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Major prion protein (PrP) (Major scrapie-associated fibril protein 1) (CD antigen CD230)

 PRIO_BOVIN              Reviewed;         264 AA.
P10279; A1YVV9; Q01880; Q0VD57; Q5UJJ5; Q5UJM6; Q5UK69; Q5UK71;
Q6UL03; Q6UL04; Q6UL05; Q6UL06; Q7YRN3; Q8MJI7;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-NOV-1991, sequence version 2.
30-AUG-2017, entry version 175.
RecName: Full=Major prion protein;
Short=PrP;
AltName: Full=Major scrapie-associated fibril protein 1;
AltName: CD_antigen=CD230;
Flags: Precursor;
Name=PRNP; Synonyms=PRP;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Holstein-Friesian;
PubMed=1671225; DOI=10.1099/0022-1317-72-1-201;
Goldmann W., Hunter N., Martin T., Dawson M., Hope J.;
"Different forms of the bovine PrP gene have five or six copies of a
short, G-C-rich element within the protein-coding exon.";
J. Gen. Virol. 72:201-204(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANTS 92-TRP--GLY 99
DEL AND ASN-154.
STRAIN=Holstein-Friesian; TISSUE=Brain;
PubMed=1362024; DOI=10.1007/BF01703083;
Yoshimoto J., Iinuma T., Ishiguro N., Horiuchi M., Imamura M.,
Shinagawa M.;
"Comparative sequence analysis and expression of bovine PrP gene in
mouse L-929 cells.";
Virus Genes 6:343-356(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8440932; DOI=10.1093/infdis/167.3.602;
Prusiner S.B., Fuzi M., Scott M., Serban D., Serban H., Taraboulos A.,
Gabriel J.M., Wells G.A., Wilesmith J.W., Bradley R.;
"Immunologic and molecular biologic studies of prion proteins in
bovine spongiform encephalopathy.";
J. Infect. Dis. 167:602-613(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Holstein-Friesian; TISSUE=Brain;
Horiuchi M., Ishiguro N., Nagasawa H., Toyoda Y., Shinagawa M.;
"Genomic organization of bovine PrP gene and complete nucleotide
sequence of bovine PrP cDNA.";
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Jersey;
PubMed=11531705; DOI=10.1046/j.1365-2052.2001.0769a.x;
Hills D., Comincini S., Schlaepfer J., Dolf G., Ferretti L.,
Williams J.L.;
"Complete genomic sequence of the bovine prion gene (PRNP) and
polymorphism in its promoter region.";
Anim. Genet. 32:231-232(2001).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT
GLY-TRP-GLY-GLN-PRO-HIS-GLY-GLY-98 INS.
Naharro G., Yugueros J., Temprano A.;
"Bovine PrP gene for prion protein.";
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Korean;
Yoo H.S., Kang S.G., Choi I.S., Kang S.K., Hwang W.S.;
"Nucleotide sequence of PrP cDNA in Korean cattle.";
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=14722726; DOI=10.1007/s00335-003-2283-y;
Heaton M.P., Leymaster K.A., Freking B.A., Hawk D.A., Smith T.P.,
Keele J.W., Snelling W.M., Fox J.M., Chitko-McKown C.G.,
Laegreid W.W.;
"Prion gene sequence variation within diverse groups of U.S. sheep,
beef cattle, and deer.";
Mamm. Genome 14:765-777(2003).
[9]
SEQUENCE REVISION TO 211, AND VARIANT LYS-211.
PubMed=18625065; DOI=10.1186/1746-6148-4-25;
Heaton M.P., Keele J.W., Harhay G.P., Richt J.A., Koohmaraie M.,
Wheeler T.L., Shackelford S.D., Casas E., King D.A., Sonstegard T.S.,
Van Tassell C.P., Neibergs H.L., Chase C.C. Jr., Kalbfleisch T.S.,
Smith T.P.L., Clawson M.L., Laegreid W.W.;
"Prevalence of the prion protein gene E211K variant in U.S. cattle.";
BMC Vet. Res. 4:25-25(2008).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-60; ARG-94;
ASN-154 AND ARG-234.
STRAIN=Holstein-Friesian, and Qinchuan; TISSUE=Blood;
Wu R., Xie Q.G., Liu X.T., Chen H.T., Cheng J.;
"Cloning and sequence analysis of bovine prion protein gene.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS 84-TRP--GLY 99 DEL;
92-TRP--GLY 99 DEL AND GLY-TRP-GLY-GLN-PRO-HIS-GLY-GLY-98 INS.
