PRND_BOVIN
ID PRND_BOVIN Reviewed; 178 AA.
AC Q9GK16; A2VDR5; Q27H90; Q29TT4; Q9MYW2;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Prion-like protein doppel;
DE AltName: Full=PrPLP;
DE Flags: Precursor;
GN Name=PRND; Synonyms=DPL;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=11331946; DOI=10.1007/s003350010285;
RA Tranulis M.A., Espenes A., Comincini S., Skretting G., Harbitz I.;
RT "The PrP-like protein Doppel gene in sheep and cattle: cDNA sequence and
RT expression.";
RL Mamm. Genome 12:376-379(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11641722; DOI=10.1007/s00335-001-2064-4;
RA Comincini S., Foti M.G., Tranulis M.A., Hills D., Di Guardo G., Vaccari G.,
RA Williams J.L., Harbitz I., Ferretti L.;
RT "Genomic organization, comparative analysis, and genetic polymorphisms of
RT the bovine and ovine prion Doppel genes (PRND).";
RL Mamm. Genome 12:729-733(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-132.
RC STRAIN=Korean;
RX PubMed=16460908; DOI=10.1016/j.ygeno.2005.12.012;
RA Choi S.-H., Kim I.-C., Kim D.-S., Kim D.-W., Chae S.-H., Choi H.-H.,
RA Choi I., Yeo J.-S., Song M.-N., Park H.-S.;
RT "Comparative genomic organization of the human and bovine PRNP locus.";
RL Genomics 87:598-607(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-132.
RA Zhang J., Liu Y., Chen H., Jiang H., Lu W., Zhu X., Xie Q., Cai X., Liu X.;
RT "Analysis and comparison of bovine, ovine and human doppel gene Prnd.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-132.
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-149.
RA Tranulis M.A., Brundtland E., Harbitz I.;
RT "Partial sequence of the bovine prion protein-like protein (doppel) gene
RT (Prnd).";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for normal acrosome reaction and for normal male
CC fertility (By similarity). Can bind Cu(2+) (By similarity).
CC {ECO:0000250|UniProtKB:Q9QUG3, ECO:0000250|UniProtKB:Q9UKY0}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9QUG3};
CC Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q9QUG3}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in testis. Detected at low
CC levels in ovary, spleen, kidney and mammary gland.
CC {ECO:0000269|PubMed:11331946}.
CC -!- DOMAIN: A short helical region is required and sufficient for Cu(2+)
CC binding. {ECO:0000250|UniProtKB:Q9UKY0}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9QUG3}.
CC -!- PTM: O-glycosylated. {ECO:0000250|UniProtKB:Q9UKY0}.
CC -!- SIMILARITY: Belongs to the prion family. {ECO:0000305}.
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DR EMBL; AJ278011; CAC22320.1; -; mRNA.
DR EMBL; DQ205538; AAK08629.1; -; Genomic_DNA.
DR EMBL; AY944236; AAY21625.1; -; Genomic_DNA.
DR EMBL; DQ408532; ABD63005.1; -; Genomic_DNA.
DR EMBL; BC133367; AAI33368.1; -; mRNA.
DR EMBL; AJ251332; CAB96195.1; -; Genomic_DNA.
DR RefSeq; NP_776583.1; NM_174158.2.
DR AlphaFoldDB; Q9GK16; -.
DR SMR; Q9GK16; -.
DR STRING; 9913.ENSBTAP00000014624; -.
DR PaxDb; Q9GK16; -.
DR GeneID; 281426; -.
DR KEGG; bta:281426; -.
DR CTD; 23627; -.
DR eggNOG; ENOG502RAT9; Eukaryota.
DR InParanoid; Q9GK16; -.
DR OrthoDB; 1431300at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR GO; GO:0007340; P:acrosome reaction; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR Gene3D; 1.10.790.10; -; 1.
DR InterPro; IPR021566; Doppel.
DR InterPro; IPR036924; Prion/Doppel_b-ribbon_dom_sf.
DR InterPro; IPR022416; Prion/Doppel_prot_b-ribbon_dom.
DR Pfam; PF11466; Doppel; 1.
DR Pfam; PF00377; Prion; 1.
DR SUPFAM; SSF54098; SSF54098; 1.
PE 2: Evidence at transcript level;
KW Amyloid; Cell membrane; Copper; Disulfide bond; Fertilization;
KW Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Metal-binding; Prion;
KW Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000250|UniProtKB:Q9UKY0"
FT CHAIN 26..154
FT /note="Prion-like protein doppel"
FT /id="PRO_0000025743"
FT PROPEP 155..178
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025744"
FT REGION 27..50
FT /note="Flexible tail"
FT /evidence="ECO:0000250"
FT REGION 51..154
FT /note="Globular"
FT /evidence="ECO:0000250"
FT REGION 124..141
FT /note="Cu(2+) binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UKY0"
FT LIPID 154
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 94..147
FT /evidence="ECO:0000250|UniProtKB:Q9QUG3"
FT DISULFID 108..142
FT /evidence="ECO:0000250|UniProtKB:Q9QUG3"
FT VARIANT 132
FT /note="R -> Q (in strain: Korean)"
FT /evidence="ECO:0000269|PubMed:16460908, ECO:0000269|Ref.4,
FT ECO:0000269|Ref.5"
FT CONFLICT 50
FT /note="R -> H (in Ref. 4; ABD63005)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="H -> Q (in Ref. 4; ABD63005)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 178 AA; 20699 MW; A209557B233AC824 CRC64;
MRKHLGGCWL AIVCILLFSQ LCSVKARGIK HRIKWNRKVL PSTSQVTEAR TAEIRPGAFI
KQGRKLDIDF GVEGNRYYEA NYWQFPDGIH YNGCSKANVT KEKFITSCIN ATQAANQEEL
SREKQDNKLY QRVLWQLIRE LCSTKHCDFW LERGAGLRVT LDQPMMLCLL VFIWFIVK
