PRIO_BOVIN
ID PRIO_BOVIN Reviewed; 264 AA.
AC P10279; A1YVV9; Q01880; Q0VD57; Q5UJJ5; Q5UJM6; Q5UK69; Q5UK71; Q6UL03;
AC Q6UL04; Q6UL05; Q6UL06; Q7YRN3; Q8MJI7;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 2.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Major prion protein;
DE Short=PrP;
DE AltName: Full=Major scrapie-associated fibril protein 1;
DE AltName: CD_antigen=CD230;
DE Flags: Precursor;
GN Name=PRNP; Synonyms=PRP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Holstein-Friesian;
RX PubMed=1671225; DOI=10.1099/0022-1317-72-1-201;
RA Goldmann W., Hunter N., Martin T., Dawson M., Hope J.;
RT "Different forms of the bovine PrP gene have five or six copies of a short,
RT G-C-rich element within the protein-coding exon.";
RL J. Gen. Virol. 72:201-204(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANTS 92-TRP--GLY 99 DEL
RP AND ASN-154.
RC STRAIN=Holstein-Friesian; TISSUE=Brain;
RX PubMed=1362024; DOI=10.1007/bf01703083;
RA Yoshimoto J., Iinuma T., Ishiguro N., Horiuchi M., Imamura M.,
RA Shinagawa M.;
RT "Comparative sequence analysis and expression of bovine PrP gene in mouse
RT L-929 cells.";
RL Virus Genes 6:343-356(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8440932; DOI=10.1093/infdis/167.3.602;
RA Prusiner S.B., Fuzi M., Scott M., Serban D., Serban H., Taraboulos A.,
RA Gabriel J.M., Wells G.A., Wilesmith J.W., Bradley R.;
RT "Immunologic and molecular biologic studies of prion proteins in bovine
RT spongiform encephalopathy.";
RL J. Infect. Dis. 167:602-613(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Holstein-Friesian; TISSUE=Brain;
RA Horiuchi M., Ishiguro N., Nagasawa H., Toyoda Y., Shinagawa M.;
RT "Genomic organization of bovine PrP gene and complete nucleotide sequence
RT of bovine PrP cDNA.";
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Jersey;
RX PubMed=11531705; DOI=10.1046/j.1365-2052.2001.0769a.x;
RA Hills D., Comincini S., Schlaepfer J., Dolf G., Ferretti L., Williams J.L.;
RT "Complete genomic sequence of the bovine prion gene (PRNP) and polymorphism
RT in its promoter region.";
RL Anim. Genet. 32:231-232(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT
RP GLY-TRP-GLY-GLN-PRO-HIS-GLY-GLY-98 INS.
RA Naharro G., Yugueros J., Temprano A.;
RT "Bovine PrP gene for prion protein.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Korean;
RA Yoo H.S., Kang S.G., Choi I.S., Kang S.K., Hwang W.S.;
RT "Nucleotide sequence of PrP cDNA in Korean cattle.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=14722726; DOI=10.1007/s00335-003-2283-y;
RA Heaton M.P., Leymaster K.A., Freking B.A., Hawk D.A., Smith T.P.,
RA Keele J.W., Snelling W.M., Fox J.M., Chitko-McKown C.G., Laegreid W.W.;
RT "Prion gene sequence variation within diverse groups of U.S. sheep, beef
RT cattle, and deer.";
RL Mamm. Genome 14:765-777(2003).
RN [9]
RP SEQUENCE REVISION TO 211, AND VARIANT LYS-211.
RX PubMed=18625065; DOI=10.1186/1746-6148-4-25;
RA Heaton M.P., Keele J.W., Harhay G.P., Richt J.A., Koohmaraie M.,
RA Wheeler T.L., Shackelford S.D., Casas E., King D.A., Sonstegard T.S.,
RA Van Tassell C.P., Neibergs H.L., Chase C.C. Jr., Kalbfleisch T.S.,
RA Smith T.P.L., Clawson M.L., Laegreid W.W.;
RT "Prevalence of the prion protein gene E211K variant in U.S. cattle.";
RL BMC Vet. Res. 4:25-25(2008).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-60; ARG-94; ASN-154 AND
RP ARG-234.
