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Major prion protein (PrP) (CD antigen CD230)

 PRIO_CAPHI              Reviewed;         256 AA.
P52113;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
25-OCT-2017, entry version 94.
RecName: Full=Major prion protein;
Short=PrP;
AltName: CD_antigen=CD230;
Flags: Precursor;
Name=PRNP; Synonyms=PRP;
Capra hircus (Goat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Caprinae; Capra.
NCBI_TaxID=9925;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Anglo-Nubian; TISSUE=Peripheral blood lymphocyte;
Martin T.C., Hughes S.L., Hughes K.J., Dawson M.;
Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MET-142, AND POLYMORPHISM.
STRAIN=Anglo-Nubian;
PubMed=8922485; DOI=10.1099/0022-1317-77-11-2885;
Goldmann W., Martin T., Foster J., Hughes S., Smith G., Hughes K.,
Dawson M., Hunter N.;
"Novel polymorphisms in the caprine PrP gene: a codon 142 mutation
associated with scrapie incubation period.";
J. Gen. Virol. 77:2885-2891(1996).
[3]
ERRATUM.
Goldmann W., Martin T., Foster J., Hughes S., Smith G., Hughes K.,
Dawson M., Hunter N.;
J. Gen. Virol. 78:697-697(1997).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=African dwarf; TISSUE=Blood;
PubMed=8746958; DOI=10.1016/S0021-9975(05)80121-5;
Obermaier G., Kretzschmar H.A., Hafner A., Heubeck D., Dahme E.;
"Spongiform central nervous system myelinopathy in African dwarf
goats.";
J. Comp. Pathol. 113:357-372(1995).
-!- FUNCTION: Its primary physiological function is unclear. Has
cytoprotective activity against internal or environmental
stresses. May play a role in neuronal development and synaptic
plasticity. May be required for neuronal myelin sheath
maintenance. May play a role in iron uptake and iron homeostasis.
Soluble oligomers are toxic to cultured neuroblastoma cells and
induce apoptosis (in vitro). 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. Mislocalized cytosolically exposed PrP
interacts with MGRN1; this interaction alters MGRN1 subcellular
location and causes lysosomal enlargement. Interacts with
KIAA1191. {ECO:0000250|UniProtKB:P04156,
ECO:0000250|UniProtKB:P04925}.
-!- 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=Polymorphism at position 142 may be related to the
alleles of scrapie incubation-control (SIC) gene in this species.
{ECO:0000269|PubMed:8922485}.
-!- DISEASE: Note=Found in high quantity in the brain of humans and
animals infected with degenerative neurological diseases such as
kuru, Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler
syndrome (GSS), scrapie, bovine spongiform encephalopathy (BSE),
transmissible mink encephalopathy (TME), etc. {ECO:0000305}.
-!- SIMILARITY: Belongs to the prion family. {ECO:0000305}.
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EMBL; X74758; CAA52774.1; -; Genomic_DNA.
EMBL; X91999; CAA63050.1; -; Genomic_DNA.
EMBL; S82626; AAD14409.1; -; Genomic_DNA.
PIR; S37149; S37149.
RefSeq; XP_005688214.2; XM_005688157.3.
UniGene; Chi.21511; -.
ProteinModelPortal; P52113; -.
SMR; P52113; -.
GeneID; 102169975; -.
CTD; 5621; -.
HOVERGEN; HBG008260; -.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
Gene3D; 1.10.790.10; -; 1.
InterPro; IPR000817; Prion.
InterPro; IPR036924; Prion/Doppel_b-ribbon_dom_sf.
InterPro; IPR022416; Prion/Doppel_prot_b-ribbon_dom.
InterPro; IPR025860; Prion_N_dom.
PANTHER; PTHR10502:SF134; PTHR10502:SF134; 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.
3: Inferred from homology;
Amyloid; Cell membrane; Copper; Disulfide bond; Glycoprotein;
Golgi apparatus; GPI-anchor; Lipoprotein; Membrane; Metal-binding;
Polymorphism; Prion; Repeat; Signal; Zinc.
SIGNAL 1 24 {ECO:0000250}.
CHAIN 25 233 Major prion protein.
/FTId=PRO_0000025641.
PROPEP 234 256 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000025642.
REPEAT 54 62 1.
REPEAT 63 70 2.
REPEAT 71 78 3.
REPEAT 79 86 4.
REPEAT 87 95 5.
REGION 25 233 Interaction with GRB2, ERI3 and SYN1.
{ECO:0000250|UniProtKB:P04925}.
REGION 54 95 5 X 8 AA tandem repeats of P-H-G-G-G-W-G-
Q.
METAL 64 64 Copper or zinc 1.
{ECO:0000250|UniProtKB:P04156}.
METAL 65 65 Copper or zinc 1; via amide nitrogen.
{ECO:0000250|UniProtKB:P04156}.
METAL 66 66 Copper or zinc 1; via amide nitrogen and
carbonyl oxygen.
{ECO:0000250|UniProtKB:P04156}.
METAL 72 72 Copper or zinc 2.
{ECO:0000250|UniProtKB:P04156}.
METAL 73 73 Copper or zinc 2; via amide nitrogen.
{ECO:0000250|UniProtKB:P04156}.
METAL 74 74 Copper or zinc 2; via amide nitrogen and
carbonyl oxygen.
{ECO:0000250|UniProtKB:P04156}.
METAL 80 80 Copper or zinc 3.
{ECO:0000250|UniProtKB:P04156}.
METAL 81 81 Copper or zinc 3; via amide nitrogen.
{ECO:0000250|UniProtKB:P04156}.
METAL 82 82 Copper or zinc 3; via amide nitrogen and
carbonyl oxygen.
{ECO:0000250|UniProtKB:P04156}.
METAL 88 88 Copper or zinc 4.
{ECO:0000250|UniProtKB:P04156}.
METAL 90 90 Copper or zinc 4; via amide nitrogen.
{ECO:0000250|UniProtKB:P04156}.
METAL 91 91 Copper or zinc 4; via amide nitrogen and
carbonyl oxygen.
{ECO:0000250|UniProtKB:P04156}.
LIPID 233 233 GPI-anchor amidated alanine.
{ECO:0000255}.
CARBOHYD 184 184 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 200 200 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 182 217 {ECO:0000250|UniProtKB:P04273}.
VARIANT 142 142 I -> M (appears to be associated with
differing disease incubation periods in
goats experimentally infected with
isolates of bovine spongiform
encephalopathy or sheep scrapie).
{ECO:0000269|PubMed:8922485}.
SEQUENCE 256 AA; 27897 MW; BDA5795F6FD99746 CRC64;
MVKSHIGSWI LVLFVAMWSD VGLCKKRPKP GGGWNTGGSR YPGQGSPGGN RYPPQGGGGW
GQPHGGGWGQ PHGGGWGQPH GGGWGQPHGG GGWGQGGSHS QWNKPSKPKT NMKHVAGAAA
AGAVVGGLGG YMLGSAMSRP LIHFGNDYED RYYRENMYRY PNQVYYRPVD QYSNQNNFVH
DCVNITVKQH TVTTTTKGEN FTETDIKIME RVVEQMCITQ YQRESQAYYQ RGASVILFSP
PPVILLISFL IFLIVG


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