PubMed=15477588; DOI=10.1073/pnas.0406403101;
Seabury C.M., Honeycutt R.L., Rooney A.P., Halbert N.D., Derr J.N.;
"Prion protein gene (PRNP) variants and evidence for strong purifying
selection in functionally important regions of bovine exon 3.";
Proc. Natl. Acad. Sci. U.S.A. 101:15142-15147(2004).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Uboldi C., Bertoni A., Del Vecchio I., Comincini S., Hills D.,
Schlaepfer J., Dolf G., Williams J.L., Ferretti L.;
"Genomic characterization of the bovine PRN loci (PRNP, PRND and
PRNT).";
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=16460908; DOI=10.1016/j.ygeno.2005.12.012;
Choi S.-H., Kim I.-C., Kim D.-S., Kim D.-W., Chae S.-H., Choi H.-H.,
Choi I., Yeo J.-S., Song M.-N., Park H.-S.;
"Comparative genomic organization of the human and bovine PRNP
locus.";
Genomics 87:598-607(2006).
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Holstein, and Japanese black; TISSUE=Semen;
Abe T., Hasebe H., Kobayashi E.;
"Frequencies of bovine PrP gene polymorphisms in Japanese-black and
Holstein bulls in japan.";
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
[15]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Brain;
Barbieri I., Brocchi E., Borre A., Moretti M., Gelmetti D.,
Capucci L.;
"Detection of prion protein in various animal species by a new set of
monoclonal antibodies.";
Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
[16]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Hypothalamus;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
[17]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
Tanaka M., Inoue S., Ikeda T., Horiuchi M., Ishiguro N., Shinagawa M.;
"Characterization of bovine PrP promoter region.";
Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
[18]
PROTEIN SEQUENCE OF 25-36.
PubMed=2904126; DOI=10.1038/336390a0;
Hope J., Reekie L.J.D., Hunter N., Multhaup G., Beyreuther K.,
White H., Scott A.C., Stack M.J., Dawson M., Wells G.A.;
"Fibrils from brains of cows with new cattle disease contain scrapie-
associated protein.";
Nature 336:390-392(1988).
[19]
STRUCTURE BY NMR OF 1-30.
PubMed=15554701; DOI=10.1021/bi0485070;
Biverstahl H., Andersson A., Graslund A., Maler L.;
"NMR solution structure and membrane interaction of the N-terminal
sequence (1-30) of the bovine prion protein.";
Biochemistry 43:14940-14947(2004).
[20]
STRUCTURE BY NMR OF 132-241.
PubMed=10899999; DOI=10.1073/pnas.97.15.8334;
Lopez Garcia F., Zahn R., Riek R., Wuethrich K.;
"NMR structure of the bovine prion protein.";
Proc. Natl. Acad. Sci. U.S.A. 97:8334-8339(2000).
[21]
X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 107-115 IN COMPLEX WITH
ANTIBODY FRAGMENT.
PubMed=16962610; DOI=10.1016/j.jmb.2006.07.027;
Luginbuhl B., Kanyo Z., Jones R.M., Fletterick R.J., Prusiner S.B.,
Cohen F.E., Williamson R.A., Burton D.R., Pluckthun A.;
"Directed evolution of an anti-prion protein scFv fragment to an
affinity of 1 pM and its structural interpretation.";
J. Mol. Biol. 363:75-97(2006).
-!- FUNCTION: Its primary physiological function is unclear. May play
a role in neuronal development and synaptic plasticity. May be
required for neuronal myelin sheath maintenance. May promote
myelin homeostasis through acting as a agonist for ADGRG6
receptor. May play a role in iron uptake and iron homeostasis.
Soluble oligomers are toxic to cultured neuroblastoma cells and
induce apoptosis (in vitro) (By similarity). Association with GPC1
(via its heparan sulfate chains) targets PRNP to lipid rafts. Also
provides Cu(2+) or ZN(2+) for the ascorbate-mediated GPC1
deaminase degradation of its heparan sulfate side chains (By
similarity). {ECO:0000250|UniProtKB:P04156,
ECO:0000250|UniProtKB:P04925}.
-!- SUBUNIT: Monomer and homodimer. Has a tendency to aggregate into
amyloid fibrils containing a cross-beta spine, formed by a steric
zipper of superposed beta-strands. Soluble oligomers may represent
an intermediate stage on the path to fibril formation. Copper
binding may promote oligomerization. Interacts with GRB2, APP,
ERI3/PRNPIP and SYN1 (By similarity). Mislocalized cytosolically
exposed PrP interacts with MGRN1; this interaction alters MGRN1
subcellular location and causes lysosomal enlargement (By
similarity). Interacts with APP. Interacts with KIAA1191 (By
similarity). Interacts with ADGRG6 (By similarity).
