.
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).
{ECO:0000250|UniProtKB:P08592}.
VAR_SEQ 289 289 E -> V (in isoform APP695).
{ECO:0000303|PubMed:11235921,
ECO:0000303|PubMed:1756177,
ECO:0000303|PubMed:3322280}.
/FTId=VSP_000012.
VAR_SEQ 290 364 Missing (in isoform APP695).
{ECO:0000303|PubMed:11235921,
ECO:0000303|PubMed:1756177,
ECO:0000303|PubMed:3322280}.
/FTId=VSP_000013.
VAR_SEQ 346 380 Missing (in isoform APP751).
{ECO:0000305}.
/FTId=VSP_000014.
MUTAGEN 728 728 Y->A: No effect on MAPK8IP1 binding.
{ECO:0000269|PubMed:11517249}.
MUTAGEN 732 733 HH->GL,GP: Almost complete loss of
binding to G(o) alpha subunit. No
inhibition of GTPase activity.
MUTAGEN 743 743 T->E: No effect on MAPK8IP1 binding.
{ECO:0000269|PubMed:11517249}.
MUTAGEN 756 756 G->F,H,N,S,W: Greatly impairs interaction
with DAB2. {ECO:0000269|PubMed:11247302}.
MUTAGEN 756 756 G->Y: Impairs interaction with DAB2.
{ECO:0000269|PubMed:11247302}.
MUTAGEN 757 757 Y->F: Greatly promotes interaction with
DAB2. {ECO:0000269|PubMed:11247302,
ECO:0000269|PubMed:11517249}.
MUTAGEN 757 757 Y->G,H,V: Greatly impairs interaction
with DAB2. {ECO:0000269|PubMed:11247302,
ECO:0000269|PubMed:11517249}.
MUTAGEN 757 757 Y->G: No MAPK8IP1 nor APBA1 nor APBB1 nor
DAB1 binding.
{ECO:0000269|PubMed:11247302,
ECO:0000269|PubMed:11517249}.
MUTAGEN 757 757 Y->I,W: Impairs interaction with DAB2.
{ECO:0000269|PubMed:11247302,
ECO:0000269|PubMed:11517249}.
MUTAGEN 759 759 N->A: No MAPK8IP1 nor APBA1 nor Dab1
binding. No effect on APBB1 binding.
{ECO:0000269|PubMed:11247302,
ECO:0000269|PubMed:11517249}.
MUTAGEN 759 759 N->G,L,M,P: Greatly impairs interaction
with DAB2. {ECO:0000269|PubMed:11247302,
ECO:0000269|PubMed:11517249}.
MUTAGEN 760 760 P->E,F,I,K,L,Q,R,V,W,Y: Greatly impairs
interaction with DAB2.
{ECO:0000269|PubMed:11247302}.
MUTAGEN 762 762 Y->A: No MAPK8IP1 nor APBA1 nor Dab1
binding. No effect on APBB1 binding.
{ECO:0000269|PubMed:11247302,
ECO:0000269|PubMed:11517249}.
MUTAGEN 762 762 Y->W: Greatly impairs interaction with
DAB2. {ECO:0000269|PubMed:11247302,
ECO:0000269|PubMed:11517249}.
CONFLICT 211 211 G -> V (in Ref. 1; AAA37139).
{ECO:0000305}.
CONFLICT 375 375 V -> A (in Ref. 4; AAB41502).
{ECO:0000305}.
HELIX 382 419 {ECO:0000244|PDB:4YN0}.
TURN 420 422 {ECO:0000244|PDB:4YN0}.
HELIX 425 481 {ECO:0000244|PDB:4YN0}.
HELIX 487 518 {ECO:0000244|PDB:4YN0}.
HELIX 520 550 {ECO:0000244|PDB:4YN0}.
HELIX 552 581 {ECO:0000244|PDB:4YN0}.
HELIX 744 753 {ECO:0000244|PDB:2ROZ}.
SEQUENCE 770 AA; 86722 MW; 988D89E089092A3E CRC64;
MLPSLALLLL AAWTVRALEV PTDGNAGLLA EPQIAMFCGK LNMHMNVQNG KWESDPSGTK
TCIGTKEGIL QYCQEVYPEL QITNVVEANQ PVTIQNWCKR GRKQCKTHTH IVIPYRCLVG
EFVSDALLVP DKCKFLHQER MDVCETHLHW HTVAKETCSE KSTNLHDYGM LLPCGIDKFR
GVEFVCCPLA EESDSVDSAD AEEDDSDVWW GGADTDYADG GEDKVVEVAE EEEVADVEEE
EADDDEDVED GDEVEEEAEE PYEEATERTT STATTTTTTT ESVEEVVREV CSEQAETGPC
RAMISRWYFD VTEGKCVPFF YGGCGGNRNN FDTEEYCMAV CGSVSTQSLL KTTSEPLPQD
PDKLPTTAAS TPDAVDKYLE TPGDENEHAH FQKAKERLEA KHRERMSQVM REWEEAERQA
KNLPKADKKA VIQHFQEKVE SLEQEAANER QQLVETHMAR VEAMLNDRRR LALENYITAL
QAVPPRPHHV FNMLKKYVRA EQKDRQHTLK HFEHVRMVDP KKAAQIRSQV MTHLRVIYER
MNQSLSLLYN VPAVAEEIQD EVDELLQKEQ NYSDDVLANM ISEPRISYGN DALMPSLTET
KTTVELLPVN GEFSLDDLQP WHPFGVDSVP ANTENEVEPV DARPAADRGL TTRPGSGLTN
IKTEEISEVK MDAEFGHDSG FEVRHQKLVF FAEDVGSNKG AIIGLMVGGV VIATVIVITL
VMLKKKQYTS IHHGVVEVDA AVTPEERHLS KMQQNGYENP TYKFFEQMQN


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