RSAD2_MOUSE
ID RSAD2_MOUSE Reviewed; 362 AA.
AC Q8CBB9; Q3U5I6; Q3U5T4; Q3U622; Q3U627; Q3U7I6; Q3U7M1; Q3U8F4; Q3U8U7;
AC Q3U941; Q3U977; Q3U9E1; Q3U9J0; Q3U9J3; Q3UBW6; Q3UC07; Q3UDI0; Q6PEU4;
AC Q8VHM2; Q9JHD4;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Radical S-adenosyl methionine domain-containing protein 2;
DE EC=4.2.-.- {ECO:0000250|UniProtKB:Q8WXG1};
DE AltName: Full=Viperin;
DE AltName: Full=Virus inhibitory protein, endoplasmic reticulum-associated, interferon-inducible;
GN Name=Rsad2 {ECO:0000312|MGI:MGI:1929628};
GN Synonyms=Vig1 {ECO:0000312|EMBL:AAL50054.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAF60314.2}
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC STRAIN=C57BL/6J {ECO:0000269|PubMed:11038379};
RC TISSUE=Lymph node {ECO:0000269|PubMed:11038379};
RX PubMed=11038379; DOI=10.1099/0022-1317-81-11-2675;
RA Boudinot P., Riffault S., Salhi S., Carrat C., Sedlik C., Mahmoudi N.,
RA Charley B., Benmansour A.;
RT "Vesicular stomatitis virus and pseudorabies virus induce a vig1/cig5
RT homologue in mouse dendritic cells via different pathways.";
RL J. Gen. Virol. 81:2675-2682(2000).
RN [2] {ECO:0000312|EMBL:BAC29401.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC29401.1};
RC TISSUE=Bone {ECO:0000312|EMBL:BAC29401.1}, and
RC Bone marrow {ECO:0000312|EMBL:BAE31887.1};
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] {ECO:0000312|EMBL:CAJ18585.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000312|EMBL:AAH57868.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NMRI {ECO:0000312|EMBL:AAH57868.1};
RC TISSUE=Mammary tumor {ECO:0000312|EMBL:AAH57868.1};
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 [5] {ECO:0000305, ECO:0000312|EMBL:AAL50054.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-362.
RX PubMed=11752458; DOI=10.1073/pnas.011593298;
RA Chin K.-C., Cresswell P.;
RT "Viperin (cig5), an IFN-inducible antiviral protein directly induced by
RT human cytomegalovirus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:15125-15130(2001).
RN [6] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=15890971; DOI=10.1161/01.atv.0000170130.85334.38;
RA Olofsson P.S., Jatta K., Waagsaeter D., Gredmark S., Hedin U.,
RA Paulsson-Berne G., Soederberg-Naucler C., Hansson G.K., Sirsjoe A.;
RT "The antiviral cytomegalovirus inducible gene 5/viperin is expressed in
RT atherosclerosis and regulated by proinflammatory agents.";
RL Arterioscler. Thromb. Vasc. Biol. 25:E113-E116(2005).
RN [7] {ECO:0000305}
RP INDUCTION.
RX PubMed=16849320; DOI=10.1074/jbc.m604516200;
RA Severa M., Coccia E.M., Fitzgerald K.A.;
RT "Toll-like receptor-dependent and -independent viperin gene expression and
RT counter-regulation by PRDI-binding factor-1/BLIMP1.";
RL J. Biol. Chem. 281:26188-26195(2006).
RN [8] {ECO:0000305}
RP FUNCTION.
RX PubMed=17686841; DOI=10.1128/jvi.01282-07;
RA Zhang Y., Burke C.W., Ryman K.D., Klimstra W.B.;
RT "Identification and characterization of interferon-induced proteins that
RT inhibit alphavirus replication.";
RL J. Virol. 81:11246-11255(2007).
RN [9]
RP FUNCTION.
RX PubMed=19047684; DOI=10.1182/blood-2008-07-171942;
RA Qiu L.Q., Cresswell P., Chin K.C.;
RT "Viperin is required for optimal Th2 responses and T-cell receptor-mediated
RT activation of NF-kappaB and AP-1.";
RL Blood 113:3520-3529(2009).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=19920176; DOI=10.1073/pnas.0911679106;
RA Hinson E.R., Cresswell P.;
RT "The antiviral protein, viperin, localizes to lipid droplets via its N-
RT terminal amphipathic alpha-helix.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:20452-20457(2009).
RN [11]
RP IDENTIFICATION BY 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).
RN [12]
RP REVIEW.
RX PubMed=22177558; DOI=10.1016/j.chom.2011.11.004;
RA Seo J.Y., Yaneva R., Cresswell P.;
RT "Viperin: a multifunctional, interferon-inducible protein that regulates
RT virus replication.";
RL Cell Host Microbe 10:534-539(2011).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH IRAK1 AND TRAF6.
