LRC19_HUMAN
ID LRC19_HUMAN Reviewed; 370 AA.
AC Q9H756; A0AV00; B9EG91;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Leucine-rich repeat-containing protein 19 {ECO:0000305};
DE Flags: Precursor;
GN Name=LRRC19 {ECO:0000312|HGNC:HGNC:23379};
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 MRNA].
RC TISSUE=Colon;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, AND ACTIVITY REGULATION.
RX PubMed=19679103; DOI=10.1016/j.bbrc.2009.08.043;
RA Chai L., Dai L., Che Y., Xu J., Liu G., Zhang Z., Yang R.;
RT "LRRC19, a novel member of the leucine-rich repeat protein family,
RT activates NF-kappaB and induces expression of proinflammatory cytokines.";
RL Biochem. Biophys. Res. Commun. 388:543-548(2009).
RN [4]
RP TISSUE SPECIFICITY, AND INTERACTION WITH TRAF2 AND TRAF6.
RX PubMed=25026888; DOI=10.1038/ncomms5434;
RA Su X., Min S., Cao S., Yan H., Zhao Y., Li H., Chai L., Mei S., Yang J.,
RA Zhang Y., Zhang Z., Liu F., Sun W., Che Y., Yang R.;
RT "LRRC19 expressed in the kidney induces TRAF2/6-mediated signals to prevent
RT infection by uropathogenic bacteria.";
RL Nat. Commun. 5:4434-4434(2014).
CC -!- FUNCTION: Pathogen-recognition receptor which mediates the activation
CC of TRAF2- and TRAF6 NF-kappa-B signaling pathways and induces the
CC expression of pro-inflammatory cytokines (PubMed:19679103,
CC PubMed:25026888). In kidney, prevents infection by uropathogenic
CC bacteria by inducing the production of cytokines, chemokines and
CC antimicrobial substances. In gut, involved in host-microbiota
CC interactions, plays a critical role in promoting the recruitment of
CC immune cells and intestinal inflammation (By similarity).
CC {ECO:0000250|UniProtKB:Q8BZT5, ECO:0000269|PubMed:19679103,
CC ECO:0000269|PubMed:25026888}.
CC -!- ACTIVITY REGULATION: Activated by TLR ligands such as LPS, bacterial
CC DNA and peptidoglycan. {ECO:0000250|UniProtKB:Q8BZT5}.
CC -!- SUBUNIT: Interacts with TRAF2 and TRAF6. {ECO:0000269|PubMed:25026888}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in renal collecting duct epithelial
CC cells. {ECO:0000269|PubMed:25026888}.
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DR EMBL; AK024955; BAB15042.1; -; mRNA.
DR EMBL; BC126156; AAI26157.1; -; mRNA.
DR EMBL; BC136298; AAI36299.1; -; mRNA.
DR CCDS; CCDS6518.1; -.
DR RefSeq; NP_075052.1; NM_022901.2.
DR AlphaFoldDB; Q9H756; -.
DR SMR; Q9H756; -.
DR STRING; 9606.ENSP00000369395; -.
DR GlyGen; Q9H756; 10 sites.
DR iPTMnet; Q9H756; -.
DR PhosphoSitePlus; Q9H756; -.
DR BioMuta; LRRC19; -.
DR DMDM; 51701695; -.
DR jPOST; Q9H756; -.
DR MassIVE; Q9H756; -.
DR PaxDb; Q9H756; -.
DR PeptideAtlas; Q9H756; -.
DR PRIDE; Q9H756; -.
DR ProteomicsDB; 81081; -.
DR Antibodypedia; 2688; 145 antibodies from 24 providers.
DR DNASU; 64922; -.
DR Ensembl; ENST00000380055.6; ENSP00000369395.5; ENSG00000184434.8.
DR GeneID; 64922; -.
DR KEGG; hsa:64922; -.
DR MANE-Select; ENST00000380055.6; ENSP00000369395.5; NM_022901.3; NP_075052.1.
DR UCSC; uc003zqh.4; human.
DR CTD; 64922; -.
DR GeneCards; LRRC19; -.
DR HGNC; HGNC:23379; LRRC19.
DR HPA; ENSG00000184434; Group enriched (intestine, kidney).
DR MalaCards; LRRC19; -.
DR MIM; 619068; gene.
DR neXtProt; NX_Q9H756; -.
DR OpenTargets; ENSG00000184434; -.
DR PharmGKB; PA134892454; -.
DR VEuPathDB; HostDB:ENSG00000184434; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000161278; -.
DR HOGENOM; CLU_063696_1_0_1; -.
DR InParanoid; Q9H756; -.
DR OMA; EVKCNFT; -.
DR OrthoDB; 622935at2759; -.
DR PhylomeDB; Q9H756; -.
DR TreeFam; TF335466; -.
DR PathwayCommons; Q9H756; -.
DR BioGRID-ORCS; 64922; 6 hits in 1016 CRISPR screens.
DR GenomeRNAi; 64922; -.
DR Pharos; Q9H756; Tbio.
DR PRO; PR:Q9H756; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9H756; protein.
DR Bgee; ENSG00000184434; Expressed in jejunal mucosa and 78 other tissues.
DR Genevisible; Q9H756; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0048874; P:host-mediated regulation of intestinal microbiota composition; ISS:UniProtKB.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IDA:MGI.
DR GO; GO:0001817; P:regulation of cytokine production; ISS:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0002224; P:toll-like receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0038008; P:TRAF-mediated signal transduction; ISS:UniProtKB.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR039489; LRRC19.
DR PANTHER; PTHR31450:SF4; PTHR31450:SF4; 1.
DR Pfam; PF13855; LRR_8; 1.
DR SMART; SM00369; LRR_TYP; 4.
DR SMART; SM00082; LRRCT; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Leucine-rich repeat; Membrane; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..370
FT /note="Leucine-rich repeat-containing protein 19"
FT /id="PRO_0000021610"
FT TOPO_DOM 25..270
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..370
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 46..71
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 72..95
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 96..119
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 120..143
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 145..168
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT DOMAIN 176..227
FT /note="LRRCT"
FT /evidence="ECO:0000255"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 62
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 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 370 AA; 42334 MW; 9B59E08CF766E902 CRC64;
MKVTGITILF WPLSMILLSD KIQSSKREVQ CNFTEKNYTL IPADIKKDVT ILDLSYNQIT
LNGTDTRVLQ TYFLLTELYL IENKVTILHN NGFGNLSSLE ILNICRNSIY VIQQGAFLGL
NKLKQLYLCQ NKIEQLNADV FVPLRSLKLL NLQGNLISYL DVPPLFHLEL ITLYGNLWNC
SCSLFNLQNW LNTSNVTLEN ENITMCSYPN SLQSYNIKTV PHKAECHSKF PSSVTEDLYI
HFQPISNSIF NSSSNNLTRN SEHEPLGKSW AFLVGVVVTV LTTSLLIFIA IKCPIWYNIL
LSYNHHRLEE HEAETYEDGF TGNPSSLSQI PETNSEETTV IFEQLHSFVV DDDGFIEDKY
IDIHELCEEN
