INAVA_HUMAN
ID INAVA_HUMAN Reviewed; 663 AA.
AC Q3KP66; B4E1K9; E9PFY0; Q9NV65; Q9NVI0;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Innate immunity activator protein {ECO:0000312|HGNC:HGNC:25599};
GN Name=INAVA {ECO:0000312|HGNC:HGNC:25599}; Synonyms=C1orf106;
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] (ISOFORMS 1 AND 2), AND VARIANT
RP CYS-538.
RC TISSUE=Trachea;
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 GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT CYS-538.
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 [4]
RP INVOLVEMENT IN IBD29, AND VARIANT IBD29 PHE-333.
RX PubMed=21983784; DOI=10.1038/ng.952;
RG National Institute of Diabetes and Digestive Kidney Diseases Inflammatory Bowel Disease Genetics Consortium (NIDDK IBDGC);
RG United Kingdom Inflammatory Bowel Disease Genetics Consortium;
RA Rivas M.A., Beaudoin M., Gardet A., Stevens C., Sharma Y., Zhang C.K.,
RA Boucher G., Ripke S., Ellinghaus D., Burtt N., Fennell T., Kirby A.,
RA Latiano A., Goyette P., Green T., Halfvarson J., Haritunians T., Korn J.M.,
RA Kuruvilla F., Lagace C., Neale B., Lo K.S., Schumm P., Toerkvist L.,
RA Dubinsky M.C., Brant S.R., Silverberg M.S., Duerr R.H., Altshuler D.,
RA Gabriel S., Lettre G., Franke A., D'Amato M., McGovern D.P., Cho J.H.,
RA Rioux J.D., Xavier R.J., Daly M.J.;
RT "Deep resequencing of GWAS loci identifies independent rare variants
RT associated with inflammatory bowel disease.";
RL Nat. Genet. 43:1066-1073(2011).
RN [5]
RP FUNCTION, INVOLVEMENT IN IBD29, TISSUE SPECIFICITY, INDUCTION BY MDP AND
RP MIR-24, SUBCELLULAR LOCATION, INTERACTION WITH IRAK1; NOD2; RIPK2 AND
RP YWHAQ, AND MUTAGENESIS OF 164-PRO--ILE-170; SER-246; 335-LYS--LYS-338;
RP SER-340; 423-ARG--PRO-426 AND SER-616.
RX PubMed=28436939; DOI=10.1172/jci86282;
RA Yan J., Hedl M., Abraham C.;
RT "An inflammatory bowel disease-risk variant in INAVA decreases pattern
RT recognition receptor-induced outcomes.";
RL J. Clin. Invest. 127:2192-2205(2017).
RN [6]
RP FUNCTION, INVOLVEMENT IN IBD29, VARIANT IBD29 PHE-333, CHARACTERIZATION OF
RP VARIANT IBD29 PHE-333, TISSUE SPECIFICITY, AND INTERACTION WITH BTRC;
RP CYTH1; CYTH2 AND FBXW11.
RX PubMed=29420262; DOI=10.1126/science.aan0814;
RA Mohanan V., Nakata T., Desch A.N., Levesque C., Boroughs A., Guzman G.,
RA Cao Z., Creasey E., Yao J., Boucher G., Charron G., Bhan A.K., Schenone M.,
RA Carr S.A., Reinecker H.C., Daly M.J., Rioux J.D., Lassen K.G., Xavier R.J.;
RT "C1orf106 is a colitis risk gene that regulates stability of epithelial
RT adherens junctions.";
RL Science 359:1161-1166(2018).
CC -!- FUNCTION: Expressed in peripheral macrophages and intestinal myeloid-
CC derived cells, is required for optimal PRR (pattern recognition
CC receptor)-induced signaling, cytokine secretion, and bacterial
CC clearance. Upon stimulation of a broad range of PRRs (pattern
CC recognition receptor) such as NOD2 or TLR2, TLR3, TLR4, TLR5, TLR7 and
CC TLR9, associates with YWHAQ/14-3-3T, which in turn leads to the
CC recruitment and activation of MAP kinases and NF-kappa-B signaling
CC complexes that amplifies PRR-induced downstream signals and cytokine
CC secretion (PubMed:28436939). In the intestine, regulates adherens
CC junction stability by regulating the degradation of CYTH1 and CYTH2,
CC probably acting as substrate cofactor for SCF E3 ubiquitin-protein
CC ligase complexes. Stabilizes adherens junctions by limiting CYTH1-
CC dependent ARF6 activation (PubMed:29420262).
