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

 A4_RAT                  Reviewed;         770 AA.
P08592; Q547B7;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-DEC-1992, sequence version 2.
25-OCT-2017, entry version 208.
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=Amyloid-beta precursor protein {ECO:0000305};
AltName: Full=Amyloidogenic glycoprotein;
Short=AG;
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=Beta-secretase C-terminal fragment;
Short=Beta-CTF;
Contains:
RecName: Full=Amyloid-beta protein 42;
Short=Abeta42;
AltName: Full=Beta-APP42;
Contains:
RecName: Full=Amyloid-beta protein 40;
Short=Abeta40;
AltName: Full=Beta-APP40;
Contains:
RecName: Full=C83;
AltName: Full=Alpha-secretase C-terminal fragment;
Short=Alpha-CTF;
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=Gamma-CTF(59);
Contains:
RecName: Full=Gamma-secretase C-terminal fragment 57;
AltName: Full=Gamma-CTF(57);
Contains:
RecName: Full=Gamma-secretase C-terminal fragment 50;
AltName: Full=Gamma-CTF(50);
Contains:
RecName: Full=C31;
Flags: Precursor;
Name=App;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM APP695).
TISSUE=Brain;
PubMed=2900758;
Shivers B.D., Hilbich C., Multhaup G., Salbaum J.M., Beyreuther K.,
Seeburg P.H.;
"Alzheimer's disease amyloidogenic glycoprotein: expression pattern in
rat brain suggests a role in cell contact.";
EMBO J. 7:1365-1370(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM APP770).
Feng J., Song S., Zheng J.;
"A new beta amyloid precursor protein cDNA found in Rat6 embryo
fibroblasts.";
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[3]
PROTEIN SEQUENCE OF 18-44.
PubMed=2968652; DOI=10.1126/science.2968652;
Schubert D., Schroeder R., LaCorbiere M., Saitoh T., Cole G.;
"Amyloid beta protein precursor is possibly a heparan sulfate
proteoglycan core protein.";
Science 241:223-226(1988).
[4]
PROTEIN SEQUENCE OF 18-32.
PubMed=1673681;
Potempska A., Styles J., Mehta P., Kim K.S., Miller D.L.;
"Purification and tissue level of the beta-amyloid peptide precursor
of rat brain.";
J. Biol. Chem. 266:8464-8469(1991).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 289-364.
TISSUE=Liver;
PubMed=2648331; DOI=10.1093/nar/17.5.2130;
Kang J., Mueller-Hill B.;
"The sequence of the two extra exons in rat preA4.";
Nucleic Acids Res. 17:2130-2130(1989).
[6]
PROTEIN SEQUENCE OF 720-730, AND MASS SPECTROMETRY.
PubMed=11483588; DOI=10.1074/jbc.C100357200;
Gu Y., Misonou H., Sato T., Dohmae N., Takio K., Ihara Y.;
"Distinct intramembrane cleavage of the beta-amyloid precursor protein
family resembling gamma-secretase-like cleavage of Notch.";
J. Biol. Chem. 276:35235-35238(2001).
[7]
ALTERNATIVE SPLICING.
PubMed=8624099; DOI=10.1111/j.1749-6632.1996.tb34433.x;
Sandbrink R., Masters C.L., Beyreuther K.;
"APP gene family. Alternative splicing generates functionally related
isoforms.";
Ann. N. Y. Acad. Sci. 777:281-287(1996).
[8]
TISSUE SPECIFICITY OF APPICAN.
PubMed=7744833; DOI=10.1074/jbc.270.20.11839;
Shioi J., Pangalos M.N., Ripellino J.A., Vassilacopoulou D.,
Mytilineou C., Margolis R.U., Robakis N.K.;
"The Alzheimer amyloid precursor proteoglycan (appican) is present in
brain and is produced by astrocytes but not by neurons in primary
neural cultures.";
J. Biol. Chem. 270:11839-11844(1995).
[9]
TISSUE SPECIFICITY OF ISOFORMS.