RC STRAIN=Holstein-Friesian, and Qinchuan; TISSUE=Blood;
RA Wu R., Xie Q.G., Liu X.T., Chen H.T., Cheng J.;
RT "Cloning and sequence analysis of bovine prion protein gene.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS 84-TRP--GLY 99 DEL;
RP 92-TRP--GLY 99 DEL AND GLY-TRP-GLY-GLN-PRO-HIS-GLY-GLY-98 INS.
RX PubMed=15477588; DOI=10.1073/pnas.0406403101;
RA Seabury C.M., Honeycutt R.L., Rooney A.P., Halbert N.D., Derr J.N.;
RT "Prion protein gene (PRNP) variants and evidence for strong purifying
RT selection in functionally important regions of bovine exon 3.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15142-15147(2004).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Uboldi C., Bertoni A., Del Vecchio I., Comincini S., Hills D.,
RA Schlaepfer J., Dolf G., Williams J.L., Ferretti L.;
RT "Genomic characterization of the bovine PRN loci (PRNP, PRND and PRNT).";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16460908; DOI=10.1016/j.ygeno.2005.12.012;
RA Choi S.-H., Kim I.-C., Kim D.-S., Kim D.-W., Chae S.-H., Choi H.-H.,
RA Choi I., Yeo J.-S., Song M.-N., Park H.-S.;
RT "Comparative genomic organization of the human and bovine PRNP locus.";
RL Genomics 87:598-607(2006).
RN [14]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Holstein, and Japanese black; TISSUE=Semen;
RA Abe T., Hasebe H., Kobayashi E.;
RT "Frequencies of bovine PrP gene polymorphisms in Japanese-black and
RT Holstein bulls in japan.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [15]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Brain;
RA Barbieri I., Brocchi E., Borre A., Moretti M., Gelmetti D., Capucci L.;
RT "Detection of prion protein in various animal species by a new set of
RT monoclonal antibodies.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [16]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [17]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
RA Tanaka M., Inoue S., Ikeda T., Horiuchi M., Ishiguro N., Shinagawa M.;
RT "Characterization of bovine PrP promoter region.";
RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN [18]
RP PROTEIN SEQUENCE OF 25-36.
RX PubMed=2904126; DOI=10.1038/336390a0;
RA Hope J., Reekie L.J.D., Hunter N., Multhaup G., Beyreuther K., White H.,
RA Scott A.C., Stack M.J., Dawson M., Wells G.A.;
RT "Fibrils from brains of cows with new cattle disease contain scrapie-
RT associated protein.";
RL Nature 336:390-392(1988).
RN [19]
RP STRUCTURE BY NMR OF 1-30.
RX PubMed=15554701; DOI=10.1021/bi0485070;
RA Biverstahl H., Andersson A., Graslund A., Maler L.;
RT "NMR solution structure and membrane interaction of the N-terminal sequence
RT (1-30) of the bovine prion protein.";
RL Biochemistry 43:14940-14947(2004).
RN [20]
RP STRUCTURE BY NMR OF 132-241.
RX PubMed=10899999; DOI=10.1073/pnas.97.15.8334;
RA Lopez Garcia F., Zahn R., Riek R., Wuethrich K.;
RT "NMR structure of the bovine prion protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:8334-8339(2000).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 107-115 IN COMPLEX WITH ANTIBODY
RP FRAGMENT.
RX PubMed=16962610; DOI=10.1016/j.jmb.2006.07.027;
RA Luginbuhl B., Kanyo Z., Jones R.M., Fletterick R.J., Prusiner S.B.,
RA Cohen F.E., Williamson R.A., Burton D.R., Pluckthun A.;
RT "Directed evolution of an anti-prion protein scFv fragment to an affinity
RT of 1 pM and its structural interpretation.";
RL J. Mol. Biol. 363:75-97(2006).
CC -!- FUNCTION: Its primary physiological function is unclear. May play a
CC role in neuronal development and synaptic plasticity. May be required
CC for neuronal myelin sheath maintenance. May promote myelin homeostasis
CC through acting as an agonist for ADGRG6 receptor. May play a role in
CC iron uptake and iron homeostasis. Soluble oligomers are toxic to
CC cultured neuroblastoma cells and induce apoptosis (in vitro) (By
CC similarity). Association with GPC1 (via its heparan sulfate chains)
CC targets PRNP to lipid rafts. Also provides Cu(2+) or Zn(2+) for the
CC ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate
CC side chains (By similarity). {ECO:0000250|UniProtKB:P04156,
CC ECO:0000250|UniProtKB:P04925}.