RX PubMed=21435586; DOI=10.1016/j.immuni.2011.03.010;
RA Saitoh T., Satoh T., Yamamoto N., Uematsu S., Takeuchi O., Kawai T.,
RA Akira S.;
RT "Antiviral protein Viperin promotes Toll-like receptor 7- and Toll-like
RT receptor 9-mediated type I interferon production in plasmacytoid dendritic
RT cells.";
RL Immunity 34:352-363(2011).
RN [14]
RP FUNCTION.
RX PubMed=21880757; DOI=10.1128/jvi.05519-11;
RA Szretter K.J., Brien J.D., Thackray L.B., Virgin H.W., Cresswell P.,
RA Diamond M.S.;
RT "The interferon-inducible gene viperin restricts West Nile virus
RT pathogenesis.";
RL J. Virol. 85:11557-11566(2011).
RN [15] {ECO:0007744|PDB:5VSL, ECO:0007744|PDB:5VSM}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 45-362 IN COMPLEX WITH
RP IRON-SULFUR (4FE-4S) AND S-ADENOSYL-L-METHIONINE, AND COFACTOR.
RX PubMed=28607080; DOI=10.1073/pnas.1705402114;
RA Fenwick M.K., Li Y., Cresswell P., Modis Y., Ealick S.E.;
RT "Structural studies of viperin, an antiviral radical SAM enzyme.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:6806-6811(2017).
CC -!- FUNCTION: Interferon-inducible antiviral protein which plays a major
CC role in the cell antiviral state induced by type I and type II
CC interferon. Catalyzes the conversion of cytidine triphosphate (CTP) to
CC 3'-deoxy-3',4'-didehydro-CTP (ddhCTP) via a SAM-dependent radical
CC mechanism. In turn, ddhCTP acts as a chain terminator for the RNA-
CC dependent RNA polymerases from multiple viruses and directly inhibits
CC viral replication. Therefore, inhibits a wide range of DNA and RNA
CC viruses (By similarity). Promotes also TLR7 and TLR9-dependent
CC production of IFN-beta production in plasmacytoid dendritic cells
CC (pDCs) by facilitating 'Lys-63'-linked ubiquitination of IRAK1 by
CC TRAF6. Plays a role in CD4+ T-cells activation and differentiation.
CC Facilitates T-cell receptor (TCR)-mediated GATA3 activation and optimal
CC T-helper 2 (Th2) cytokine production by modulating NFKB1 and JUNB
CC activities. Can inhibit secretion of soluble proteins (By similarity)
CC (PubMed:17686841, PubMed:19047684, PubMed:21435586, PubMed:21880757).
CC {ECO:0000250|UniProtKB:Q8WXG1, ECO:0000269|PubMed:17686841,
CC ECO:0000269|PubMed:19047684, ECO:0000269|PubMed:21435586,
CC ECO:0000269|PubMed:21880757}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + CTP + S-adenosyl-L-methionine = 3'-deoxy-3',4'-
CC didehydro-CTP + 5'-deoxyadenosine + A + H(+) + H2O + L-methionine;
CC Xref=Rhea:RHEA:65944, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:37563, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:166821; Evidence={ECO:0000250|UniProtKB:Q8WXG1};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:28607080, ECO:0007744|PDB:5VSL,
CC ECO:0007744|PDB:5VSM};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000269|PubMed:28607080, ECO:0007744|PDB:5VSL,
CC ECO:0007744|PDB:5VSM};
CC -!- ACTIVITY REGULATION: IRAK1 and TRAF6 synergistically activate RSAD2
CC increasing its activity with CTP as substrate about 10-fold.
CC {ECO:0000250|UniProtKB:Q8WXG1}.
CC -!- SUBUNIT: Homodimer. Interacts with IRAK1 and TRAF6 (PubMed:21435586).
CC Interacts with FPPS. Interacts with HADHB. Interacts (via C-terminus)
CC with VAPA/VAP33 (via C-terminus) (By similarity).
CC {ECO:0000250|UniProtKB:Q8WXG1, ECO:0000269|PubMed:21435586}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8WXG1}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q8WXG1}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q8WXG1}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q8WXG1}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q8WXG1}. Lipid droplet
CC {ECO:0000269|PubMed:19920176, ECO:0000269|PubMed:21435586}.
CC Mitochondrion {ECO:0000250|UniProtKB:Q8WXG1}. Mitochondrion inner
CC membrane {ECO:0000250|UniProtKB:Q8WXG1}. Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q8WXG1}.
CC -!- TISSUE SPECIFICITY: Expressed at higher levels in atherosclerotic
CC arteries than in normal arteries. {ECO:0000269|PubMed:15890971}.
CC -!- INDUCTION: By interferon type I, type II and LPS. Induced by infection
CC with Vesicular stomatitis virus and pseudorabies virus in dendritic
CC cells, presumably through type I interferon pathway.
CC {ECO:0000269|PubMed:11038379, ECO:0000269|PubMed:16849320}.
