PRND_SHEEP
ID PRND_SHEEP Reviewed; 178 AA.
AC Q9GJY2; Q9MYU2;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Prion-like protein doppel;
DE AltName: Full=PrPLP;
DE Flags: Precursor;
GN Name=PRND;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / 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 / MRNA].
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].
RA Essalmani R., Taourit S., Besnard N., Vilotte J.-L.;
RT "Sequence and expression in transgenic mice of the ovine doppel-encoding
RT gene.";
RL Submitted (JUN-2001) 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 lymph node, spleen and ovary. {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; AJ278010; CAC22340.1; -; mRNA.
DR EMBL; AJ251331; CAB96388.1; -; Genomic_DNA.
DR EMBL; AY017311; AAK08630.1; -; Genomic_DNA.
DR EMBL; AF394223; AAK77164.1; -; Genomic_DNA.
DR RefSeq; NP_001009261.1; NM_001009261.1.
DR PDB; 2M1J; NMR; -; A=1-30.
DR PDBsum; 2M1J; -.
DR AlphaFoldDB; Q9GJY2; -.
DR BMRB; Q9GJY2; -.
DR SMR; Q9GJY2; -.
DR STRING; 9940.ENSOARP00000005010; -.
DR Ensembl; ENSOART00000005095; ENSOARP00000005010; ENSOARG00000004683.
DR Ensembl; ENSOART00020017909; ENSOARP00020014793; ENSOARG00020011760.
DR GeneID; 443194; -.
DR KEGG; oas:443194; -.
DR CTD; 23627; -.
DR eggNOG; ENOG502RAT9; Eukaryota.
DR HOGENOM; CLU_1524583_0_0_1; -.
DR OMA; DGIHYDG; -.
DR OrthoDB; 1431300at2759; -.
DR Proteomes; UP000002356; Chromosome 13.
DR Bgee; ENSOARG00000004683; Expressed in testis and 40 other tissues.
DR ExpressionAtlas; Q9GJY2; baseline.
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 1: Evidence at protein level;
KW 3D-structure; Amyloid; Cell membrane; Copper; Disulfide bond;
KW Fertilization; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Metal-binding; Prion; 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_0000025749"
FT PROPEP 155..178
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025750"
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 HELIX 10..22
FT /evidence="ECO:0007829|PDB:2M1J"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:2M1J"
SQ SEQUENCE 178 AA; 20648 MW; B978750CE0F4D5D4 CRC64;
MRKHLGGCWL AIVCVLLFSQ LSSVKARGIK HRIKWNRKVL PSTSQVTEAH TAEIRPGAFI
KQGRKLDINF GVEGNRYYEA NYWQFPDGIH YNGCSEANVT KEKFVTSCIN ATQVANQEEL
SREKQDNKLY QRVLWQLIRE LCSIKHCDFW LERGAGLQVT LDQPMMLCLL VFIWFIVK