CC -!- SUBUNIT: Monomer and homodimer. Has a tendency to aggregate into
CC amyloid fibrils containing a cross-beta spine, formed by a steric
CC zipper of superposed beta-strands. Soluble oligomers may represent an
CC intermediate stage on the path to fibril formation. Copper binding may
CC promote oligomerization. Interacts with GRB2, APP, ERI3/PRNPIP and SYN1
CC (By similarity). Mislocalized cytosolically exposed PrP interacts with
CC MGRN1; this interaction alters MGRN1 subcellular location and causes
CC lysosomal enlargement (By similarity). Interacts with APP. Interacts
CC with KIAA1191 (By similarity). Interacts with ADGRG6 (By similarity).
CC {ECO:0000250|UniProtKB:P04156, ECO:0000250|UniProtKB:P04925}.
CC -!- INTERACTION:
CC P10279; P10279: PRNP; NbExp=3; IntAct=EBI-7430632, EBI-7430632;
CC P10279; P04156: PRNP; Xeno; NbExp=5; IntAct=EBI-7430632, EBI-977302;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P04156};
CC Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P04156}. Golgi
CC apparatus {ECO:0000250|UniProtKB:P04925}. Note=Targeted to lipid rafts
CC via association with the heparan sulfate chains of GPC1. Colocates, in
CC the presence of Cu(2+), to vesicles in para- and perinuclear regions,
CC where both proteins undergo internalization. Heparin displaces PRNP
CC from lipid rafts and promotes endocytosis.
CC {ECO:0000250|UniProtKB:P04156}.
CC -!- DOMAIN: The normal, monomeric form has a mainly alpha-helical
CC structure. The disease-associated, protease-resistant form forms
CC amyloid fibrils containing a cross-beta spine, formed by a steric
CC zipper of superposed beta-strands. Disease mutations may favor
CC intermolecular contacts via short beta strands, and may thereby trigger
CC oligomerization. {ECO:0000250|UniProtKB:P04156}.
CC -!- DOMAIN: Contains an N-terminal region composed of octamer repeats. At
CC low copper concentrations, the sidechains of His residues from three or
CC four repeats contribute to the binding of a single copper ion.
CC Alternatively, a copper ion can be bound by interaction with the
CC sidechain and backbone amide nitrogen of a single His residue. The
CC observed copper binding stoichiometry suggests that two repeat regions
CC cooperate to stabilize the binding of a single copper ion. At higher
CC copper concentrations, each octamer can bind one copper ion by
CC interactions with the His sidechain and Gly backbone atoms. A mixture
CC of binding types may occur, especially in the case of octamer repeat
CC expansion. Copper binding may stabilize the conformation of this region
CC and may promote oligomerization. {ECO:0000250|UniProtKB:P04156}.
CC -!- DISEASE: Note=Variations in PRNP are responsible of transmissible
CC bovine spongiform encephalopathies (BSE), a class of neurodegenerative
CC diseases that affect various mammals. These diseases are caused by
CC abnormally folded prion proteins. BSE can be subdivided into at least
CC three groups: classical, H-type and L-type, with the latter 2
CC collectively referred to as atypical BSE. Susceptibility or resistance
CC to a BSE disease can be influenced by at least 3 factors related to the
CC host prion protein: protein expression levels, number of octapeptide
CC repeats, and specific polymorphisms. In cattle, as in humans, BSEs can
CC occur as infectious, spontaneous and genetic diseases. {ECO:0000305}.
CC -!- MISCELLANEOUS: This protein is produced by a bicistronic gene which
CC also produces the major prion protein/PRNP from an overlapping reading
CC frame.
CC -!- MISCELLANEOUS: The alternative prion protein/AltPrP (AC F7VJQ2) and
CC PRNP have no apparent direct functional relation since a mutation that
CC removes the start codon of the AltPrP has no apparent effect on the
CC biology of PRNP (By similarity). In mouse and hamster, the alternative
CC initiation AUG codon is absent and is replaced by a GUG codon.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the prion family. {ECO:0000305}.
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DR EMBL; X55882; CAA39368.1; -; Genomic_DNA.
DR EMBL; D10612; BAA01467.1; -; mRNA.
