PRIO_CHICK
ID PRIO_CHICK Reviewed; 273 AA.
AC P27177;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Major prion protein homolog;
DE AltName: Full=65-21 protein;
DE AltName: Full=Acetylcholine receptor-inducing activity;
DE Short=ARIA;
DE AltName: Full=PR-LP;
DE Flags: Precursor;
GN Name=PRNP; Synonyms=PRN-P;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1409608; DOI=10.1073/pnas.89.19.9097;
RA Gabriel J.M., Oesch B., Kretzschmar H., Scott M., Prusiner S.B.;
RT "Molecular cloning of a candidate chicken prion protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:9097-9101(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 25-51.
RC TISSUE=Brain;
RX PubMed=1715573; DOI=10.1073/pnas.88.17.7664;
RA Harris D.A., Falls D.L., Johnson F.A., Fischbach G.D.;
RT "A prion-like protein from chicken brain copurifies with an acetylcholine
RT receptor-inducing activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:7664-7668(1991).
RN [3]
RP REVIEW.
RX PubMed=2132829; DOI=10.1101/sqb.1990.055.01.040;
RA Falls D.L., Harris D.A., Johnson F.A., Morgan M.M., Corfas G.,
RA Fischbach G.D.;
RT "Mr 42,000 ARIA: a protein that may regulate the accumulation of
RT acetylcholine receptors at developing chick neuromuscular junctions.";
RL Cold Spring Harb. Symp. Quant. Biol. 55:397-406(1990).
RN [4]
RP STRUCTURE BY NMR OF 134-248.
RX PubMed=15647366; DOI=10.1073/pnas.0408939102;
RA Calzolai L., Lysek D.A., Perez D.R., Guentert P., Wuethrich K.;
RT "Prion protein NMR structures of chickens, turtles, and frogs.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:651-655(2005).
CC -!- FUNCTION: Its primary physiological function is unclear. Has
CC cytoprotective activity against internal or environmental stresses. May
CC play a role in neuronal development and synaptic plasticity. May be
CC required for neuronal myelin sheath maintenance. 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).
CC Association with GPC1 (via its heparan sulfate chains) targets PRNP to
CC lipid rafts. Also provides Cu(2+) or Zn(2+) for the ascorbate-mediated
CC GPC1 deaminase degradation of its heparan sulfate side chains (By
CC 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. {ECO:0000250|UniProtKB:P04156,
CC ECO:0000250|UniProtKB:P04925}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- TISSUE SPECIFICITY: Spinal cord and brain.
CC -!- SIMILARITY: Belongs to the prion family. {ECO:0000305}.
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DR EMBL; M95404; AAC28970.1; -; Genomic_DNA.
DR EMBL; M61145; AAA49041.1; -; mRNA.
DR PIR; A37372; A37372.
DR PIR; A41280; UJCH.
DR PIR; A46280; A46280.
DR RefSeq; NP_990796.2; NM_205465.2.
DR RefSeq; XP_015152786.1; XM_015297300.1.
DR PDB; 1U3M; NMR; -; A=134-248.
DR PDBsum; 1U3M; -.
DR AlphaFoldDB; P27177; -.
DR SMR; P27177; -.
DR STRING; 9031.ENSGALP00000040285; -.
DR PaxDb; P27177; -.
DR Ensembl; ENSGALT00000000277; ENSGALP00000040285; ENSGALG00000000209.
DR GeneID; 396452; -.
DR KEGG; gga:396452; -.
DR CTD; 5621; -.
DR VEuPathDB; HostDB:geneid_396452; -.
DR eggNOG; ENOG502S2A8; Eukaryota.
DR GeneTree; ENSGT00510000049083; -.
DR HOGENOM; CLU_094631_0_0_1; -.
DR InParanoid; P27177; -.
DR OMA; HNPGYPH; -.
DR OrthoDB; 1403854at2759; -.
DR PhylomeDB; P27177; -.
DR TreeFam; TF105188; -.
DR Reactome; R-GGA-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR EvolutionaryTrace; P27177; -.
DR PRO; PR:P27177; -.
DR Proteomes; UP000000539; Chromosome 22.
DR Bgee; ENSGALG00000000209; Expressed in cerebellum and 11 other tissues.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005604; C:basement membrane; IDA:AgBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043083; C:synaptic cleft; IDA:AgBase.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:AgBase.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:AgBase.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:0098737; P:protein insertion into plasma membrane; IDA:AgBase.
DR DisProt; DP01663; -.
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 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; GPI-anchor; Lipoprotein; Membrane;
KW Metal-binding; Prion; Reference proteome; Repeat; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:1715573"
FT CHAIN 25..248
FT /note="Major prion protein homolog"
FT /id="PRO_0000025741"
FT PROPEP 249..273
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000025742"
FT REPEAT 42..47
FT /note="1"
FT REPEAT 48..53
FT /note="2"
FT REPEAT 54..59
FT /note="3"
FT REPEAT 60..65
FT /note="4"
FT REPEAT 66..71
FT /note="5"
FT REPEAT 72..77
FT /note="6"
FT REPEAT 78..83
FT /note="7"
FT REPEAT 84..89
FT /note="8"
FT REGION 25..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..89
FT /note="8 X 6 AA tandem repeats of [HR]-[NQ]-P-G-Y-P"
FT COMPBIAS 49..90
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 66
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04156"
FT BINDING 72
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04156"
FT BINDING 78
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="4"
FT /evidence="ECO:0000250|UniProtKB:P04156"
FT BINDING 93
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P04156"
FT LIPID 248
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000250|UniProtKB:P04273"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 192..237
FT CONFLICT 78..83
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="S -> R (in Ref. 2; AAA49041)"
FT /evidence="ECO:0000305"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:1U3M"
FT HELIX 157..167
FT /evidence="ECO:0007829|PDB:1U3M"
FT HELIX 185..200
FT /evidence="ECO:0007829|PDB:1U3M"
FT HELIX 219..246
FT /evidence="ECO:0007829|PDB:1U3M"
SQ SEQUENCE 273 AA; 29909 MW; 32D700918E787DD2 CRC64;
MARLLTTCCL LALLLAACTD VALSKKGKGK PSGGGWGAGS HRQPSYPRQP GYPHNPGYPH
NPGYPHNPGY PHNPGYPHNP GYPQNPGYPH NPGYPGWGQG YNPSSGGSYH NQKPWKPPKT
NFKHVAGAAA AGAVVGGLGG YAMGRVMSGM NYHFDSPDEY RWWSENSARY PNRVYYRDYS
SPVPQDVFVA DCFNITVTEY SIGPAAKKNT SEAVAAANQT EVEMENKVVT KVIREMCVQQ
YREYRLASGI QLHPADTWLA VLLLLLTTLF AMH