{ECO:0000250|UniProtKB:P04156, ECO:0000250|UniProtKB:P04925}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-7430632, EBI-7430632;
P04156:PRNP (xeno); NbExp=5; IntAct=EBI-7430632, EBI-977302;
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P04156}; Lipid-anchor, GPI-anchor
{ECO:0000250|UniProtKB:P04156}. Golgi apparatus
{ECO:0000250|UniProtKB:P04925}. Note=Targeted to lipid rafts via
association with the heparan sulfate chains of GPC1. Colocates, in
the presence of Cu(2+), to vesicles in para- and perinuclear
regions, where both proteins undergo internalization. Heparin
displaces PRNP from lipid rafts and promotes endocytosis.
{ECO:0000250|UniProtKB:P04156}.
-!- DOMAIN: The normal, monomeric form has a mainly alpha-helical
structure. The disease-associated, protease-resistant form forms
amyloid fibrils containing a cross-beta spine, formed by a steric
zipper of superposed beta-strands. Disease mutations may favor
intermolecular contacts via short beta strands, and may thereby
trigger oligomerization. {ECO:0000250|UniProtKB:P04156}.
-!- DOMAIN: Contains an N-terminal region composed of octamer repeats.
At low copper concentrations, the sidechains of His residues from
three or four repeats contribute to the binding of a single copper
ion. Alternatively, a copper ion can be bound by interaction with
the sidechain and backbone amide nitrogen of a single His residue.
The observed copper binding stoichiometry suggests that two repeat
regions cooperate to stabilize the binding of a single copper ion.
At higher copper concentrations, each octamer can bind one copper
ion by interactions with the His sidechain and Gly backbone atoms.
A mixture of binding types may occur, especially in the case of
octamer repeat expansion. Copper binding may stabilize the
conformation of this region and may promote oligomerization.
{ECO:0000250|UniProtKB:P04156}.
-!- DISEASE: Note=Variations in PRNP are responsible of transmissible
bovine spongiform encephalopathies (BSE), a class of
neurodegenerative diseases that affect various mammals. These
diseases are caused by abnormally folded prion proteins. BSE can
be subdivided into at least three groups: classical, H-type and L-
type, with the latter 2 collectively referred to as atypical BSE.
Susceptibility or resistance to a BSE disease can be influenced by
at least 3 factors related to the host prion protein: protein
expression levels, number of octapeptide repeats, and specific
polymorphisms. In cattle, as in humans, BSEs can occur as
infectious, spontaneous and genetic diseases. {ECO:0000305}.
-!- MISCELLANEOUS: This protein is produced by a bicistronic gene
which also produces the major prion protein/PRNP from an
overlapping reading frame.
-!- MISCELLANEOUS: The alternative prion protein/AltPrP (AC F7VJQ2)
and PRNP have no apparent direct functional relation since a
mutation that removes the start codon of the AltPrP has no
apparent effect on the biology of PRNP (By similarity). In mouse
and hamster, the alternative initiation AUG codon is absent and is
replaced by a GUG codon. {ECO:0000250}.
-!- SIMILARITY: Belongs to the prion family. {ECO:0000305}.
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EMBL; X55882; CAA39368.1; -; Genomic_DNA.
EMBL; D10612; BAA01467.1; -; mRNA.
EMBL; D10613; BAA01468.1; -; Genomic_DNA.
EMBL; D10614; BAA01469.1; -; Genomic_DNA.
EMBL; S55629; AAB25514.1; -; mRNA.
EMBL; AB001468; BAA19253.1; -; mRNA.
EMBL; AJ298878; CAC37367.1; -; Genomic_DNA.
EMBL; AF455119; AAM73856.1; -; Genomic_DNA.
EMBL; AF517842; AAM66709.1; -; mRNA.
EMBL; AY335912; AAP84097.2; -; Genomic_DNA.
EMBL; AY367638; AAQ64645.1; -; Genomic_DNA.
EMBL; AY367639; AAQ64646.1; -; Genomic_DNA.
EMBL; AY367640; AAQ64647.1; -; Genomic_DNA.
EMBL; AY367641; AAQ64648.1; -; Genomic_DNA.
EMBL; AY367642; AAQ64649.1; -; Genomic_DNA.
EMBL; AY367643; AAQ64650.1; -; Genomic_DNA.
EMBL; AY720445; AAV30252.1; -; Genomic_DNA.
EMBL; AY720446; AAV30253.1; -; Genomic_DNA.
EMBL; AY720448; AAV30255.1; -; Genomic_DNA.
EMBL; AY720449; AAV30256.1; -; Genomic_DNA.
EMBL; AY720450; AAV30257.1; -; Genomic_DNA.
EMBL; AY720451; AAV30258.1; -; Genomic_DNA.
EMBL; AY720452; AAV30259.1; -; Genomic_DNA.
EMBL; AY720453; AAV30260.1; -; Genomic_DNA.