DR EMBL; D10613; BAA01468.1; -; Genomic_DNA.
DR EMBL; D10614; BAA01469.1; -; Genomic_DNA.
DR EMBL; S55629; AAB25514.1; -; mRNA.
DR EMBL; AB001468; BAA19253.1; -; mRNA.
DR EMBL; AJ298878; CAC37367.1; -; Genomic_DNA.
DR EMBL; AF455119; AAM73856.1; -; Genomic_DNA.
DR EMBL; AF517842; AAM66709.1; -; mRNA.
DR EMBL; AY335912; AAP84097.2; -; Genomic_DNA.
DR EMBL; AY367638; AAQ64645.1; -; Genomic_DNA.
DR EMBL; AY367639; AAQ64646.1; -; Genomic_DNA.
DR EMBL; AY367640; AAQ64647.1; -; Genomic_DNA.
DR EMBL; AY367641; AAQ64648.1; -; Genomic_DNA.
DR EMBL; AY367642; AAQ64649.1; -; Genomic_DNA.
DR EMBL; AY367643; AAQ64650.1; -; Genomic_DNA.
DR EMBL; AY720445; AAV30252.1; -; Genomic_DNA.
DR EMBL; AY720446; AAV30253.1; -; Genomic_DNA.
DR EMBL; AY720448; AAV30255.1; -; Genomic_DNA.
DR EMBL; AY720449; AAV30256.1; -; Genomic_DNA.
DR EMBL; AY720450; AAV30257.1; -; Genomic_DNA.
DR EMBL; AY720451; AAV30258.1; -; Genomic_DNA.
DR EMBL; AY720452; AAV30259.1; -; Genomic_DNA.
DR EMBL; AY720453; AAV30260.1; -; Genomic_DNA.
DR EMBL; AY720454; AAV30261.1; -; Genomic_DNA.
DR EMBL; AY720455; AAV30262.1; -; Genomic_DNA.
DR EMBL; AY720458; AAV30265.1; -; Genomic_DNA.
DR EMBL; AY720459; AAV30266.1; -; Genomic_DNA.
DR EMBL; AY720460; AAV30267.1; -; Genomic_DNA.
DR EMBL; AY720461; AAV30268.1; -; Genomic_DNA.
DR EMBL; AY720462; AAV30269.1; -; Genomic_DNA.
DR EMBL; AY720463; AAV30270.1; -; Genomic_DNA.
DR EMBL; AY720464; AAV30271.1; -; Genomic_DNA.
DR EMBL; AY720465; AAV30272.1; -; Genomic_DNA.
DR EMBL; AY720466; AAV30273.1; -; Genomic_DNA.
DR EMBL; AY720467; AAV30274.1; -; Genomic_DNA.
DR EMBL; AY720468; AAV30275.1; -; Genomic_DNA.
DR EMBL; AY720469; AAV30276.1; -; Genomic_DNA.
DR EMBL; AY720470; AAV30277.1; -; Genomic_DNA.
DR EMBL; AY720471; AAV30278.1; -; Genomic_DNA.
DR EMBL; AY720472; AAV30279.1; -; Genomic_DNA.
DR EMBL; AY720473; AAV30280.1; -; Genomic_DNA.
DR EMBL; AY720474; AAV30281.1; -; Genomic_DNA.
DR EMBL; AY720475; AAV30282.1; -; Genomic_DNA.
DR EMBL; AY720476; AAV30283.1; -; Genomic_DNA.
DR EMBL; AY720477; AAV30284.1; -; Genomic_DNA.
DR EMBL; AY720478; AAV30285.1; -; Genomic_DNA.
DR EMBL; AY720479; AAV30286.1; -; Genomic_DNA.
DR EMBL; AY720480; AAV30287.1; -; Genomic_DNA.
DR EMBL; AY720481; AAV30288.1; -; Genomic_DNA.
DR EMBL; AY720482; AAV30289.1; -; Genomic_DNA.
DR EMBL; AY720483; AAV30290.1; -; Genomic_DNA.
DR EMBL; AY720484; AAV30291.1; -; Genomic_DNA.
DR EMBL; AY720485; AAV30292.1; -; Genomic_DNA.
DR EMBL; AY720486; AAV30293.1; -; Genomic_DNA.
DR EMBL; AY720488; AAV30295.1; -; Genomic_DNA.
