ID DDAH2_HUMAN Reviewed; 285 AA. AC O95865; A2BEZ7; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 27-MAR-2024, entry version 188. DE RecName: Full=Putative hydrolase DDAH2 {ECO:0000305}; DE EC=3.-.-.- {ECO:0000305}; DE AltName: Full=DDAHII; DE AltName: Full=Inactive N(G),N(G)-dimethylarginine dimethylaminohydrolase 2 {ECO:0000305|PubMed:37296100}; DE Short=DDAH-2; DE Short=Inactive dimethylarginine dimethylaminohydrolase 2; DE AltName: Full=Protein G6a; DE AltName: Full=S-phase protein; GN Name=DDAH2 {ECO:0000312|HGNC:HGNC:2716}; Synonyms=DDAH, G6A, NG30; 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 [MRNA], ORIGINAL FUNCTION, TISSUE SPECIFICITY, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=10493931; DOI=10.1042/bj3430209; RA Leiper J.M., Santa Maria J., Chubb A., MacAllister R.J., Charles I.G., RA Whitley G.S., Vallance P.; RT "Identification of two human dimethylarginine dimethylaminohydrolases with RT distinct tissue distributions and homology with microbial arginine RT deiminases."; RL Biochem. J. 343:209-214(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Umbilical cord blood; RX PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for 300 RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor RT cells."; RL Genome Res. 10:1546-1560(2000). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10384126; RA Ribas G., Neville M., Wixon J.L., Cheng J., Campbell R.D.; RT "Genes encoding three new members of the leukocyte antigen 6 superfamily RT and a novel member of Ig superfamily, together with genes encoding the RT regulatory nuclear chloride ion channel protein (hRNCC) and an N omega-N RT omega-dimethylarginine dimethylaminohydrolase homologue, are found in a 30- RT kb segment of the MHC class III region."; RL J. Immunol. 163:278-287(1999). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Yu L.; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14656967; DOI=10.1101/gr.1736803; RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., RA Hood L.; RT "Analysis of the gene-dense major histocompatibility complex class III RT region and its comparison to mouse."; RL Genome Res. 13:2621-2636(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Shiina S., Tamiya G., Oka A., Inoko H.; RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; 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 [10] RP PROTEIN SEQUENCE OF 18-40; 113-134; 148-173 AND 268-285, AND IDENTIFICATION RP BY MASS SPECTROMETRY. RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex; RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP FUNCTION, AND CAUTION. RX PubMed=21493890; DOI=10.1161/atvbaha.110.222638; RA Hu X., Atzler D., Xu X., Zhang P., Guo H., Lu Z., Fassett J., RA Schwedhelm E., Boeger R.H., Bache R.J., Chen Y.; RT "Dimethylarginine dimethylaminohydrolase-1 is the critical enzyme for RT degrading the cardiovascular risk factor asymmetrical dimethylarginine."; RL Arterioscler. Thromb. Vasc. Biol. 31:1540-1546(2011). RN [13] RP SUBCELLULAR LOCATION. RX PubMed=21898353; DOI=10.1002/art.30652; RA Cillero-Pastor B., Mateos J., Fernandez-Lopez C., Oreiro N., RA Ruiz-Romero C., Blanco F.J.; RT "Dimethylarginine dimethylaminohydrolase 2, a newly identified RT mitochondrial protein modulating nitric oxide synthesis in normal human RT chondrocytes."; RL Arthritis Rheum. 64:204-212(2012). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [15] RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, SUBCELLULAR LOCATION RP (MICROBIAL INFECTION), AND MUTAGENESIS OF SER-68; SER-162; THR-163; RP THR-183; THR-203; SER-209; THR-211; SER-245 AND SER-253. RX PubMed=33850055; DOI=10.1126/scisignal.abc7931; RA Huang S., Li Z., Wu Z., Liu C., Yu M., Wen M., Zhang L., Wang X.; RT "DDAH2 suppresses RLR-MAVS-mediated innate antiviral immunity by RT stimulating nitric oxide-activated, Drp1-induced mitochondrial fission."; RL Sci. Signal. 