EMBL; AY720454; AAV30261.1; -; Genomic_DNA.
EMBL; AY720455; AAV30262.1; -; Genomic_DNA.
EMBL; AY720458; AAV30265.1; -; Genomic_DNA.
EMBL; AY720459; AAV30266.1; -; Genomic_DNA.
EMBL; AY720460; AAV30267.1; -; Genomic_DNA.
EMBL; AY720461; AAV30268.1; -; Genomic_DNA.
EMBL; AY720462; AAV30269.1; -; Genomic_DNA.
EMBL; AY720463; AAV30270.1; -; Genomic_DNA.
EMBL; AY720464; AAV30271.1; -; Genomic_DNA.
EMBL; AY720465; AAV30272.1; -; Genomic_DNA.
EMBL; AY720466; AAV30273.1; -; Genomic_DNA.
EMBL; AY720467; AAV30274.1; -; Genomic_DNA.
EMBL; AY720468; AAV30275.1; -; Genomic_DNA.
EMBL; AY720469; AAV30276.1; -; Genomic_DNA.
EMBL; AY720470; AAV30277.1; -; Genomic_DNA.
EMBL; AY720471; AAV30278.1; -; Genomic_DNA.
EMBL; AY720472; AAV30279.1; -; Genomic_DNA.
EMBL; AY720473; AAV30280.1; -; Genomic_DNA.
EMBL; AY720474; AAV30281.1; -; Genomic_DNA.
EMBL; AY720475; AAV30282.1; -; Genomic_DNA.
EMBL; AY720476; AAV30283.1; -; Genomic_DNA.
EMBL; AY720477; AAV30284.1; -; Genomic_DNA.
EMBL; AY720478; AAV30285.1; -; Genomic_DNA.
EMBL; AY720479; AAV30286.1; -; Genomic_DNA.
EMBL; AY720480; AAV30287.1; -; Genomic_DNA.
EMBL; AY720481; AAV30288.1; -; Genomic_DNA.
EMBL; AY720482; AAV30289.1; -; Genomic_DNA.
EMBL; AY720483; AAV30290.1; -; Genomic_DNA.
EMBL; AY720484; AAV30291.1; -; Genomic_DNA.
EMBL; AY720485; AAV30292.1; -; Genomic_DNA.
EMBL; AY720486; AAV30293.1; -; Genomic_DNA.
EMBL; AY720488; AAV30295.1; -; Genomic_DNA.
EMBL; AY720489; AAV30296.1; -; Genomic_DNA.
EMBL; AY720492; AAV30299.1; -; Genomic_DNA.
EMBL; AY720493; AAV30300.1; -; Genomic_DNA.
EMBL; AY720494; AAV30301.1; -; Genomic_DNA.
EMBL; AY720495; AAV30302.1; -; Genomic_DNA.
EMBL; AY720496; AAV30303.1; -; Genomic_DNA.
EMBL; AY720497; AAV30304.1; -; Genomic_DNA.
EMBL; AY720498; AAV30305.1; -; Genomic_DNA.
EMBL; AY720503; AAV30310.1; -; Genomic_DNA.
EMBL; AY720504; AAV30311.1; -; Genomic_DNA.
EMBL; AY720505; AAV30312.1; -; Genomic_DNA.
EMBL; AY720506; AAV30313.1; -; Genomic_DNA.
EMBL; AY720507; AAV30314.1; -; Genomic_DNA.
EMBL; AY720508; AAV30315.1; -; Genomic_DNA.
EMBL; AY720509; AAV30316.1; -; Genomic_DNA.
EMBL; AY720510; AAV30317.1; -; Genomic_DNA.
EMBL; AY720511; AAV30318.1; -; Genomic_DNA.
EMBL; AY720512; AAV30319.1; -; Genomic_DNA.
EMBL; AY720513; AAV30320.1; -; Genomic_DNA.
EMBL; AY720514; AAV30321.1; -; Genomic_DNA.
EMBL; AY720525; AAV30332.1; -; Genomic_DNA.
EMBL; AY720530; AAV30337.1; -; Genomic_DNA.
EMBL; AY720531; AAV30338.1; -; Genomic_DNA.
EMBL; AY720532; AAV30339.1; -; Genomic_DNA.
EMBL; AY720533; AAV30340.1; -; Genomic_DNA.
EMBL; AY720534; AAV30341.1; -; Genomic_DNA.
EMBL; AY720535; AAV30342.1; -; Genomic_DNA.
EMBL; AY720540; AAV30347.1; -; Genomic_DNA.
EMBL; AY720541; AAV30348.1; -; Genomic_DNA.
EMBL; AY720544; AAV30351.1; -; Genomic_DNA.