DR EMBL; AY720489; AAV30296.1; -; Genomic_DNA.
DR EMBL; AY720492; AAV30299.1; -; Genomic_DNA.
DR EMBL; AY720493; AAV30300.1; -; Genomic_DNA.
DR EMBL; AY720494; AAV30301.1; -; Genomic_DNA.
DR EMBL; AY720495; AAV30302.1; -; Genomic_DNA.
DR EMBL; AY720496; AAV30303.1; -; Genomic_DNA.
DR EMBL; AY720497; AAV30304.1; -; Genomic_DNA.
DR EMBL; AY720498; AAV30305.1; -; Genomic_DNA.
DR EMBL; AY720503; AAV30310.1; -; Genomic_DNA.
DR EMBL; AY720504; AAV30311.1; -; Genomic_DNA.
DR EMBL; AY720505; AAV30312.1; -; Genomic_DNA.
DR EMBL; AY720506; AAV30313.1; -; Genomic_DNA.
DR EMBL; AY720507; AAV30314.1; -; Genomic_DNA.
DR EMBL; AY720508; AAV30315.1; -; Genomic_DNA.
DR EMBL; AY720509; AAV30316.1; -; Genomic_DNA.
DR EMBL; AY720510; AAV30317.1; -; Genomic_DNA.
DR EMBL; AY720511; AAV30318.1; -; Genomic_DNA.
DR EMBL; AY720512; AAV30319.1; -; Genomic_DNA.
DR EMBL; AY720513; AAV30320.1; -; Genomic_DNA.
DR EMBL; AY720514; AAV30321.1; -; Genomic_DNA.
DR EMBL; AY720525; AAV30332.1; -; Genomic_DNA.
DR EMBL; AY720530; AAV30337.1; -; Genomic_DNA.
DR EMBL; AY720531; AAV30338.1; -; Genomic_DNA.
DR EMBL; AY720532; AAV30339.1; -; Genomic_DNA.
DR EMBL; AY720533; AAV30340.1; -; Genomic_DNA.
DR EMBL; AY720534; AAV30341.1; -; Genomic_DNA.
DR EMBL; AY720535; AAV30342.1; -; Genomic_DNA.
DR EMBL; AY720540; AAV30347.1; -; Genomic_DNA.
DR EMBL; AY720541; AAV30348.1; -; Genomic_DNA.
DR EMBL; AY720544; AAV30351.1; -; Genomic_DNA.
DR EMBL; AY720545; AAV30352.1; -; Genomic_DNA.
DR EMBL; AY720546; AAV30353.1; -; Genomic_DNA.
DR EMBL; AY720547; AAV30354.1; -; Genomic_DNA.
DR EMBL; AY720548; AAV30355.1; -; Genomic_DNA.
DR EMBL; AY720549; AAV30356.1; -; Genomic_DNA.
DR EMBL; AY720550; AAV30357.1; -; Genomic_DNA.
DR EMBL; AY720551; AAV30358.1; -; Genomic_DNA.
DR EMBL; AY720552; AAV30359.1; -; Genomic_DNA.
DR EMBL; AY720553; AAV30360.1; -; Genomic_DNA.
DR EMBL; AY720554; AAV30361.1; -; Genomic_DNA.
DR EMBL; AY720555; AAV30362.1; -; Genomic_DNA.
DR EMBL; AY720556; AAV30363.1; -; Genomic_DNA.
DR EMBL; AY720557; AAV30364.1; -; Genomic_DNA.
DR EMBL; AY720558; AAV30365.1; -; Genomic_DNA.
DR EMBL; AY720559; AAV30366.1; -; Genomic_DNA.
DR EMBL; AY720560; AAV30367.1; -; Genomic_DNA.
DR EMBL; AY720561; AAV30368.1; -; Genomic_DNA.
DR EMBL; AY720562; AAV30369.1; -; Genomic_DNA.
DR EMBL; AY720563; AAV30370.1; -; Genomic_DNA.
DR EMBL; AY720564; AAV30371.1; -; Genomic_DNA.
DR EMBL; AY720565; AAV30372.1; -; Genomic_DNA.
DR EMBL; AY720566; AAV30373.1; -; Genomic_DNA.
DR EMBL; AY720567; AAV30374.1; -; Genomic_DNA.
DR EMBL; AY720568; AAV30375.1; -; Genomic_DNA.