CC {ECO:0000269|PubMed:28436939, ECO:0000269|PubMed:29420262}.
CC -!- SUBUNIT: Interacts with IRAK1, NOD2 and RIPK2; the interaction takes
CC place upon PRR stimulation (PubMed:28436939). Interacts with YWHAQ/14-
CC 3-3T; the interaction increases upon PRR stimulation and is required
CC for cellular signaling pathway activation and cytokine secretion
CC (PubMed:28436939). Interacts (via N-terminal domain) with CYTH1 and
CC CYTH2 (via their N-terminal domains) (PubMed:29420262). Interacts with
CC FBXW11 and BTRC; associates with SCF E3 ubiquitin-protein ligase
CC complexes (PubMed:29420262). {ECO:0000269|PubMed:28436939,
CC ECO:0000269|PubMed:29420262}.
CC -!- INTERACTION:
CC Q3KP66; Q9Y297: BTRC; NbExp=2; IntAct=EBI-7545562, EBI-307461;
CC Q3KP66; Q15438: CYTH1; NbExp=6; IntAct=EBI-7545562, EBI-997830;
CC Q3KP66; Q99418: CYTH2; NbExp=2; IntAct=EBI-7545562, EBI-448974;
CC Q3KP66; Q9UKB1: FBXW11; NbExp=2; IntAct=EBI-7545562, EBI-355189;
CC Q3KP66; O95271: TNKS; NbExp=2; IntAct=EBI-7545562, EBI-1105254;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28436939}. Cytoplasm
CC {ECO:0000269|PubMed:28436939}. Note=Translocates to the nucleus upon
CC NOD2 stimulation. {ECO:0000269|PubMed:28436939}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3KP66-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3KP66-3; Sequence=VSP_046048;
CC -!- TISSUE SPECIFICITY: Highly expressed in intestinal myeloid-derived
CC cells and expressed in monocyte-derived macrophages upon induction by
CC PRR activation. {ECO:0000269|PubMed:28436939,
CC ECO:0000269|PubMed:29420262}.
CC -!- INDUCTION: Expression is induced by the component of peptidoglycan
CC muramyl dipeptide (PubMed:28436939). Negatively regulated by microRNA-
CC 24 (miR-24) (PubMed:28436939). {ECO:0000269|PubMed:28436939}.
CC -!- DISEASE: Inflammatory bowel disease 29 (IBD29) [MIM:618077]: A chronic,
CC relapsing inflammation of the gastrointestinal tract with a complex
CC etiology. It is subdivided into Crohn disease and ulcerative colitis
CC phenotypes. Crohn disease may affect any part of the gastrointestinal
CC tract from the mouth to the anus, but most frequently it involves the
CC terminal ileum and colon. Bowel inflammation is transmural and
CC discontinuous; it may contain granulomas or be associated with
CC intestinal or perianal fistulas. In contrast, in ulcerative colitis,
CC the inflammation is continuous and limited to rectal and colonic
CC mucosal layers; fistulas and granulomas are not observed. Both diseases
CC include extraintestinal inflammation of the skin, eyes, or joints.
CC {ECO:0000269|PubMed:21983784, ECO:0000269|PubMed:28436939,
CC ECO:0000269|PubMed:29420262}. Note=Disease susceptibility is associated
CC with variants affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91771.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence={ECO:0000305};
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DR EMBL; AK001583; BAA91771.1; ALT_SEQ; mRNA.
DR EMBL; AK001763; BAA91892.1; -; mRNA.
DR EMBL; AK303885; BAG64821.1; -; mRNA.
DR EMBL; AK316510; BAH14881.1; -; mRNA.
DR EMBL; AC099756; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC106877; AAI06878.1; -; mRNA.
DR CCDS; CCDS44292.1; -. [Q3KP66-3]
DR RefSeq; NP_001136041.1; NM_001142569.2. [Q3KP66-3]
DR RefSeq; NP_060735.3; NM_018265.3. [Q3KP66-1]
DR RefSeq; XP_011508056.1; XM_011509754.2. [Q3KP66-3]
DR RefSeq; XP_011508057.1; XM_011509755.1. [Q3KP66-3]
DR AlphaFoldDB; Q3KP66; -.
DR SMR; Q3KP66; -.
DR BioGRID; 120883; 72.
DR IntAct; Q3KP66; 44.
DR MINT; Q3KP66; -.
DR STRING; 9606.ENSP00000392105; -.
DR iPTMnet; Q3KP66; -.
DR PhosphoSitePlus; Q3KP66; -.