EMBL; AY720545; AAV30352.1; -; Genomic_DNA.
EMBL; AY720546; AAV30353.1; -; Genomic_DNA.
EMBL; AY720547; AAV30354.1; -; Genomic_DNA.
EMBL; AY720548; AAV30355.1; -; Genomic_DNA.
EMBL; AY720549; AAV30356.1; -; Genomic_DNA.
EMBL; AY720550; AAV30357.1; -; Genomic_DNA.
EMBL; AY720551; AAV30358.1; -; Genomic_DNA.
EMBL; AY720552; AAV30359.1; -; Genomic_DNA.
EMBL; AY720553; AAV30360.1; -; Genomic_DNA.
EMBL; AY720554; AAV30361.1; -; Genomic_DNA.
EMBL; AY720555; AAV30362.1; -; Genomic_DNA.
EMBL; AY720556; AAV30363.1; -; Genomic_DNA.
EMBL; AY720557; AAV30364.1; -; Genomic_DNA.
EMBL; AY720558; AAV30365.1; -; Genomic_DNA.
EMBL; AY720559; AAV30366.1; -; Genomic_DNA.
EMBL; AY720560; AAV30367.1; -; Genomic_DNA.
EMBL; AY720561; AAV30368.1; -; Genomic_DNA.
EMBL; AY720562; AAV30369.1; -; Genomic_DNA.
EMBL; AY720563; AAV30370.1; -; Genomic_DNA.
EMBL; AY720564; AAV30371.1; -; Genomic_DNA.
EMBL; AY720565; AAV30372.1; -; Genomic_DNA.
EMBL; AY720566; AAV30373.1; -; Genomic_DNA.
EMBL; AY720567; AAV30374.1; -; Genomic_DNA.
EMBL; AY720568; AAV30375.1; -; Genomic_DNA.
EMBL; AY720569; AAV30376.1; -; Genomic_DNA.
EMBL; AY720570; AAV30377.1; -; Genomic_DNA.
EMBL; AY720571; AAV30378.1; -; Genomic_DNA.
EMBL; AY720572; AAV30379.1; -; Genomic_DNA.
EMBL; AY720573; AAV30380.1; -; Genomic_DNA.
EMBL; AY720574; AAV30381.1; -; Genomic_DNA.
EMBL; AY720581; AAV30388.1; -; Genomic_DNA.
EMBL; AY720582; AAV30389.1; -; Genomic_DNA.
EMBL; AY720583; AAV30390.1; -; Genomic_DNA.
EMBL; AY720584; AAV30391.1; -; Genomic_DNA.
EMBL; AY720585; AAV30392.1; -; Genomic_DNA.
EMBL; AY720588; AAV30395.1; -; Genomic_DNA.
EMBL; AY720591; AAV30398.1; -; Genomic_DNA.
EMBL; AY720594; AAV30401.1; -; Genomic_DNA.
EMBL; AY720595; AAV30402.1; -; Genomic_DNA.
EMBL; AY720596; AAV30403.1; -; Genomic_DNA.
EMBL; AY720597; AAV30404.1; -; Genomic_DNA.
EMBL; AY720600; AAV30407.1; -; Genomic_DNA.
EMBL; AY720601; AAV30408.1; -; Genomic_DNA.
EMBL; AY720602; AAV30409.1; -; Genomic_DNA.
EMBL; AY720603; AAV30410.1; -; Genomic_DNA.
EMBL; AY720604; AAV30411.1; -; Genomic_DNA.
EMBL; AY720605; AAV30412.1; -; Genomic_DNA.
EMBL; AY720606; AAV30413.1; -; Genomic_DNA.
EMBL; AY720607; AAV30414.1; -; Genomic_DNA.
EMBL; AY720608; AAV30415.1; -; Genomic_DNA.
EMBL; AY720609; AAV30416.1; -; Genomic_DNA.
EMBL; AY720610; AAV30417.1; -; Genomic_DNA.
EMBL; AY720611; AAV30418.1; -; Genomic_DNA.
EMBL; AY720612; AAV30419.1; -; Genomic_DNA.
EMBL; AY720613; AAV30420.1; -; Genomic_DNA.
EMBL; AY720622; AAV30429.1; -; Genomic_DNA.
EMBL; AY720623; AAV30430.1; -; Genomic_DNA.
EMBL; AY720624; AAV30431.1; -; Genomic_DNA.
EMBL; AY720625; AAV30432.1; -; Genomic_DNA.
EMBL; AY720626; AAV30433.1; -; Genomic_DNA.
EMBL; AY720627; AAV30434.1; -; Genomic_DNA.
EMBL; AY720628; AAV30435.1; -; Genomic_DNA.
EMBL; AY720629; AAV30436.1; -; Genomic_DNA.