DR EMBL; AY720569; AAV30376.1; -; Genomic_DNA.
DR EMBL; AY720570; AAV30377.1; -; Genomic_DNA.
DR EMBL; AY720571; AAV30378.1; -; Genomic_DNA.
DR EMBL; AY720572; AAV30379.1; -; Genomic_DNA.
DR EMBL; AY720573; AAV30380.1; -; Genomic_DNA.
DR EMBL; AY720574; AAV30381.1; -; Genomic_DNA.
DR EMBL; AY720581; AAV30388.1; -; Genomic_DNA.
DR EMBL; AY720582; AAV30389.1; -; Genomic_DNA.
DR EMBL; AY720583; AAV30390.1; -; Genomic_DNA.
DR EMBL; AY720584; AAV30391.1; -; Genomic_DNA.
DR EMBL; AY720585; AAV30392.1; -; Genomic_DNA.
DR EMBL; AY720588; AAV30395.1; -; Genomic_DNA.
DR EMBL; AY720591; AAV30398.1; -; Genomic_DNA.
DR EMBL; AY720594; AAV30401.1; -; Genomic_DNA.
DR EMBL; AY720595; AAV30402.1; -; Genomic_DNA.
DR EMBL; AY720596; AAV30403.1; -; Genomic_DNA.
DR EMBL; AY720597; AAV30404.1; -; Genomic_DNA.
DR EMBL; AY720600; AAV30407.1; -; Genomic_DNA.
DR EMBL; AY720601; AAV30408.1; -; Genomic_DNA.
DR EMBL; AY720602; AAV30409.1; -; Genomic_DNA.
DR EMBL; AY720603; AAV30410.1; -; Genomic_DNA.
DR EMBL; AY720604; AAV30411.1; -; Genomic_DNA.
DR EMBL; AY720605; AAV30412.1; -; Genomic_DNA.
DR EMBL; AY720606; AAV30413.1; -; Genomic_DNA.
DR EMBL; AY720607; AAV30414.1; -; Genomic_DNA.
DR EMBL; AY720608; AAV30415.1; -; Genomic_DNA.
DR EMBL; AY720609; AAV30416.1; -; Genomic_DNA.
DR EMBL; AY720610; AAV30417.1; -; Genomic_DNA.
DR EMBL; AY720611; AAV30418.1; -; Genomic_DNA.
DR EMBL; AY720612; AAV30419.1; -; Genomic_DNA.
DR EMBL; AY720613; AAV30420.1; -; Genomic_DNA.
DR EMBL; AY720622; AAV30429.1; -; Genomic_DNA.
DR EMBL; AY720623; AAV30430.1; -; Genomic_DNA.
DR EMBL; AY720624; AAV30431.1; -; Genomic_DNA.
DR EMBL; AY720625; AAV30432.1; -; Genomic_DNA.
DR EMBL; AY720626; AAV30433.1; -; Genomic_DNA.
DR EMBL; AY720627; AAV30434.1; -; Genomic_DNA.
DR EMBL; AY720628; AAV30435.1; -; Genomic_DNA.
DR EMBL; AY720629; AAV30436.1; -; Genomic_DNA.
DR EMBL; AY720630; AAV30437.1; -; Genomic_DNA.
DR EMBL; AY720631; AAV30438.1; -; Genomic_DNA.
DR EMBL; AY720632; AAV30439.1; -; Genomic_DNA.
DR EMBL; AY720633; AAV30440.1; -; Genomic_DNA.
DR EMBL; AY720634; AAV30441.1; -; Genomic_DNA.
DR EMBL; AY720635; AAV30442.1; -; Genomic_DNA.
DR EMBL; AY720636; AAV30443.1; -; Genomic_DNA.
DR EMBL; AY720637; AAV30444.1; -; Genomic_DNA.
DR EMBL; AY720640; AAV30447.1; -; Genomic_DNA.
DR EMBL; AY720641; AAV30448.1; -; Genomic_DNA.
DR EMBL; AY720642; AAV30449.1; -; Genomic_DNA.
DR EMBL; AY720643; AAV30450.1; -; Genomic_DNA.
DR EMBL; AY720644; AAV30451.1; -; Genomic_DNA.
DR EMBL; AY720645; AAV30452.1; -; Genomic_DNA.
DR EMBL; AY720648; AAV30455.1; -; Genomic_DNA.