PubMed=8996834;
Sandbrink R., Monning U., Masters C.L., Beyreuther K.;
"Expression of the APP gene family in brain cells, brain development
and aging.";
Gerontology 43:119-131(1997).
[10]
INTERACTION WITH DDB1, AND MUTAGENESIS OF TYR-757; ASN-759 AND
TYR-762.
PubMed=9930726; DOI=10.1046/j.1471-4159.1999.0720549.x;
Watanabe T., Sukegawa J., Tomita S., Iijima K., Oguchi S., Suzuki T.,
Nairn A.C., Greengard P.;
"A 127-kDa protein (UV-DDB) binds to the cytoplasmic domain of the
Alzheimer's amyloid precursor protein.";
J. Neurochem. 72:549-556(1999).
[11]
INTERACTION WITH GNAO1, AND MUTAGENESIS OF 732-HIS-HIS-733.
PubMed=10024358;
Brouillet E., Trembleau A., Galanaud D., Volovitch M., Bouillot C.,
Valenza C., Prochiantz A., Allinquant B.;
"The amyloid precursor protein interacts with Go heterotrimeric
protein within a cell compartment specialized in signal
transduction.";
J. Neurosci. 19:1717-1727(1999).
[12]
COPPER-BINDING.
PubMed=7913895; DOI=10.1016/0014-5793(94)00658-X;
Hesse L., Beher D., Masters C.L., Multhaup G.;
"The beta A4 amyloid precursor protein binding to copper.";
FEBS Lett. 349:109-116(1994).
[13]
CHARACTERISTICS OF APPICAN, AND MUTAGENESIS OF SER-656.
PubMed=7737970; DOI=10.1074/jbc.270.18.10388;
Pangalos M.N., Efthimiopoulos S., Shioi J., Robakis N.K.;
"The chondroitin sulfate attachment site of appican is formed by
splicing out exon 15 of the amyloid precursor gene.";
J. Biol. Chem. 270:10388-10391(1995).
[14]
AMYLOID-BETA METAL-BINDING.
PubMed=10386999; DOI=10.1021/bi990438f;
Huang X., Atwood C.S., Hartshorn M.A., Multhaup G., Goldstein L.E.,
Scarpa R.C., Cuajungco M.P., Gray D.N., Lim J., Moir R.D., Tanzi R.E.,
Bush A.I.;
"The A beta peptide of Alzheimer's disease directly produces hydrogen
peroxide through metal ion reduction.";
Biochemistry 38:7609-7616(1999).
[15]
AMYLOID-BETA ZINC-BINDING.
PubMed=10413512; DOI=10.1021/bi990205o;
Liu S.T., Howlett G., Barrow C.J.;
"Histidine-13 is a crucial residue in the zinc ion-induced aggregation
of the A beta peptide of Alzheimer's disease.";
Biochemistry 38:9373-9378(1999).
[16]
IMPORTANCE OF GLY-704 IN FREE RADICAL PROPAGATION, AND MUTAGENESIS OF
GLY-704.
PubMed=11959460; DOI=10.1016/S0925-4439(01)00097-7;
Kanski J., Varadarajan S., Aksenova M., Butterfield D.A.;
"Role of glycine-33 and methionine-35 in Alzheimer's amyloid-beta
peptide 1-42-associated oxidative stress and neurotoxicity.";
Biochim. Biophys. Acta 1586:190-198(2002).
[17]
PHOSPHORYLATION AT THR-729; SER-730 AND THR-743.
PubMed=9085254;
Oishi M., Nairn A.C., Czernik A.J., Lim G.S., Isohara T., Gandy S.E.,
Greengard P., Suzuki T.;
"The cytoplasmic domain of Alzheimer's amyloid precursor protein is
phosphorylated at Thr654, Ser655, and Thr668 in adult rat brain and
cultured cells.";
Mol. Med. 3:111-123(1997).
[18]
PHOSPHORYLATION AT SER-730.