EMBL; AY720630; AAV30437.1; -; Genomic_DNA.
EMBL; AY720631; AAV30438.1; -; Genomic_DNA.
EMBL; AY720632; AAV30439.1; -; Genomic_DNA.
EMBL; AY720633; AAV30440.1; -; Genomic_DNA.
EMBL; AY720634; AAV30441.1; -; Genomic_DNA.
EMBL; AY720635; AAV30442.1; -; Genomic_DNA.
EMBL; AY720636; AAV30443.1; -; Genomic_DNA.
EMBL; AY720637; AAV30444.1; -; Genomic_DNA.
EMBL; AY720640; AAV30447.1; -; Genomic_DNA.
EMBL; AY720641; AAV30448.1; -; Genomic_DNA.
EMBL; AY720642; AAV30449.1; -; Genomic_DNA.
EMBL; AY720643; AAV30450.1; -; Genomic_DNA.
EMBL; AY720644; AAV30451.1; -; Genomic_DNA.
EMBL; AY720645; AAV30452.1; -; Genomic_DNA.
EMBL; AY720648; AAV30455.1; -; Genomic_DNA.
EMBL; AY720649; AAV30456.1; -; Genomic_DNA.
EMBL; AY720650; AAV30457.1; -; Genomic_DNA.
EMBL; AY720651; AAV30458.1; -; Genomic_DNA.
EMBL; AY720652; AAV30459.1; -; Genomic_DNA.
EMBL; AY720653; AAV30460.1; -; Genomic_DNA.
EMBL; AY720654; AAV30461.1; -; Genomic_DNA.
EMBL; AY720655; AAV30462.1; -; Genomic_DNA.
EMBL; AY720656; AAV30463.1; -; Genomic_DNA.
EMBL; AY720657; AAV30464.1; -; Genomic_DNA.
EMBL; AY720662; AAV30469.1; -; Genomic_DNA.
EMBL; AY720663; AAV30470.1; -; Genomic_DNA.
EMBL; AY720664; AAV30471.1; -; Genomic_DNA.
EMBL; AY720667; AAV30474.1; -; Genomic_DNA.
EMBL; AY720668; AAV30475.1; -; Genomic_DNA.
EMBL; AY720669; AAV30476.1; -; Genomic_DNA.
EMBL; AY720670; AAV30477.1; -; Genomic_DNA.
EMBL; AY720671; AAV30478.1; -; Genomic_DNA.
EMBL; AY720672; AAV30479.1; -; Genomic_DNA.
EMBL; AY720673; AAV30480.1; -; Genomic_DNA.
EMBL; AY720674; AAV30481.1; -; Genomic_DNA.
EMBL; AY720675; AAV30482.1; -; Genomic_DNA.
EMBL; AY720676; AAV30483.1; -; Genomic_DNA.
EMBL; AY720677; AAV30484.1; -; Genomic_DNA.
EMBL; AY720678; AAV30485.1; -; Genomic_DNA.
EMBL; DQ205538; ABB51165.1; -; Genomic_DNA.
EMBL; AY944236; AAY21624.1; -; Genomic_DNA.
EMBL; AB248079; BAE78586.1; -; Genomic_DNA.
EMBL; AB247937; BAE78583.1; -; Genomic_DNA.
EMBL; EF139165; ABL75501.1; -; Genomic_DNA.
EMBL; BC119821; AAI19822.1; -; mRNA.
EMBL; D26151; BAA05138.1; -; Genomic_DNA.
PIR; A54330; A54330.
PIR; JU0268; JU0268.
RefSeq; NP_001258555.1; NM_001271626.2.
RefSeq; NP_851358.2; NM_181015.3.
UniGene; Bt.4737; -.
PDB; 1DWY; NMR; -; A=132-241.
PDB; 1DWZ; NMR; -; A=132-241.
PDB; 1DX0; NMR; -; A=25-241.
PDB; 1DX1; NMR; -; A=25-241.
PDB; 1SKH; NMR; -; A=6-30.
PDB; 2HH0; X-ray; 2.85 A; P=107-115.
PDB; 2RSK; NMR; -; C/D=108-119.
PDB; 2RU7; NMR; -; C/D=108-119.
PDB; 4YX2; X-ray; 2.19 A; A=103-242.
PDBsum; 1DWY; -.
PDBsum; 1DWZ; -.
PDBsum; 1DX0; -.
PDBsum; 1DX1; -.
PDBsum; 1SKH; -.
PDBsum; 2HH0; -.
PDBsum; 2RSK; -.
PDBsum; 2RU7; -.
PDBsum; 4YX2; -.
DisProt; DP00783; -.
ProteinModelPortal; P10279; -.
SMR; P10279; -.
