ID A2BDH2_PONAB Unreviewed; 253 AA. AC A2BDH2; A0A2J8RZW5; A0A6D2XFT6; DT 20-FEB-2007, integrated into UniProtKB/TrEMBL. DT 20-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 132. DE RecName: Full=Major prion protein {ECO:0000256|ARBA:ARBA00021648, ECO:0000256|RuleBase:RU003882}; GN Name=prnp {ECO:0000313|EMBL:CAJ43808.1}; GN Synonyms=PRNP {ECO:0000313|Ensembl:ENSPPYP00000012064.1}; GN ORFNames=CR201_G0047355 {ECO:0000313|EMBL:PNJ14066.1}; OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Pongo. OX NCBI_TaxID=9601 {ECO:0000313|EMBL:CAJ43808.1}; RN [1] {ECO:0000313|EMBL:CAJ43808.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=17199895; DOI=10.1186/1471-2164-8-1; RA Premzl M., Gamulin V.; RT "Comparative genomic analysis of prion genes."; RL BMC Genomics 8:1-1(2007). RN [2] {ECO:0000313|Ensembl:ENSPPYP00000012064.1, ECO:0000313|Proteomes:UP000001595} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Wilson R.K., Mardis E.; RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:CAJ43808.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=19247565; DOI=10.1007/s00239-008-9176-3; RA Premzl M., Gamulin V.; RT "Positive selection in prion protein."; RL J. Mol. Evol. 68:205-207(2009). RN [4] {ECO:0000313|EMBL:PNJ14066.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Susie {ECO:0000313|EMBL:PNJ14066.1}; RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M., RA Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J., RA Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M., RA Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B., RA Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.; RT "High-resolution comparative analysis of great ape genomes."; RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|Ensembl:ENSPPYP00000012064.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Golgi CC apparatus {ECO:0000256|ARBA:ARBA00004555}. Membrane CC {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor CC {ECO:0000256|ARBA:ARBA00004589}. CC -!- SIMILARITY: Belongs to the prion family. CC {ECO:0000256|ARBA:ARBA00009910, ECO:0000256|RuleBase:RU003882}. 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; BN000848; CAJ43808.1; -; Genomic_DNA. DR EMBL; NDHI03003628; PNJ14066.1; -; Genomic_DNA. DR EMBL; NDHI03003628; PNJ14067.1; -; Genomic_DNA. DR RefSeq; NP_001124544.1; NM_001131072.1. DR RefSeq; XP_009231669.1; XM_009233394.1. DR RefSeq; XP_009231670.1; XM_009233395.1. DR STRING; 9601.ENSPPYP00000012064; -. DR Ensembl; ENSPPYT00000012541.2; ENSPPYP00000012064.1; ENSPPYG00000010800.2. DR GeneID; 100173712; -. DR KEGG; pon:100173712; -. DR CTD; 5621; -. DR eggNOG; ENOG502S2A8; Eukaryota. DR GeneTree; ENSGT00510000049083; -. DR HOGENOM; CLU_094631_0_0_1; -. DR OMA; QMCTTQY; -. DR OrthoDB; 5265139at2759; -. DR TreeFam; TF105188; -. DR Proteomes; UP000001595; Chromosome 20. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0030425; C:dendrite; IEA:Ensembl. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl. DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell. DR GO; GO:0016234; C:inclusion body; IEA:Ensembl. DR GO; GO:0045121; C:membrane raft; IEA:Ensembl. DR GO; GO:0031965; C:nuclear membrane; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW. DR GO; GO:0043195; C:terminal bouton; IEA:Ensembl. DR GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl. DR GO; GO:0019828; F:aspartic-type endopeptidase inhibitor activity; IEA:Ensembl. DR GO; GO:1903135; F:cupric ion binding; IEA:Ensembl. DR GO; GO:1903136; F:cuprous ion binding; IEA:Ensembl. DR GO; GO:0005539; F:glycosaminoglycan binding; IEA:Ensembl. DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl. DR GO; GO:0008017; F:microtubule binding; IEA:Ensembl. DR GO; GO:0140693; F:molecular condensate scaffold activity; IEA:Ensembl. DR GO; GO:0140677; F:molecular function activator activity; IEA:Ensembl. DR GO; GO:0002020; F:protease binding; IEA:Ensembl. DR GO; GO:0140311; F:protein sequestering