PubMed=10329382; DOI=10.1006/bbrc.1999.0637;
Isohara T., Horiuchi A., Watanabe T., Ando K., Czernik A.J., Uno I.,
Greengard P., Nairn A.C., Suzuki T.;
"Phosphorylation of the cytoplasmic domain of Alzheimer's beta-amyloid
precursor protein at Ser655 by a novel protein kinase.";
Biochem. Biophys. Res. Commun. 258:300-305(1999).
[19]
PHOSPHORYLATION, INDUCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
THR-743.
PubMed=10341243;
Ando K., Oishi M., Takeda S., Iijima K., Isohara T., Nairn A.C.,
Kirino Y., Greengard P., Suzuki T.;
"Role of phosphorylation of Alzheimer's amyloid precursor protein
during neuronal differentiation.";
J. Neurosci. 19:4421-4427(1999).
[20]
PHOSPHORYLATION AT THR-743.
PubMed=10936190; DOI=10.1046/j.1471-4159.2000.0751085.x;
Iijima K., Ando K., Takeda S., Satoh Y., Seki T., Itohara S.,
Greengard P., Kirino Y., Nairn A.C., Suzuki T.;
"Neuron-specific phosphorylation of Alzheimer's beta-amyloid precursor
protein by cyclin-dependent kinase 5.";
J. Neurochem. 75:1085-1091(2000).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-441, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[22]
UBIQUITINATION AT LYS-763, AND MUTAGENESIS OF LYS-763.
PubMed=22847417; DOI=10.1073/pnas.1206786109;
El Ayadi A., Stieren E.S., Barral J.M., Boehning D.;
"Ubiquilin-1 regulates amyloid precursor protein maturation and
degradation by stimulating K63-linked polyubiquitination of lysine
688.";
Proc. Natl. Acad. Sci. U.S.A. 109:13416-13421(2012).
[23]
PROTEOLYTIC PROCESSING, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=26479776; DOI=10.1021/acs.jproteome.5b00820;
Tsuchiya T., Osaki T., Minamino N., Sasaki K.;
"Peptidomics for studying limited proteolysis.";
J. Proteome Res. 14:4921-4931(2015).
[24]
STRUCTURE OF CARBOHYDRATE IN APPICAN.
PubMed=11479316; DOI=10.1074/jbc.M105818200;
Tsuchida K., Shioi J., Yamada S., Boghosian G., Wu A., Cai H.,
Sugahara K., Robakis N.K.;
"Appican, the proteoglycan form of the amyloid precursor protein,
contains chondroitin sulfate E in the repeating disaccharide region
and 4-O-sulfated galactose in the linkage region.";
J. Biol. Chem. 276:37155-37160(2001).
-!- 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 (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. Inhibits
G(o) alpha ATPase activity. 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. 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
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. Rat and mouse amyloid-beta peptides bind
only weakly transient metals and have little reducing activity due
to substitutions of transient metal chelating residues. Amyloid-
beta protein 42 may activate mononuclear phagocytes in the brain
and elicits inflammatory responses. Promotes both tau aggregation
and TPK II-mediated phosphorylation. Also binds GPC1 in lipid
rafts (By similarity). {ECO:0000250}.
-!- FUNCTION: Appicans elicit adhesion of neural cells to the
extracellular matrix and may regulate neurite outgrowth in the
brain.
-!- 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) (By similarity)
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;
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). {ECO:0000250,
ECO:0000250|UniProtKB:P05067}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10341243};
Single-pass type I membrane protein {ECO:0000269|PubMed:10341243}.
Membrane, clathrin-coated pit {ECO:0000269|PubMed:10341243}.