BioGrid; 158758; 3.
IntAct; P10279; 1.
MINT; MINT-1486044; -.
STRING; 9913.ENSBTAP00000043233; -.
PaxDb; P10279; -.
PRIDE; P10279; -.
Ensembl; ENSBTAT00000040292; ENSBTAP00000043233; ENSBTAG00000027937.
GeneID; 281427; -.
CTD; 5621; -.
eggNOG; ENOG410IJMM; Eukaryota.
eggNOG; ENOG410YXUU; LUCA.
GeneTree; ENSGT00510000049083; -.
HOVERGEN; HBG008260; -.
InParanoid; P10279; -.
OMA; GYPHNPG; -.
OrthoDB; EOG091G0HMV; -.
TreeFam; TF105188; -.
EvolutionaryTrace; P10279; -.
Proteomes; UP000009136; Chromosome 13.
Bgee; ENSBTAG00000027937; -.
ExpressionAtlas; P10279; baseline and differential.
GO; GO:0106003; C:amyloid-beta complex; IEA:Ensembl.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0016234; C:inclusion body; IEA:Ensembl.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0031965; C:nuclear membrane; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl.
GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
GO; GO:1903135; F:cupric ion binding; IEA:Ensembl.
GO; GO:1903136; F:cuprous ion binding; IEA:Ensembl.
GO; GO:0005539; F:glycosaminoglycan binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
GO; GO:0002020; F:protease binding; IEA:Ensembl.
GO; GO:0004872; F:receptor activity; IEA:Ensembl.
GO; GO:0004871; F:signal transducer activity; IEA:Ensembl.
GO; GO:0031802; F:type 5 metabotropic glutamate receptor binding; IEA:Ensembl.
GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; IEA:Ensembl.
GO; GO:1904646; P:cellular response to amyloid-beta; IEA:Ensembl.
GO; GO:0071280; P:cellular response to copper ion; IEA:Ensembl.
GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
GO; GO:0007611; P:learning or memory; IEA:Ensembl.
GO; GO:0090647; P:modulation of age-related behavioral decline; IEA:Ensembl.
GO; GO:0046007; P:negative regulation of activated T cell proliferation; IEA:Ensembl.
GO; GO:1902430; P:negative regulation of amyloid-beta formation; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; IEA:Ensembl.
GO; GO:0043086; P:negative regulation of catalytic activity; IEA:Ensembl.
GO; GO:1902951; P:negative regulation of dendritic spine maintenance; IEA:Ensembl.
GO; GO:0032689; P:negative regulation of interferon-gamma production; IEA:Ensembl.
GO; GO:0032700; P:negative regulation of interleukin-17 production; IEA:Ensembl.
GO; GO:0032703; P:negative regulation of interleukin-2 production; IEA:Ensembl.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IEA:Ensembl.
GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; IEA:Ensembl.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0090314; P:positive regulation of protein targeting to membrane; IEA:Ensembl.
GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IEA:Ensembl.
GO; GO:0031648; P:protein destabilization; IEA:Ensembl.
GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
GO; GO:1905664; P:regulation of calcium ion import across plasma membrane; IEA:Ensembl.
GO; GO:1902938; P:regulation of intracellular calcium activated chloride channel activity; IEA:Ensembl.
GO; GO:1901379; P:regulation of potassium ion transmembrane transport; IEA:Ensembl.
GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
Gene3D; 1.10.790.10; -; 1.
InterPro; IPR000817; Prion.
InterPro; IPR022416; Prion/Doppel_prot_b-ribbon_dom.
InterPro; IPR025860; Prion_N_dom.
PANTHER; PTHR10502:SF163; PTHR10502:SF163; 1.
Pfam; PF00377; Prion; 1.
Pfam; PF11587; Prion_bPrPp; 1.
PRINTS; PR00341; PRION.
SMART; SM00157; PRP; 1.
SUPFAM; SSF54098; SSF54098; 1.
PROSITE; PS00291; PRION_1; 1.
PROSITE; PS00706; PRION_2; 1.
1: Evidence at protein level;
3D-structure; Amyloid; Cell membrane; Complete proteome; Copper;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Golgi apparatus; GPI-anchor; Lipoprotein; Membrane; Metal-binding;
Polymorphism; Prion; Reference proteome; Repeat; Signal; Zinc.
SIGNAL 1 24 {ECO:0000269|PubMed:2904126}.
CHAIN 25 241 Major prion protein.
/FTId=PRO_0000025627.
PROPEP 242 264 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000025628.
REPEAT 54 62 1.
REPEAT 63 70 2.
REPEAT 71 78 3.
REPEAT 79 86 4.
REPEAT 87 94 5.
REPEAT 95 103 6.