DR EMBL; AY720649; AAV30456.1; -; Genomic_DNA.
DR EMBL; AY720650; AAV30457.1; -; Genomic_DNA.
DR EMBL; AY720651; AAV30458.1; -; Genomic_DNA.
DR EMBL; AY720652; AAV30459.1; -; Genomic_DNA.
DR EMBL; AY720653; AAV30460.1; -; Genomic_DNA.
DR EMBL; AY720654; AAV30461.1; -; Genomic_DNA.
DR EMBL; AY720655; AAV30462.1; -; Genomic_DNA.
DR EMBL; AY720656; AAV30463.1; -; Genomic_DNA.
DR EMBL; AY720657; AAV30464.1; -; Genomic_DNA.
DR EMBL; AY720662; AAV30469.1; -; Genomic_DNA.
DR EMBL; AY720663; AAV30470.1; -; Genomic_DNA.
DR EMBL; AY720664; AAV30471.1; -; Genomic_DNA.
DR EMBL; AY720667; AAV30474.1; -; Genomic_DNA.
DR EMBL; AY720668; AAV30475.1; -; Genomic_DNA.
DR EMBL; AY720669; AAV30476.1; -; Genomic_DNA.
DR EMBL; AY720670; AAV30477.1; -; Genomic_DNA.
DR EMBL; AY720671; AAV30478.1; -; Genomic_DNA.
DR EMBL; AY720672; AAV30479.1; -; Genomic_DNA.
DR EMBL; AY720673; AAV30480.1; -; Genomic_DNA.
DR EMBL; AY720674; AAV30481.1; -; Genomic_DNA.
DR EMBL; AY720675; AAV30482.1; -; Genomic_DNA.
DR EMBL; AY720676; AAV30483.1; -; Genomic_DNA.
DR EMBL; AY720677; AAV30484.1; -; Genomic_DNA.
DR EMBL; AY720678; AAV30485.1; -; Genomic_DNA.
DR EMBL; DQ205538; ABB51165.1; -; Genomic_DNA.
DR EMBL; AY944236; AAY21624.1; -; Genomic_DNA.
DR EMBL; AB248079; BAE78586.1; -; Genomic_DNA.
DR EMBL; AB247937; BAE78583.1; -; Genomic_DNA.
DR EMBL; EF139165; ABL75501.1; -; Genomic_DNA.
DR EMBL; BC119821; AAI19822.1; -; mRNA.
DR EMBL; D26151; BAA05138.1; -; Genomic_DNA.
DR PIR; A54330; A54330.
DR PIR; JU0268; JU0268.
DR RefSeq; NP_001258555.1; NM_001271626.2.
DR RefSeq; NP_851358.2; NM_181015.3.
DR PDB; 1DWY; NMR; -; A=132-241.
DR PDB; 1DWZ; NMR; -; A=132-241.
DR PDB; 1DX0; NMR; -; A=25-241.
DR PDB; 1DX1; NMR; -; A=25-241.
DR PDB; 1SKH; NMR; -; A=1-30.
DR PDB; 2HH0; X-ray; 2.85 A; P=107-115.
DR PDB; 2RSK; NMR; -; C/D=108-119.
DR PDB; 2RU7; NMR; -; C/D=108-119.
DR PDB; 4YX2; X-ray; 2.19 A; A=103-242.
DR PDBsum; 1DWY; -.
DR PDBsum; 1DWZ; -.
DR PDBsum; 1DX0; -.
DR PDBsum; 1DX1; -.
DR PDBsum; 1SKH; -.
DR PDBsum; 2HH0; -.
DR PDBsum; 2RSK; -.
DR PDBsum; 2RU7; -.
DR PDBsum; 4YX2; -.
DR AlphaFoldDB; P10279; -.
DR BMRB; P10279; -.
DR SMR; P10279; -.
DR BioGRID; 158758; 3.
DR IntAct; P10279; 1.
DR MINT; P10279; -.
DR STRING; 9913.ENSBTAP00000043233; -.
DR PaxDb; P10279; -.
DR ABCD; P10279; 10 sequenced antibodies.
DR GeneID; 281427; -.
DR CTD; 5621; -.
DR eggNOG; ENOG502S2A8; Eukaryota.
DR HOGENOM; CLU_094631_0_0_1; -.