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). Associates with
GPC1 in perinuclear compartments (By similarity). Amyloid-beta
protein 42 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-742 phosphorylated form
is located mainly in growth cones, moderately in neurites and
sparingly in the cell body. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Name=APP770;
IsoId=P08592-1; Sequence=Displayed;
Name=APP695;
IsoId=P08592-2; Sequence=VSP_000015, VSP_000016;
Name=L-APP677;
IsoId=P08592-3; Sequence=Not described;
Note=L-isoforms are referred to as appicans.;
Name=L-APP696;
IsoId=P08592-4; Sequence=Not described;
Note=L-isoforms are referred to as appicans.;
Name=APP714;
IsoId=P08592-5; Sequence=Not described;
Name=L-APP733;
IsoId=P08592-6; Sequence=Not described;
Note=L-isoforms are referred to as appicans.;
Name=APP751;
IsoId=P08592-7; Sequence=Not described;
Name=L-APP752;
IsoId=P08592-8; Sequence=Not described;
Note=L-isoforms are referred to as appicans.;
-!- TISSUE SPECIFICITY: In the brain, non-L-APP isoforms are expressed
in neurons, isoform APP695 being the predominant form. In
astrocytes and microglial cells, almost 50% is L-isoform
(appican). {ECO:0000269|PubMed:7744833,
ECO:0000269|PubMed:8996834}.
-!- DEVELOPMENTAL STAGE: From 6 days to 7 months, levels of KPI-
containing isoforms increase in the brain cortex and hippocampus.
Levels of L-APP increase in all brain regions during the same
period, but levels are low compared to non-L-APP isoforms.
-!- INDUCTION: Phosphorylation of mature, glycosylated APP occurs 48-
72 hours after treatment of neuronal cells with nerve growth
factor which correlates with the timing of neurite outgrowth.
{ECO:0000269|PubMed:10341243}.
-!- 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.
-!- 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-glycosylated.
-!- PTM: O-glycosylated. O-linkage of chondroitin sulfate to the L-APP
isoforms produces the APP proteoglycan core proteins, the
appicans. The chondroitin sulfate chain of appicans contains 4-O-
sulfated galactose in the linkage region and chondroitin sulfate E
in the repeated disaccharide region.
-!- 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.
Phosphorylation on Tyr-757 is required for SHC binding.
Phosphorylated in the extracellular domain by casein kinases on
both soluble and membrane-bound APP. This phosphorylation is
inhibited by heparin. {ECO:0000269|PubMed:10329382,
ECO:0000269|PubMed:10341243, ECO:0000269|PubMed:10936190,
ECO:0000269|PubMed:9085254}.
-!- 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: Amyloid-beta peptides are degraded by IDE. {ECO:0000250}.
-!- MASS SPECTROMETRY: Mass=5911.3; Method=MALDI; Range=721-770;
Evidence={ECO:0000269|PubMed:11483588};
-!- MASS SPECTROMETRY: Mass=6024.4; Method=MALDI; Range=720-770;
Evidence={ECO:0000269|PubMed:11483588};
-!- MISCELLANEOUS: Chelation of metal ions, notably copper, iron and
zinc, can induce histidine-bridging between amyloid-beta molecules
resulting in amyloid-beta-metal aggregates. Rat and mouse amyloid-
beta 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}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X07648; CAA30488.1; -; mRNA.
EMBL; AF513015; AAM90259.1; -; mRNA.
EMBL; X14066; CAA32229.1; -; mRNA.
PIR; S00550; S00550.
PIR; S03607; S03607.
PIR; S23094; S23094.
RefSeq; NP_062161.1; NM_019288.2. [P08592-1]
RefSeq; XP_006248073.1; XM_006248011.3. [P08592-2]
UniGene; Rn.2104; -.
PDB; 1M7E; X-ray; 2.45 A; D/E/F=755-763.
PDB; 1NMJ; NMR; -; A=672-699.
PDB; 1OQN; X-ray; 2.30 A; C/D=755-763.
PDB; 2LI9; NMR; -; A/B=672-687.
PDBsum; 1M7E; -.
PDBsum; 1NMJ; -.
PDBsum; 1OQN; -.
PDBsum; 2LI9; -.
ProteinModelPortal; P08592; -.
SMR; P08592; -.