REGION 25 241 Interaction with GRB2, ERI3 and SYN1.
{ECO:0000250|UniProtKB:P04925}.
REGION 25 41 Interaction with ADGRG6.
{ECO:0000250|UniProtKB:P04925}.
REGION 54 103 6 X 8 AA tandem repeats of P-H-G-G-G-W-G-
Q.
METAL 72 72 Copper or zinc 1.
{ECO:0000250|UniProtKB:P04156}.
METAL 73 73 Copper or zinc 1; via amide nitrogen.
{ECO:0000250|UniProtKB:P04156}.
METAL 74 74 Copper or zinc 1; via amide nitrogen and
carbonyl oxygen.
{ECO:0000250|UniProtKB:P04156}.
METAL 80 80 Copper or zinc 2.
{ECO:0000250|UniProtKB:P04156}.
METAL 81 81 Copper or zinc 2; via amide nitrogen.
{ECO:0000250|UniProtKB:P04156}.
METAL 82 82 Copper or zinc 2; via amide nitrogen and
carbonyl oxygen.
{ECO:0000250|UniProtKB:P04156}.
METAL 88 88 Copper or zinc 3.
{ECO:0000250|UniProtKB:P04156}.
METAL 89 89 Copper or zinc 3; via amide nitrogen.
{ECO:0000250|UniProtKB:P04156}.
METAL 90 90 Copper or zinc 3; via amide nitrogen and
carbonyl oxygen.
{ECO:0000250|UniProtKB:P04156}.
METAL 96 96 Copper or zinc 4.
{ECO:0000250|UniProtKB:P04156}.
METAL 98 98 Copper or zinc 4; via amide nitrogen.
{ECO:0000250|UniProtKB:P04156}.
METAL 99 99 Copper or zinc 4; via amide nitrogen and
carbonyl oxygen.
{ECO:0000250|UniProtKB:P04156}.
LIPID 241 241 GPI-anchor amidated alanine.
{ECO:0000255}.
CARBOHYD 192 192 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
CARBOHYD 208 208 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
DISULFID 190 225
VARIANT 60 60 W -> R. {ECO:0000269|Ref.10}.
VARIANT 71 78 Missing (in allele 2).
VARIANT 84 99 Missing. {ECO:0000269|PubMed:15477588}.
VARIANT 92 99 Missing. {ECO:0000269|PubMed:1362024,
ECO:0000269|PubMed:15477588}.
VARIANT 94 94 Q -> R. {ECO:0000269|Ref.10}.
VARIANT 98 98 G -> GGWGQPHGG. {ECO:0000269|Ref.6}.
VARIANT 154 154 S -> N. {ECO:0000269|PubMed:1362024,
ECO:0000269|Ref.10}.
VARIANT 211 211 E -> K. {ECO:0000269|PubMed:18625065}.
VARIANT 234 234 Q -> R. {ECO:0000269|Ref.10}.
CONFLICT 106 108 THG -> SHS (in Ref. 2; BAA01469).
{ECO:0000305}.
CONFLICT 218 218 E -> K (in Ref. 2; BAA01467 and 4;
BAA19253). {ECO:0000305}.
TURN 6 8 {ECO:0000244|PDB:1SKH}.
HELIX 9 21 {ECO:0000244|PDB:1SKH}.
STRAND 24 26 {ECO:0000244|PDB:1SKH}.
STRAND 109 111 {ECO:0000244|PDB:2HH0}.
HELIX 136 138 {ECO:0000244|PDB:1DWY}.
STRAND 139 141 {ECO:0000244|PDB:1DWY}.
HELIX 155 164 {ECO:0000244|PDB:4YX2}.
HELIX 165 167 {ECO:0000244|PDB:4YX2}.
HELIX 177 179 {ECO:0000244|PDB:4YX2}.
STRAND 180 182 {ECO:0000244|PDB:4YX2}.
HELIX 183 204 {ECO:0000244|PDB:4YX2}.
HELIX 211 233 {ECO:0000244|PDB:4YX2}.
SEQUENCE 264 AA; 28614 MW; D6D214038316A231 CRC64;
MVKSHIGSWI LVLFVAMWSD VGLCKKRPKP GGGWNTGGSR YPGQGSPGGN RYPPQGGGGW
GQPHGGGWGQ PHGGGWGQPH GGGWGQPHGG GWGQPHGGGG WGQGGTHGQW NKPSKPKTNM
KHVAGAAAAG AVVGGLGGYM LGSAMSRPLI HFGSDYEDRY YRENMHRYPN QVYYRPVDQY
SNQNNFVHDC VNITVKEHTV TTTTKGENFT ETDIKMMERV VEQMCITQYQ RESQAYYQRG
ASVILFSSPP VILLISFLIF LIVG


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