ID   APRIO_HUMAN             Reviewed;          73 AA.
AC   F7VJQ1;
DT   28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Alternative prion protein;
DE   AltName: Full=AltPrP;
GN   Name=PRNP; Synonyms=ALTPRP, PRIP, PRP;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [2]
RP   IDENTIFICATION, SUBCELLULAR LOCATION, INDUCTION, AND TISSUE SPECIFICITY.
RX   PubMed=21478263; DOI=10.1096/fj.10-173815;
RA   Vanderperre B., Staskevicius A.B., Tremblay G., McCoy M., O'Neill M.A.,
RA   Cashman N.R., Roucou X.;
RT   "An overlapping reading frame in the PRNP gene encodes a novel polypeptide
RT   distinct from the prion protein.";
RL   FASEB J. 25:2373-2386(2011).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000269|PubMed:21478263}; Single-pass membrane protein
CC       {ECO:0000269|PubMed:21478263}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=3; Synonyms=AltPrP;
CC         IsoId=F7VJQ1-1; Sequence=Displayed;
CC       Name=1; Synonyms=PrP;
CC         IsoId=P04156-1; Sequence=External;
CC   -!- TISSUE SPECIFICITY: Detected in brain homogenate, primary neurons, and
CC       peripheral blood mononuclear cells (at protein level).
CC       {ECO:0000269|PubMed:21478263}.
CC   -!- INDUCTION: Up-regulated by endoplasmic reticulum stress and proteasomal
CC       inhibition. {ECO:0000269|PubMed:21478263}.
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. {ECO:0000305|PubMed:21478263}.
CC   -!- MISCELLANEOUS: The alternative prion protein/AltPrP and PRNP (AC
CC       P04156) have no apparent direct functional relation since a mutation
CC       that removes the start codon of the AltPrP has no apparent effect on
CC       the biology of PRNP. In mouse and hamster, the alternative initiation
CC       AUG codon is absent and is replaced by a GUG codon (PubMed:21478263).
CC       {ECO:0000305|PubMed:21478263}.
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DR   EMBL; AL133396; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BK007887; DAA34790.1; -; Genomic_DNA.
DR   RefSeq; NP_001258490.1; NM_001271561.2. [F7VJQ1-1]
DR   AlphaFoldDB; F7VJQ1; -.
DR   BioGRID; 111606; 443.
DR   DrugBank; DB09130; Copper.
DR   SwissPalm; F7VJQ1; -.
DR   BioMuta; PRNP; -.
DR   PRIDE; F7VJQ1; -.
DR   DNASU; 5621; -.
DR   GeneID; 5621; -.
DR   CTD; 5621; -.
DR   DisGeNET; 5621; -.
DR   GeneCards; PRNP; -.
DR   GeneReviews; PRNP; -.
DR   HGNC; HGNC:9449; PRNP.
DR   MalaCards; PRNP; -.
DR   neXtProt; NX_F7VJQ1; -.
DR   PathwayCommons; F7VJQ1; -.
DR   SignaLink; F7VJQ1; -.
DR   SIGNOR; F7VJQ1; -.
DR   BioGRID-ORCS; 5621; 10 hits in 1089 CRISPR screens.
DR   ChiTaRS; PRNP; human.
DR   GeneWiki; PRNP; -.
DR   GenomeRNAi; 5621; -.
DR   Pharos; F7VJQ1; Tbio.
DR   Proteomes; UP000005640; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Alternative initiation; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..73
FT                   /note="Alternative prion protein"
FT                   /id="PRO_0000420424"
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   73 AA;  8691 MW;  4360C28341A4CA52 CRC64;
     MEHWGQPIPG AGQPWRQPLP TSGRWWLGAA SWWWLGAASW WWLGAAPWWW LGTASWWWLG
     SRRWHPQSVE QAE