ID B3F6B5_BOVIN Unreviewed; 264 AA. AC B3F6B5; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 08-MAY-2019, entry version 55. DE RecName: Full=Major prion protein {ECO:0000256|RuleBase:RU003882}; GN Name=PRNP {ECO:0000313|EMBL:ABU98047.1}; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913 {ECO:0000313|EMBL:ABU98047.1}; RN [1] {ECO:0000313|EMBL:ABU98047.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=50-0039-3 {ECO:0000313|EMBL:ABU98047.1}; RX PubMed=18096956; RA Brunelle B.W., Kehrli M.E.Jr., Stabel J.R., Spurlock D.M., RA Hansen L.B., Nicholson E.M.; RT "Short communication: Allele, genotype, and haplotype data for bovine RT spongiform encephalopathy-resistance polymorphisms from healthy US RT Holstein cattle."; RL J. Dairy Sci. 91:338-342(2008). 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 CC an intermediate stage on the path to fibril formation. Copper CC binding may promote oligomerization. CC {ECO:0000256|SAAS:SAAS00537365}. CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|SAAS:SAAS00541856}; Lipid-anchor, GPI-anchor CC {ECO:0000256|SAAS:SAAS00541856}. CC -!- SIMILARITY: Belongs to the prion family. CC {ECO:0000256|RuleBase:RU003882, ECO:0000256|SAAS:SAAS00541861}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; EF626285; ABU98047.1; -; Genomic_DNA. DR eggNOG; ENOG410IJMM; Eukaryota. DR eggNOG; ENOG410YXUU; LUCA. DR OrthoDB; 1403854at2759; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro. DR Gene3D; 1.10.790.10; -; 1. 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 3: Inferred from homology; KW Amyloid {ECO:0000256|RuleBase:RU003882, ECO:0000313|EMBL:ABU98047.1}; KW Cell membrane {ECO:0000256|RuleBase:RU003882, KW ECO:0000256|SAAS:SAAS00424755}; KW Copper {ECO:0000256|SAAS:SAAS00944119}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00017659}; KW Membrane {ECO:0000256|RuleBase:RU003882, KW ECO:0000256|SAAS:SAAS00017645, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|SAAS:SAAS00944118}; KW Prion {ECO:0000256|RuleBase:RU003882, ECO:0000313|EMBL:ABU98047.1}; KW Repeat {ECO:0000256|SAAS:SAAS00216679}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 24 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 122 142 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 243 263 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 124 139 Prion/Doppel_prot_b-ribbon_dom. FT {ECO:0000259|PROSITE:PS00291}. FT DOMAIN 211 229 Prion/Doppel_prot_b-ribbon_dom. FT {ECO:0000259|PROSITE:PS00706}. SQ SEQUENCE 264 AA; 28668 MW; 751470504574A54C CRC64; MVKSHIGSWI LVLFVAMWSD VGLCKKRPKP GGGWNTGGSR YPGQGSPGGN RYPPQGGGXW GQPHGGGWGQ PHGGGWGQPH GGGWGQPHGG GWGQPHGGGG WGQGGTHGQW NKPSKPKTNM KHVAGAAAAG AVVGGLGGYM LGSAMSRPLI HFGSDYEDRY YRENMHRYPN QVYYRPVDQY SNQNNFVHDC VNITVKEHTV TTTTKGENFT ETDIKMMERV VEQMCITQYQ RESQAYYQRG ASVILFSSPP VILLISFLIF LIVG //