activity; IEA:Ensembl. DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl. DR GO; GO:0038023; F:signaling receptor activity; IEA:Ensembl. DR GO; GO:0031802; F:type 5 metabotropic glutamate receptor binding; IEA:Ensembl. DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; IEA:Ensembl. DR GO; GO:1904646; P:cellular response to amyloid-beta; IEA:Ensembl. DR GO; GO:0071280; P:cellular response to copper ion; IEA:Ensembl. DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl. DR GO; GO:0007611; P:learning or memory; IEA:Ensembl. DR GO; GO:0046007; P:negative regulation of activated T cell proliferation; IEA:Ensembl. DR GO; GO:1902430; P:negative regulation of amyloid-beta formation; IEA:Ensembl. DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl. DR GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; IEA:Ensembl. DR GO; GO:1902951; P:negative regulation of dendritic spine maintenance; IEA:Ensembl. DR GO; GO:0032700; P:negative regulation of interleukin-17 production; IEA:Ensembl. DR GO; GO:0032703; P:negative regulation of interleukin-2 production; IEA:Ensembl. DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl. DR GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; IEA:Ensembl. DR GO; GO:0032689; P:negative regulation of type II interferon production; IEA:Ensembl. DR GO; GO:1990535; P:neuron projection maintenance; IEA:Ensembl. DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl. DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl. DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IEA:Ensembl. DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; IEA:Ensembl. DR GO; GO:0031648; P:protein destabilization; IEA:Ensembl. DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro. DR GO; GO:1905664; P:regulation of calcium ion import across plasma membrane; IEA:Ensembl. DR GO; GO:1900449; P:regulation of glutamate receptor signaling pathway; IEA:Ensembl. DR GO; GO:1901379; P:regulation of potassium ion transmembrane transport; IEA:Ensembl. DR GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl. DR Gene3D; 1.10.790.10; Prion/Doppel protein, beta-ribbon domain; 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 PANTHER; PTHR15506; DOPPEL PRION; 1. DR PANTHER; PTHR15506:SF2; MAJOR PRION PROTEIN; 1. DR Pfam; PF00377; Prion; 1. DR Pfam; PF11587; Prion_bPrPp; 1. DR PRINTS; PR00341; PRION. DR SMART; SM00157; PRP; 1. DR SUPFAM; SSF54098; Prion-like; 1. DR PROSITE; PS00291; PRION_1; 1. DR PROSITE; PS00706; PRION_2; 1. PE 3: Inferred from homology; KW Amyloid {ECO:0000256|ARBA:ARBA00023087}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, KW ECO:0000256|RuleBase:RU003882}; Copper {ECO:0000256|ARBA:ARBA00023008}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034}; KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622}; KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU003882}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Prion {ECO:0000256|ARBA:ARBA00022678, ECO:0000256|RuleBase:RU003882}; KW Reference proteome {ECO:0000313|Proteomes:UP000001595}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}. FT SIGNAL 1..22 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 23..253 FT /note="Major prion protein" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5014565264" FT TRANSMEM 112..131 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 232..252 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 113..128 FT /note="Prion/Doppel protein beta-ribbon" FT /evidence="ECO:0000259|PROSITE:PS00291" FT DOMAIN 200..218 FT /note="Prion/Doppel protein beta-ribbon" FT /evidence="ECO:0000259|PROSITE:PS00706" FT REGION 25..108 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 253 AA; 27680 MW; A8D0E6972F1D5B26 CRC64; MANLGCWMLV LFVATWSNLG LCKKRPKPGG WNTGGSRYPG QGSPGGNRYP PQGGGGWGQP HGGGWGQPHG GGWGQPHGGG WGQPHGGGWG QGGGTHSQWN KPSKPKTNMK HMAGAAAAGA VVGGLGGYML GSAMSRPIIH FGNDYEDRYY RENMYRYPNQ VYYRPVDQYS NQNNFVHDCV NITIKQHTVT TTTKGENFTE TDVKMMERVV EQMCITQYER ESQAYYQRGS SMVLFSSPPV ILLISFLIFL IVG //