LRC25_MOUSE
ID LRC25_MOUSE Reviewed; 297 AA.
AC Q8K1T1; Q3TAD5;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 124.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Aorta, Spleen, and Vein;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-289, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211; SER-238; SER-267 AND
RP TYR-289, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; AJ422149; CAD19532.1; -; mRNA.
DR EMBL; AK080022; BAC37807.1; -; mRNA.
DR EMBL; AK171924; BAE42733.1; -; mRNA.
DR CCDS; CCDS22375.1; -.
DR RefSeq; NP_694714.1; NM_153074.3.
DR AlphaFoldDB; Q8K1T1; -.
DR STRING; 10090.ENSMUSP00000049686; -.
DR GlyGen; Q8K1T1; 4 sites.
DR iPTMnet; Q8K1T1; -.
DR PhosphoSitePlus; Q8K1T1; -.
DR jPOST; Q8K1T1; -.
DR MaxQB; Q8K1T1; -.
DR PaxDb; Q8K1T1; -.
DR PRIDE; Q8K1T1; -.
DR ProteomicsDB; 287264; -.
DR Antibodypedia; 28033; 346 antibodies from 19 providers.
DR Ensembl; ENSMUST00000052437; ENSMUSP00000049686; ENSMUSG00000049988.
DR GeneID; 211228; -.
DR KEGG; mmu:211228; -.
DR UCSC; uc009maz.1; mouse.
DR CTD; 126364; -.
DR MGI; MGI:2445284; Lrrc25.
DR VEuPathDB; HostDB:ENSMUSG00000049988; -.
DR eggNOG; ENOG502S9V5; Eukaryota.
DR GeneTree; ENSGT00390000004001; -.
DR HOGENOM; CLU_906014_0_0_1; -.
DR InParanoid; Q8K1T1; -.
DR OMA; WHNVSAF; -.
DR OrthoDB; 1374271at2759; -.
DR PhylomeDB; Q8K1T1; -.
DR TreeFam; TF337414; -.
DR BioGRID-ORCS; 211228; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q8K1T1; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8K1T1; protein.
DR Bgee; ENSMUSG00000049988; Expressed in granulocyte and 46 other tissues.
DR ExpressionAtlas; Q8K1T1; baseline and differential.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR039243; LRRC25.
DR PANTHER; PTHR20878; PTHR20878; 1.
DR Pfam; PF13855; LRR_8; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Glycoprotein; Leucine-rich repeat; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..297
FT /note="Leucine-rich repeat-containing protein 25"
FT /id="PRO_0000021614"
FT TOPO_DOM 26..169
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 66..89
FT /note="LRR 1"
FT REPEAT 90..113
FT /note="LRR 2"
FT REGION 202..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 289
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660,
FT ECO:0007744|PubMed:19144319"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 297 AA; 32673 MW; 3DFB43C8D547CD2B CRC64;
MGSIRTRLLW LCLLMLLALL HKSGSQDLTC MVHPSRVDWT QTFNGTCLNF SGLGLSLPRS
PLQASHAQVL DLSKNGLQVL PGAFFDKLEK LQTLIVTHNQ LDSVDRSLAL RCDLELKADC
SCGLASWYAL RQNCSGQQQL LCLHPATEAP RNLSTFLQVS CPPSWGPGTI GALVAGTISL
AVAVSGSVLA WRLLRRRRRA SEHSLSKAQM SPHDIPKPVT DFLPRYSSRR PGPKAPDSPP
SRFTMDYENV FIGQPAEDCS WSAARNSPSG DSDCYMNYRS VDQDSQPVYC NLESLGR