14:0-0(2021). RN [16] RP FUNCTION, AND CAUTION. RX PubMed=37296100; DOI=10.1038/s41467-023-38467-9; RA Ragavan V.N., Nair P.C., Jarzebska N., Angom R.S., Ruta L., Bianconi E., RA Grottelli S., Tararova N.D., Ryazanskiy D., Lentz S.R., Tommasi S., RA Martens-Lobenhoffer J., Suzuki-Yamamoto T., Kimoto M., Rubets E., Chau S., RA Chen Y., Hu X., Bernhardt N., Spieth P.M., Weiss N., Bornstein S.R., RA Mukhopadhyay D., Bode-Boeger S.M., Maas R., Wang Y., Macchiarulo A., RA Mangoni A.A., Cellini B., Rodionov R.N.; RT "A multicentric consortium study demonstrates that dimethylarginine RT dimethylaminohydrolase 2 is not a dimethylarginine RT dimethylaminohydrolase."; RL Nat. Commun. 14:3392-3392(2023). CC -!- FUNCTION: Putative hydrolase with unknown substrate (Probable). Does CC not hydrolyze N(G),N(G)-dimethyl-L-arginine (ADMA) which acts as an CC inhibitor of NOS (PubMed:37296100, PubMed:21493890). In endothelial CC cells, induces expression of vascular endothelial growth factor (VEGF) CC via phosphorylation of the transcription factor SP1 by PKA in a process CC that is independent of NO and NO synthase (By similarity). Similarly, CC enhances pancreatic insulin secretion through SP1-mediated CC transcriptional up-regulation of secretagogin/SCGN, an insulin vesicle CC docking protein (By similarity). Upon viral infection, relocates to CC mitochondria where it promotes mitochondrial fission through activation CC of DNM1L leading to the inhibition of innate response activation CC mediated by MAVS (PubMed:33850055). {ECO:0000250|UniProtKB:Q99LD8, CC ECO:0000269|PubMed:21493890, ECO:0000269|PubMed:33850055, CC ECO:0000269|PubMed:37296100, ECO:0000305|PubMed:10493931, CC ECO:0000305|PubMed:21493890, ECO:0000305|PubMed:37296100}. CC -!- INTERACTION: CC O95865; Q08043: ACTN3; NbExp=3; IntAct=EBI-749139, EBI-2880652; CC O95865; Q9NW38: FANCL; NbExp=3; IntAct=EBI-749139, EBI-2339898; CC O95865; Q86VF2-5: IGFN1; NbExp=3; IntAct=EBI-749139, EBI-11955401; CC O95865; Q86UR1-2: NOXA1; NbExp=3; IntAct=EBI-749139, EBI-12025760; CC O95865; O43741: PRKAB2; NbExp=3; IntAct=EBI-749139, EBI-1053424; CC O95865; Q15645: TRIP13; NbExp=6; IntAct=EBI-749139, EBI-358993; CC O95865; PRO_0000037314 [P0C6X7]: rep; Xeno; NbExp=2; IntAct=EBI-749139, EBI-25487672; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21898353, CC ECO:0000269|PubMed:33850055}. Mitochondrion CC {ECO:0000269|PubMed:21898353, ECO:0000269|PubMed:33850055}. CC Note=Translocates from cytosol to mitochondrion upon IL1B stimulation CC in chondrocytes. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:33850055}. CC Note=(Microbial infection) Translocates to the mitochondrion upon CC Sendai viral infection. {ECO:0000269|PubMed:33850055}. CC -!- TISSUE SPECIFICITY: Detected in heart, placenta, lung, liver, skeletal CC muscle, kidney and pancreas, and at very low levels in brain. CC {ECO:0000269|PubMed:10493931}. CC -!- PTM: Phosphorylated by TBK1. Phosphorylation inhibits the translocation CC into the mitochondrion upon Sendai viral infection. CC {ECO:0000269|PubMed:33850055}. CC -!- SIMILARITY: Belongs to the DDAH family. {ECO:0000305}. CC -!