BioGrid; 248450; 3.
DIP; DIP-618N; -.
ELM; P08592; -.
IntAct; P08592; 9.
MINT; MINT-1521802; -.
STRING; 10116.ENSRNOP00000041613; -.
BindingDB; P08592; -.
ChEMBL; CHEMBL3638365; -.
MEROPS; I02.015; -.
TCDB; 1.C.50.1.1; the amyloid Beta-protein peptide (aBetapp) family.
iPTMnet; P08592; -.
PhosphoSitePlus; P08592; -.
PaxDb; P08592; -.
PRIDE; P08592; -.
Ensembl; ENSRNOT00000048854; ENSRNOP00000041613; ENSRNOG00000006997. [P08592-1]
GeneID; 54226; -.
KEGG; rno:54226; -.
UCSC; RGD:2139; rat. [P08592-1]
CTD; 351; -.
RGD; 2139; App.
eggNOG; KOG3540; Eukaryota.
eggNOG; ENOG410ZTKC; LUCA.
GeneTree; ENSGT00530000063252; -.
HOGENOM; HOG000232190; -.
HOVERGEN; HBG000051; -.
InParanoid; P08592; -.
KO; K04520; -.
OMA; REVCSEQ; -.
OrthoDB; EOG091G0UW4; -.
PhylomeDB; P08592; -.
TreeFam; TF317274; -.
Reactome; R-RNO-114608; Platelet degranulation.
Reactome; R-RNO-1810476; RIP-mediated NFkB activation via ZBP1.
Reactome; R-RNO-3000178; ECM proteoglycans.
Reactome; R-RNO-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-RNO-416476; G alpha (q) signalling events.
Reactome; R-RNO-418594; G alpha (i) signalling events.
Reactome; R-RNO-432720; Lysosome Vesicle Biogenesis.
Reactome; R-RNO-444473; Formyl peptide receptors bind formyl peptides and many other ligands.
Reactome; R-RNO-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-RNO-879415; Advanced glycosylation endproduct receptor signaling.
Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
Reactome; R-RNO-933542; TRAF6 mediated NF-kB activation.
EvolutionaryTrace; P08592; -.
PRO; PR:P08592; -.
Proteomes; UP000002494; Chromosome 11.
Bgee; ENSRNOG00000006997; -.
ExpressionAtlas; P08592; baseline and differential.
Genevisible; P08592; RN.
GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
GO; GO:0097449; C:astrocyte projection; IDA:RGD.
GO; GO:0030424; C:axon; IDA:AgBase.
GO; GO:0009986; C:cell surface; IDA:AgBase.
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; IDA:RGD.
GO; GO:0043198; C:dendritic shaft; IEA:Ensembl.
GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
GO; GO:0005768; C:endosome; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
GO; GO:0030426; C:growth cone; IDA:RGD.
GO; GO:1990812; C:growth cone filopodium; IDA:RGD.
GO; GO:1990761; C:growth cone lamellipodium; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
GO; GO:0044304; C:main axon; IDA:RGD.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0005641; C:nuclear envelope lumen; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0043235; C:receptor complex; IEA:Ensembl.
GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
GO; GO:0005790; C:smooth endoplasmic reticulum; IEA:GOC.
GO; GO:0051233; C:spindle midzone; IEA:Ensembl.
GO; GO:0043195; C:terminal bouton; IDA:ParkinsonsUK-UCL.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
GO; GO:0070851; F:growth factor receptor binding; IPI:RGD.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0016504; F:peptidase activator activity; IDA:RGD.
GO; GO:0051425; F:PTB domain binding; IEA:Ensembl.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
GO; GO:0000187; P:activation of MAPK activity; IDA:ARUK-UCL.
GO; GO:0008344; P:adult locomotory behavior; ISS:UniProtKB.
GO; GO:1990000; P:amyloid fibril formation; IEA:Ensembl.
GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
GO; GO:0019732; P:antifungal humoral response; IDA:UniProtKB.
GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
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:0071320; P:cellular response to cAMP; IEP:RGD.
GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEP:RGD.
GO; GO:0071874; P:cellular response to norepinephrine stimulus; IMP:RGD.
GO; GO:0008203; P:cholesterol metabolic process; IEA:Ensembl.
GO; GO:0048669; P:collateral sprouting in absence of injury; ISS:UniProtKB.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA: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:0045087; P:innate immune response; IDA:UniProtKB.
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: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:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:ARUK-UCL.
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:0045931; P:positive regulation of mitotic cell cycle; ISS:UniProtKB.
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:0051247; P:positive regulation of protein metabolic process; IDA:ARUK-UCL.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IEA:Ensembl.
GO; GO:2000406; P:positive regulation of T cell migration; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; 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:1905945; P:regulation of response to calcium ion; IGI:ARUK-UCL.
GO; GO:0050803; P:regulation of synapse structure or activity; ISS:UniProtKB.
GO; GO:0006417; P:regulation of translation; ISS:UniProtKB.
GO; GO:0010288; P:response to lead ion; IEP:RGD.
GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
GO; GO:0001878; P:response to yeast; IDA:UniProtKB.
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; 3.30.1490.140; -; 1.
Gene3D; 3.90.570.10; -; 1.
Gene3D; 4.10.230.10; -; 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; IPR020901; Prtase_inh_Kunz-CS.
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.
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; Direct protein sequencing;
Disulfide bond; Endocytosis; Glycoprotein; Heparin-binding; Iron;
Isopeptide bond; Membrane; Metal-binding; Notch signaling pathway;
Phosphoprotein; Protease inhibitor; Proteoglycan; 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.
/FTId=PRO_0000000159.
CHAIN 18 687 Soluble APP-alpha. {ECO:0000250}.
/FTId=PRO_0000000160.
CHAIN 18 671 Soluble APP-beta. {ECO:0000255}.
/FTId=PRO_0000000161.
CHAIN 18 286 N-APP. {ECO:0000250}.
/FTId=PRO_0000381971.
CHAIN 672 770 C99. {ECO:0000255}.
/FTId=PRO_0000000162.
CHAIN 672 713 Amyloid-beta protein 42. {ECO:0000250}.
/FTId=PRO_0000000163.
CHAIN 672 711 Amyloid-beta protein 40. {ECO:0000250}.
/FTId=PRO_0000000164.
CHAIN 688 770 C83. {ECO:0000250}.
/FTId=PRO_0000000165.
PEPTIDE 688 713 P3(42). {ECO:0000250}.
/FTId=PRO_0000000166.
PEPTIDE 688 711 P3(40). {ECO:0000250}.
/FTId=PRO_0000000167.
CHAIN 691 770 C80.
/FTId=PRO_0000384579.
CHAIN 712 770 Gamma-secretase C-terminal fragment 59.
/FTId=PRO_0000000168.
CHAIN 714 770 Gamma-secretase C-terminal fragment 57.
/FTId=PRO_0000000169.
CHAIN 721 770 Gamma-secretase C-terminal fragment 50.
/FTId=PRO_0000000170.
CHAIN 740 770 C31. {ECO:0000250}.
/FTId=PRO_0000000171.
TOPO_DOM 18 699 Extracellular. {ECO:0000255}.
TRANSMEM 700 723 Helical. {ECO:0000255}.
TOPO_DOM 724 770 Cytoplasmic. {ECO:0000250}.
DOMAIN 291 341 BPTI/Kunitz inhibitor.
{ECO:0000255|PROSITE-ProRule:PRU00031}.
REGION 96 110 Heparin-binding. {ECO:0000250}.
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.
{ECO:0000250}.
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.
SITE 687 688 Cleavage; by alpha-secretase.
{ECO:0000269|PubMed:26479776}.
SITE 690 691 Cleavage; by theta-secretase.
{ECO:0000269|PubMed:26479776}.