DR InParanoid; P10279; -.
DR OrthoDB; 1403854at2759; -.
DR TreeFam; TF105188; -.
DR EvolutionaryTrace; P10279; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR DisProt; DP00783; -.
DR Gene3D; 1.10.790.10; -; 1.
DR IDEAL; IID50068; -.
DR InterPro; IPR000817; Prion.
DR InterPro; IPR036924; Prion/Doppel_b-ribbon_dom_sf.
DR InterPro; IPR022416; Prion/Doppel_prot_b-ribbon_dom.
DR InterPro; IPR025860; Prion_N_dom.
DR Pfam; PF00377; Prion; 1.
DR Pfam; PF11587; Prion_bPrPp; 1.
DR PRINTS; PR00341; PRION.
DR SMART; SM00157; PRP; 1.
DR SUPFAM; SSF54098; SSF54098; 1.
DR PROSITE; PS00291; PRION_1; 1.
DR PROSITE; PS00706; PRION_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amyloid; Cell membrane; Copper; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Golgi apparatus; GPI-anchor; Lipoprotein;
KW Membrane; Metal-binding; Prion; Reference proteome; Repeat; Signal; Zinc.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:2904126"
FT CHAIN 25..241
FT /note="Major prion protein"
FT /id="PRO_0000025627"
FT PROPEP 242..264
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000025628"
FT REPEAT 54..62
FT /note="1"
FT REPEAT 63..70
FT /note="2"
FT REPEAT 71..78
FT /note="3"
FT REPEAT 79..86
FT /note="4"
FT REPEAT 87..94
FT /note="5"
FT REPEAT 95..103
FT /note="6"
FT REGION 25..241
FT /note="Interaction with GRB2, ERI3 and SYN1"
FT /evidence="ECO:0000250|UniProtKB:P04925"
FT REGION 25..41
FT /note="Interaction with ADGRG6"
FT /evidence="ECO:0000250|UniProtKB:P04925"
FT REGION 28..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..103
FT /note="6 X 8 AA tandem repeats of P-H-G-G-G-W-G-Q"
FT BINDING 72
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04156"
FT BINDING 73
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04156"
FT BINDING 74
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04156"
FT BINDING 80
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04156"
FT BINDING 81
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04156"
FT BINDING 82
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04156"
FT BINDING 88
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P04156"
FT BINDING 89
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P04156"
FT BINDING 90
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P04156"
FT BINDING 96
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P04156"
FT BINDING 98
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P04156"
FT BINDING 99
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P04156"
FT LIPID 241
FT /note="GPI-anchor amidated alanine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 190..225
FT VARIANT 60
FT /note="W -> R"
FT /evidence="ECO:0000269|Ref.10"
FT VARIANT 71..78
FT /note="Missing (in allele 2)"
FT VARIANT 84..99
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:15477588"
FT VARIANT 92..99
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:1362024,
FT ECO:0000269|PubMed:15477588"
FT VARIANT 94
FT /note="Q -> R"
FT /evidence="ECO:0000269|Ref.10"
FT VARIANT 98
FT /note="G -> GGWGQPHGG"
FT /evidence="ECO:0000269|Ref.6"
FT VARIANT 154
FT /note="S -> N"
FT /evidence="ECO:0000269|PubMed:1362024, ECO:0000269|Ref.10"
FT VARIANT 211
FT /note="E -> K"
FT /evidence="ECO:0000269|PubMed:18625065"
FT VARIANT 234
FT /note="Q -> R"
FT /evidence="ECO:0000269|Ref.10"
FT CONFLICT 106..108
FT /note="THG -> SHS (in Ref. 2; BAA01469)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="E -> K (in Ref. 2; BAA01467 and 4; BAA19253)"
FT /evidence="ECO:0000305"
FT TURN 3..8
FT /evidence="ECO:0007829|PDB:1SKH"
FT HELIX 9..21
FT /evidence="ECO:0007829|PDB:1SKH"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:1SKH"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:2HH0"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:1DWY"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:1DWY"
FT HELIX 155..164
FT /evidence="ECO:0007829|PDB:4YX2"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:4YX2"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:4YX2"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:4YX2"
FT HELIX 183..204
FT /evidence="ECO:0007829|PDB:4YX2"
FT HELIX 211..233
FT /evidence="ECO:0007829|PDB:4YX2"
SQ 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