- CAUTION: Was originally thought to be a dimethylarginine CC dimethylaminohydrolase (with EC:3.5.3.18) able to hydrolyze N(G),N(G)- CC dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) CC (PubMed:10493931). However, a recent multicentre study has shown that CC DDAH2 does not have dimethylarginine dimethylaminohydrolase activity by CC using different approaches (PubMed:37296100, PubMed:21493890). CC {ECO:0000269|PubMed:10493931, ECO:0000269|PubMed:21493890, CC ECO:0000269|PubMed:37296100}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF070667; AAD20973.1; -; mRNA. DR EMBL; AJ012008; CAB46079.1; -; Genomic_DNA. DR EMBL; AF087894; AAP97193.1; -; mRNA. DR EMBL; AF129756; AAD18074.1; -; Genomic_DNA. DR EMBL; BA000025; BAB63377.1; -; Genomic_DNA. DR EMBL; AL662899; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL670886; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL844216; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX248244; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR354443; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR759787; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR936239; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471081; EAX03500.1; -; Genomic_DNA. DR EMBL; BC001435; AAH01435.1; -; mRNA. DR CCDS; CCDS4718.1; -. DR RefSeq; NP_001289936.1; NM_001303007.1. DR RefSeq; NP_001289937.1; NM_001303008.1. DR RefSeq; NP_039268.1; NM_013974.2. DR RefSeq; XP_011512750.1; XM_011514448.2. DR AlphaFoldDB; O95865; -. DR SMR; O95865; -. DR BioGRID; 117107; 72. DR IntAct; O95865; 40. DR MINT; O95865; -. DR STRING; 9606.ENSP00000364949; -. DR DrugBank; DB00155; Citrulline. DR GlyCosmos; O95865; 2 sites, 1 glycan. DR GlyGen; O95865; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; O95865; -. DR MetOSite; O95865; -. DR PhosphoSitePlus; O95865; -. DR SwissPalm; O95865; -. DR BioMuta; DDAH2; -. DR REPRODUCTION-2DPAGE; IPI00000760; -. DR REPRODUCTION-2DPAGE; O95865; -. DR EPD; O95865; -. DR jPOST; O95865; -. DR MassIVE; O95865; -. DR PaxDb; 9606-ENSP00000364945; -. DR PeptideAtlas; O95865; -. DR ProteomicsDB; 51100; -. DR Pumba; O95865; -. DR Antibodypedia; 27580; 310 antibodies from 34 providers. DR DNASU; 23564; -. DR Ensembl; ENST00000375787.6; ENSP00000364943.2; ENSG00000213722.10. DR Ensembl; ENST00000375789.7; ENSP00000364945.2; ENSG00000213722.10. DR Ensembl; ENST00000375792.7; ENSP00000364949.3; ENSG00000213722.10. DR Ensembl; ENST00000383409.6; ENSP00000372901.2; ENSG00000206395.8. DR Ensembl; ENST00000400062.5; ENSP00000382935.1; ENSG00000206395.8. DR Ensembl; ENST00000400063.7; ENSP00000382936.3; ENSG00000206395.8. DR Ensembl; ENST00000411456.6; ENSP00000409396.2; ENSG00000226634.6. DR Ensembl; ENST00000413532.5; ENSP00000402594.1; ENSG00000226634.6. DR Ensembl; ENST00000413655.5; ENSP00000412800.1; ENSG00000233076.6. DR Ensembl; ENST00000414455.5; ENSP00000404342.1; ENSG00000225635.7. DR Ensembl; ENST00000416410.6; ENSP00000397466.2; ENSG00000213722.10. DR Ensembl; ENST00000424790.5; ENSP00000391632.1; ENSG00000233076.6. DR Ensembl; ENST00000426149.5; ENSP00000412327.1; ENSG00000228128.6. DR Ensembl; ENST00000427126.5; ENSP00000395372.1; ENSG00000228128.6. DR Ensembl; ENST00000430482.5; ENSP00000408148.1; ENSG00000227317.6. DR Ensembl; ENST00000434464.6; ENSP00000391833.2; ENSG00000228128.6. DR Ensembl; ENST00000436437.2; ENSP00000395759.2; ENSG00000213722.10. DR Ensembl; ENST00000437889.6; ENSP00000399023.2; ENSG00000227317.6. DR Ensembl; ENST00000443533.5; ENSP00000389552.1; ENSG00000226634.6. DR Ensembl; ENST00000444699.5; ENSP00000404851.1; ENSG00000225635.7. DR Ensembl; ENST00000447101.6; ENSP00000405515.2; ENSG00000233076.6. DR Ensembl; ENST00000451411.5; ENSP00000403154.1; ENSG00000227317.6. DR Ensembl; ENST00000454138.6; ENSP00000399357.2; ENSG00000225635.7. DR GeneID; 23564; -. DR KEGG; hsa:23564; -. DR MANE-Select; ENST00000375789.7; ENSP00000364945.2; NM_001303007.2; NP_001289936.1. DR AGR; HGNC:2716; -. DR CTD; 23564; -. DR DisGeNET; 23564; -. DR GeneCards; DDAH2; -. DR HGNC; HGNC:2716; DDAH2. DR HPA; ENSG00000213722; Low tissue specificity. DR MIM; 604744; gene. DR neXtProt; NX_O95865; -. DR