DR BioMuta; INAVA; -.
DR DMDM; 317373328; -.
DR EPD; Q3KP66; -.
DR jPOST; Q3KP66; -.
DR MassIVE; Q3KP66; -.
DR MaxQB; Q3KP66; -.
DR PaxDb; Q3KP66; -.
DR PeptideAtlas; Q3KP66; -.
DR PRIDE; Q3KP66; -.
DR ProteomicsDB; 20202; -.
DR ProteomicsDB; 61715; -. [Q3KP66-1]
DR Antibodypedia; 34491; 124 antibodies from 20 providers.
DR DNASU; 55765; -.
DR Ensembl; ENST00000367342.8; ENSP00000356311.4; ENSG00000163362.11. [Q3KP66-1]
DR Ensembl; ENST00000413687.3; ENSP00000392105.2; ENSG00000163362.11. [Q3KP66-3]
DR GeneID; 55765; -.
DR KEGG; hsa:55765; -.
DR MANE-Select; ENST00000413687.3; ENSP00000392105.2; NM_001142569.3; NP_001136041.1. [Q3KP66-3]
DR UCSC; uc010ppm.3; human. [Q3KP66-1]
DR CTD; 55765; -.
DR DisGeNET; 55765; -.
DR GeneCards; INAVA; -.
DR HGNC; HGNC:25599; INAVA.
DR HPA; ENSG00000163362; Tissue enhanced (esophagus, intestine, skin).
DR MalaCards; INAVA; -.
DR MIM; 618051; gene.
DR MIM; 618077; phenotype.
DR neXtProt; NX_Q3KP66; -.
DR OpenTargets; ENSG00000163362; -.
DR PharmGKB; PA142672490; -.
DR VEuPathDB; HostDB:ENSG00000163362; -.
DR eggNOG; KOG3529; Eukaryota.
DR GeneTree; ENSGT00940000154102; -.
DR HOGENOM; CLU_035581_0_0_1; -.
DR InParanoid; Q3KP66; -.
DR OMA; WDSWENS; -.
DR OrthoDB; 509744at2759; -.
DR PhylomeDB; Q3KP66; -.
DR TreeFam; TF328984; -.
DR PathwayCommons; Q3KP66; -.
DR SignaLink; Q3KP66; -.
DR BioGRID-ORCS; 55765; 19 hits in 1036 CRISPR screens.
DR ChiTaRS; C1orf106; human.
DR GenomeRNAi; 55765; -.
DR Pharos; Q3KP66; Tbio.
DR PRO; PR:Q3KP66; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q3KP66; protein.
DR Bgee; ENSG00000163362; Expressed in ileal mucosa and 152 other tissues.
DR ExpressionAtlas; Q3KP66; baseline and differential.
DR Genevisible; Q3KP66; HS.
DR GO; GO:0005737; C:cytoplasm; IMP:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IMP:UniProtKB.
DR GO; GO:0034334; P:adherens junction maintenance; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
DR GO; GO:0060729; P:intestinal epithelial structure maintenance; ISS:UniProtKB.
DR GO; GO:0070431; P:nucleotide-binding oligomerization domain containing 2 signaling pathway; IMP:UniProtKB.
DR GO; GO:0002221; P:pattern recognition receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0002720; P:positive regulation of cytokine production involved in immune response; IMP:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IMP:UniProtKB.
DR GO; GO:0032733; P:positive regulation of interleukin-10 production; IMP:UniProtKB.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:GO_Central.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IMP:UniProtKB.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IMP:UniProtKB.
DR GO; GO:1903409; P:reactive oxygen species biosynthetic process; IMP:UniProtKB.
DR GO; GO:0032495; P:response to muramyl dipeptide; IMP:UniProtKB.
DR GO; GO:0032494; P:response to peptidoglycan; IMP:UniProtKB.
DR InterPro; IPR043447; CCDC120/INAVA.
DR InterPro; IPR021774; DUF3338.
DR InterPro; IPR039106; INAVA.
DR PANTHER; PTHR16093; PTHR16093; 1.
DR PANTHER; PTHR16093:SF4; PTHR16093:SF4; 1.
DR Pfam; PF11819; CUPID; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Disease variant; Immunity;
KW Innate immunity; Nucleus; Reference proteome.