SITE 711 712 Cleavage; by gamma-secretase; site 1.
{ECO:0000269|PubMed:26479776}.
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:22673903}.
MOD_RES 497 497 Phosphotyrosine.
{ECO:0000250|UniProtKB:P05067}.
MOD_RES 729 729 Phosphothreonine.
{ECO:0000269|PubMed:9085254}.
MOD_RES 730 730 Phosphoserine; by APP-kinase I.
{ECO:0000269|PubMed:10329382,
ECO:0000269|PubMed:9085254}.
MOD_RES 743 743 Phosphothreonine; by CDK5 and MAPK10.
{ECO:0000269|PubMed:10936190,
ECO:0000269|PubMed:9085254}.
MOD_RES 757 757 Phosphotyrosine; by ABL1.
{ECO:0000250|UniProtKB:P12023}.
CARBOHYD 542 542 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 571 571 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 656 656 O-linked (Xyl...) (chondroitin sulfate)
serine; in L-APP isoforms.
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:0000269|PubMed:22847417}.
VAR_SEQ 289 289 E -> V (in isoform APP695).
{ECO:0000303|PubMed:2900758}.
/FTId=VSP_000015.
VAR_SEQ 290 364 Missing (in isoform APP695).
{ECO:0000303|PubMed:2900758}.
/FTId=VSP_000016.
MUTAGEN 656 656 S->A: No chondroitin sulfate linkage to
isoform L-APP733.
{ECO:0000269|PubMed:7737970}.
MUTAGEN 704 704 G->V: Little oxidized neuronal proteins.
Scarce amyloid-beta protein 42
aggregation. No neurotoxicity.
{ECO:0000269|PubMed:11959460}.
MUTAGEN 732 733 HH->GL,GP: Almost complete loss of
binding to GNAO1. No inhibition of GTPase
activity. {ECO:0000269|PubMed:10024358}.
MUTAGEN 743 743 T->A: No effect on neurite growth and
maturation.
{ECO:0000269|PubMed:10341243}.
MUTAGEN 743 743 T->E: Inhibits neurite growth and
maturation.
{ECO:0000269|PubMed:10341243}.
MUTAGEN 757 757 Y->G: No DBB1 binding.
{ECO:0000269|PubMed:9930726}.
MUTAGEN 759 759 N->A: Some DBB1 binding.
{ECO:0000269|PubMed:9930726}.
MUTAGEN 762 762 Y->A: Some DBB1 binding.
{ECO:0000269|PubMed:9930726}.
MUTAGEN 763 763 K->R: Loss of ubiquitination.
{ECO:0000269|PubMed:22847417}.
TURN 674 676 {ECO:0000244|PDB:2LI9}.
TURN 679 686 {ECO:0000244|PDB:1NMJ}.
HELIX 687 695 {ECO:0000244|PDB:1NMJ}.
SEQUENCE 770 AA; 86704 MW; C26C9D6BB2D929A7 CRC64;
MLPSLALLLL AAWTVRALEV PTDGNAGLLA EPQIAMFCGK LNMHMNVQNG KWESDPSGTK
TCIGTKEGIL QYCQEVYPEL QITNVVEANQ PVTIQNWCKR GRKQCKTHTH IVIPYRCLVG
EFVSDALLVP DKCKFLHQER MDVCETHLHW HTVAKETCSE KSTNLHDYGM LLPCGIDKFR
GVEFVCCPLA EESDSIDSAD AEEDDSDVWW GGADTDYADG GEDKVVEVAE EEEVADVEEE
EAEDDEDVED GDEVEEEAEE PYEEATERTT SIATTTTTTT ESVEEVVREV CSEQAETGPC
RAMISRWYFD VTEGKCAPFF YGGCGGNRNN FDTEEYCMAV CGSVSSQSLL KTTSEPLPQD
PVKLPTTAAS 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


Related products :

Catalog number Product name Quantity


 

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 Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
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

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
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 U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

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
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
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
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

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

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
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