OpenTargets; ENSG00000213722; -. DR PharmGKB; PA27186; -. DR VEuPathDB; HostDB:ENSG00000213722; -. DR eggNOG; ENOG502QW4J; Eukaryota. DR GeneTree; ENSGT00940000160769; -. DR InParanoid; O95865; -. DR OMA; CPYGRFT; -. DR OrthoDB; 315054at2759; -. DR PhylomeDB; O95865; -. DR TreeFam; TF314737; -. DR BioCyc; MetaCyc:HS03493-MONOMER; -. DR BRENDA; 3.5.3.18; 2681. DR PathwayCommons; O95865; -. DR SignaLink; O95865; -. DR BioGRID-ORCS; 23564; 15 hits in 1157 CRISPR screens. DR ChiTaRS; DDAH2; human. DR GenomeRNAi; 23564; -. DR Pharos; O95865; Tbio. DR PRO; PR:O95865; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; O95865; Protein. DR Bgee; ENSG00000213722; Expressed in ganglionic eminence and 93 other cell types or tissues. DR ExpressionAtlas; O95865; baseline and differential. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0016597; F:amino acid binding; IBA:GO_Central. DR GO; GO:0016403; F:dimethylargininase activity; IBA:GO_Central. DR GO; GO:0006525; P:arginine metabolic process; IBA:GO_Central. DR GO; GO:0000052; P:citrulline metabolic process; IBA:GO_Central. DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB. DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISS:BHF-UCL. DR InterPro; IPR033199; DDAH-like. DR PANTHER; PTHR12737; DIMETHYLARGININE DIMETHYLAMINOHYDROLASE; 1. DR PANTHER; PTHR12737:SF16; N(G),N(G)-DIMETHYLARGININE DIMETHYLAMINOHYDROLASE 2; 1. DR SUPFAM; SSF55909; Pentein; 1. DR Genevisible; O95865; HS. PE 1: Evidence at protein level; KW Cytoplasm; Direct protein sequencing; Hydrolase; Mitochondrion; KW Reference proteome. FT CHAIN 1..285 FT /note="Putative hydrolase DDAH2" FT /id="PRO_0000171121" FT ACT_SITE 171 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:O94760" FT ACT_SITE 276 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:O94760" FT MUTAGEN 68 FT /note="S->D: No effect on inhibition of MAVS-mediated FT innate response activation." FT /evidence="ECO:0000269|PubMed:33850055" FT MUTAGEN 162 FT /note="S->D: No effect on inhibition of MAVS-mediated FT innate response activation." FT /evidence="ECO:0000269|PubMed:33850055" FT MUTAGEN 163 FT /note="T->D: No effect on inhibition of MAVS-mediated FT innate response activation." FT /evidence="ECO:0000269|PubMed:33850055" FT MUTAGEN 183 FT /note="T->D: No effect on inhibition of MAVS-mediated FT innate response activation." FT /evidence="ECO:0000269|PubMed:33850055" FT MUTAGEN 203 FT /note="T->D: Loss of mitochondrial translocation upon viral FT infection. Loss of inhibition of MAVS-mediated innate FT response activation." FT /evidence="ECO:0000269|PubMed:33850055" FT MUTAGEN 209 FT /note="S->D: No effect on inhibition of MAVS-mediated FT innate response activation." FT /evidence="ECO:0000269|PubMed:33850055" FT MUTAGEN 211 FT /note="T->D: Loss of mitochondrial translocation upon viral FT infection. Loss of inhibition of MAVS-mediated innate FT response activation." FT /evidence="ECO:0000269|PubMed:33850055" FT MUTAGEN 245 FT /note="S->D: Loss of mitochondrial translocation upon viral FT infection. Loss of inhibition of MAVS-mediated innate FT response activation." FT /evidence="ECO:0000269|PubMed:33850055" FT MUTAGEN 253 FT /note="S->D: Loss of mitochondrial translocation upon viral FT infection. Loss of inhibition of MAVS-mediated innate FT response activation." FT /evidence="ECO:0000269|PubMed:33850055" SQ SEQUENCE 285 AA; 29644 MW; B3D9B00F29492548 CRC64; MGTPGEGLGR CSHALIRGVP ESLASGEGAG AGLPALDLAK AQREHGVLGG KLRQRLGLQL LELPPEESLP LGPLLGDTAV IQGDTALITR PWSPARRPEV DGVRKALQDL GLRIVEIGDE NATLDGTDVL FTGREFFVGL SKWTNHRGAE IVADTFRDFA VSTVPVSGPS HLRGLCGMGG PRTVVAGSSD AAQKAVRAMA VLTDHPYASL TLPDDAAADC LFLRPGLPGV PPFLLHRGGG DLPNSQEALQ KLSDVTLVPV SCSELEKAGA GLSSLCLVLS TRPHS //