FT CHAIN 1..663
FT /note="Innate immunity activator protein"
FT /id="PRO_0000251729"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 118..147
FT /evidence="ECO:0000255"
FT MOTIF 164..170
FT /note="Nuclear localization signal (NLS) 1"
FT /evidence="ECO:0000269|PubMed:28436939"
FT MOTIF 332..338
FT /note="Nuclear localization signal (NLS) 2"
FT /evidence="ECO:0000269|PubMed:28436939"
FT MOTIF 422..428
FT /note="Nuclear localization signal (NLS) 3"
FT /evidence="ECO:0000269|PubMed:28436939"
FT COMPBIAS 283..299
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..85
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046048"
FT VARIANT 333
FT /note="Y -> F (in IBD29; decreases protein stability;
FT dbSNP:rs41313912)"
FT /evidence="ECO:0000269|PubMed:21983784,
FT ECO:0000269|PubMed:29420262"
FT /id="VAR_080249"
FT VARIANT 538
FT /note="R -> C (in dbSNP:rs296520)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_030835"
FT MUTAGEN 164..170
FT /note="PKVRRRI->AAAAAAA: No effect on nuclear translocation
FT upon induction by MDP. Abolishes nuclear translocation upon
FT induction by MDP and slightly decreases NOD2-induced AP-1
FT and NF-kappaB activation and IL6 secretion; when associated
FT with 335-A--A-338 and 423-A--A-426."
FT /evidence="ECO:0000269|PubMed:28436939"
FT MUTAGEN 246
FT /note="S->A: Decreases interaction with YWHAQ, cellular
FT signaling pathway activation and cytokine secretion."
FT /evidence="ECO:0000269|PubMed:28436939"
FT MUTAGEN 335..338
FT /note="KPRK->AAAA: No effect on nuclear translocation upon
FT induction by MDP. Abolishes nuclear translocation upon
FT induction by MDP and slightly decreases NOD2-induced AP-1
FT and NF-kappaB activation and IL6 secretion; when associated
FT with 164-A--A-170 and 423-A--A-426."
FT /evidence="ECO:0000269|PubMed:28436939"
FT MUTAGEN 340
FT /note="S->A: Decreases interaction with YWHAQ, cellular
FT signaling pathway activation and cytokine secretion."
FT /evidence="ECO:0000269|PubMed:28436939"
FT MUTAGEN 423..426
FT /note="RRRP->AAAA: No effect on nuclear translocation upon
FT induction by MDP. Abolishes nuclear translocation upon
FT induction by MDP and slightly decreases NOD2-induced AP-1
FT and NF-kappaB activation and IL6 secretion; when associated
FT with 164-A--A-170 and 335-A--A-338."
FT /evidence="ECO:0000269|PubMed:28436939"
FT MUTAGEN 616
FT /note="S->A: Decreases interaction with YWHAQ, cellular
FT signaling pathway activation and cytokine secretion."
FT /evidence="ECO:0000269|PubMed:28436939"
FT CONFLICT 641
FT /note="R -> W (in Ref. 1; BAA91892)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 663 AA; 72914 MW; 77EB3D76DC55EF8A CRC64;
MLQMPKLNEI PPGRAGRREA RGEGRWPGQT GPEAARLEWR AQGQAGGARA PWDSWGSSRL
PTQPGPGWSR CPPSLLCALS FQKSTMESKD EVSDTDSGII LQSGPDSPVS PMKELTHAVH
KQQRALEARL EACLEELRRL CLREAELTGT LPAEYPLKPG EKAPKVRRRI GAAYKLDDWA
LHREDPLSSL ERQLALQLQI TEAARRLCLE ENLSRQARRQ RKHSMLQEEK KLQELQRCLV
ERRRNSEPPP AAALPLGREL SASDDSSLSD GLLLEEEESQ VPKPPPESPA PPSRPLPPQT
LEGLQPTGPE AGSPERAPVQ NSPWKETSLD HPYEKPRKSS EPWSESSSPA TTPQDGPSAS
SLWLLEPASY HVVPIRGVPG QWQGRTSAPA TPEIQGRRGQ SQSLRVDSFR AGPEGRGRSA
FPRRRPTHYT VTVPDSCFPA TKPPLPHAAC HSCSEDSGSD VSSISHPTSP GSSSPDISFL
QPLSPPKTHR HRGAWVPAGS RELVAHHPKL LLPPGYFPAG RYVVVAESPL PPGEWELRRA
APGPAYEEEG TPLRYQRLVP SRSRIVRTPS LKDSPAGRGL SKAAVSEELK WWHERARLRS
TRPHSLDRQG AFRVRSLPLG REGFGRALGP RAQVPTVCVL RRSPDGAPVQ VFVPEKGEII
SQV
