ID   LRC25_BOVIN             Reviewed;         307 AA.
AC   Q8MII8;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   02-JUN-2021, entry version 88.
DE   RecName: Full=Leucine-rich repeat-containing protein 25;
DE   AltName: Full=Monocyte and plasmacytoid-activated protein;
DE   Flags: Precursor;
GN   Name=LRRC25; Synonyms=MAPA;
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].
RC   TISSUE=Plasmacytoid dendritic cell;
RX   PubMed=12384430; DOI=10.1182/blood-2002-02-0638;
RA   Rissoan M.-C., Duhen T., Bridon J.-M., Bendriss-Vermare N., Peronne C.,
RA   de Saint-Vis B.M., Briere F., Bates E.E.M.;
RT   "Subtractive hybridization reveals the expression of immunoglobulin like
RT   transcript 7, Eph-B1, granzyme B, and 3 novel transcripts in human
RT   plasmacytoid dendritic cells.";
RL   Blood 100:3295-3303(2002).
CC   -!- FUNCTION: Plays a role in the inhibition of RLR-mediated type I
CC       interferon signaling pathway by targeting DDX58/RIG-I for autophagic
CC       degradation. Interacts specifically with ISG15-associated DDX58 to
CC       promote interaction between DDX58 and the autophagic cargo receptor
CC       p62/SQSTM1 to mediate DDX58 degradation via selective autophagy. Plays
CC       also a role in the inhibition of NF-kappa-B signaling pathway and
CC       inflammatory response by promoting the degradation of p65/RELA.
CC       {ECO:0000250|UniProtKB:Q8N386}.
CC   -!- SUBUNIT: Interacts with DDX58. Interacts with SQSTM1. Interacts with
CC       p65/RELA; this interaction promotes the degradation of RELA through
CC       autophagy. {ECO:0000250|UniProtKB:Q8N386}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8N386}; Single-
CC       pass type I membrane protein {ECO:0000250|UniProtKB:Q8N386}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q8N386}.
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DR   EMBL; AJ422150; CAD19533.1; -; mRNA.
DR   STRING; 9913.ENSBTAP00000022955; -.
DR   PaxDb; Q8MII8; -.
DR   eggNOG; ENOG502S9V5; Eukaryota.
DR   InParanoid; Q8MII8; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR039243; LRRC25.
DR   PANTHER; PTHR20878; PTHR20878; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Glycoprotein; Leucine-rich repeat; Membrane; Phosphoprotein;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..307
FT                   /note="Leucine-rich repeat-containing protein 25"
FT                   /id="PRO_0000021612"
FT   TOPO_DOM        21..168
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        190..307
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          63..86
FT                   /note="LRR 1"
FT   REPEAT          87..110
FT                   /note="LRR 2"
FT   REGION          205..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..242
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         286
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K1T1"
FT   CARBOHYD        44
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        56
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        95
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        132
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        151
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   307 AA;  33934 MW;  FE7F8BEED1A64FFE CRC64;
     MGGPLMWALL LPLLLHQAGS QTSSCSVLSG YMDWTKEYFD TCLNFSGKIL TQLPQNQSLR
     ARSVQLLDLS ANGLQRLPWS FFRDLEQLQL LIVTNNSLDF VDRALXXXGC GLELLADCSC
     ALLDWHTDRQ DNCSGPELPR CLDVPTGAWH NLSVFLDVSC PSGLTKIAIG ALAASGSLLL
     VLAIAGPVLA WRFCRHRMDQ NLSKTWASQD GSRSGSGRQP RYSSQGRRPK SPANTPPRSS
     TPDYENVFVG PPAARHQWDE LRSPPSEGGD FYMTYDSLQH ESQPVYCNLQ SLSQVPLDDE
     EYVVPGR