CC -!- DOMAIN: The N-terminal region (1-43) is necessary for its localization
CC to the endoplasmic reticulum membrane and lipid droplet.
CC -!- PTM: Acetylated by HAT1. HAT1-mediated acetylation of Lys-198 in turn
CC recruits UBE4A that stimulates RSAD2 polyubiquitination leading to
CC proteasomal degradation. {ECO:0000250|UniProtKB:Q8WXG1}.
CC -!- PTM: 'Lys-6'-linked polyubiquitination at Lys-207 leads to RSAD2
CC protein degradation. {ECO:0000250|UniProtKB:Q8WXG1}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. RSAD2 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE29281.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF236064; AAF60314.2; -; mRNA.
DR EMBL; AK036373; BAC29401.1; -; mRNA.
DR EMBL; AK150069; BAE29281.1; ALT_SEQ; mRNA.
DR EMBL; AK150406; BAE29532.1; -; mRNA.
DR EMBL; AK150425; BAE29548.1; -; mRNA.
DR EMBL; AK150525; BAE29636.1; -; mRNA.
DR EMBL; AK150616; BAE29706.1; -; mRNA.
DR EMBL; AK150684; BAE29764.1; -; mRNA.
DR EMBL; AK150731; BAE29807.1; -; mRNA.
DR EMBL; AK150767; BAE29833.1; -; mRNA.
DR EMBL; AK150783; BAE29848.1; -; mRNA.
DR EMBL; AK150788; BAE29852.1; -; mRNA.
DR EMBL; AK150812; BAE29875.1; -; mRNA.
DR EMBL; AK150835; BAE29895.1; -; mRNA.
DR EMBL; AK151140; BAE30147.1; -; mRNA.
DR EMBL; AK151185; BAE30184.1; -; mRNA.
DR EMBL; AK151191; BAE30188.1; -; mRNA.
DR EMBL; AK151206; BAE30203.1; -; mRNA.
DR EMBL; AK151286; BAE30271.1; -; mRNA.
DR EMBL; AK151308; BAE30290.1; -; mRNA.
DR EMBL; AK151339; BAE30317.1; -; mRNA.
DR EMBL; AK151389; BAE30360.1; -; mRNA.
DR EMBL; AK151410; BAE30375.1; -; mRNA.
DR EMBL; AK151412; BAE30377.1; -; mRNA.
DR EMBL; AK151414; BAE30379.1; -; mRNA.
DR EMBL; AK151476; BAE30431.1; -; mRNA.
DR EMBL; AK151502; BAE30453.1; -; mRNA.
DR EMBL; AK151538; BAE30485.1; -; mRNA.
DR EMBL; AK151767; BAE30673.1; -; mRNA.
DR EMBL; AK151770; BAE30676.1; -; mRNA.
DR EMBL; AK151825; BAE30722.1; -; mRNA.
DR EMBL; AK151833; BAE30726.1; -; mRNA.
DR EMBL; AK151846; BAE30737.1; -; mRNA.
DR EMBL; AK151906; BAE30787.1; -; mRNA.
DR EMBL; AK151909; BAE30790.1; -; mRNA.
DR EMBL; AK151940; BAE30816.1; -; mRNA.
DR EMBL; AK151954; BAE30826.1; -; mRNA.
DR EMBL; AK151971; BAE30840.1; -; mRNA.
DR EMBL; AK152050; BAE30906.1; -; mRNA.
DR EMBL; AK152065; BAE30920.1; -; mRNA.
DR EMBL; AK152075; BAE30927.1; -; mRNA.
DR EMBL; AK152235; BAE31060.1; -; mRNA.
DR EMBL; AK152239; BAE31062.1; -; mRNA.
DR EMBL; AK152241; BAE31064.1; -; mRNA.
DR EMBL; AK152310; BAE31116.1; -; mRNA.
DR EMBL; AK152354; BAE31146.1; -; mRNA.
DR EMBL; AK152493; BAE31264.1; -; mRNA.
DR EMBL; AK152600; BAE31348.1; -; mRNA.
DR EMBL; AK152601; BAE31349.1; -; mRNA.
DR EMBL; AK152631; BAE31374.1; -; mRNA.
DR EMBL; AK152644; BAE31383.1; -; mRNA.
DR EMBL; AK152664; BAE31399.1; -; mRNA.
DR EMBL; AK152796; BAE31501.1; -; mRNA.
DR EMBL; AK152861; BAE31552.1; -; mRNA.
DR EMBL; AK152880; BAE31565.1; -; mRNA.
DR EMBL; AK152895; BAE31578.1; -; mRNA.
DR EMBL; AK152934; BAE31608.1; -; mRNA.
DR EMBL; AK152962; BAE31625.1; -; mRNA.
DR EMBL; AK153003; BAE31643.1; -; mRNA.
DR EMBL; AK153024; BAE31658.1; -; mRNA.
DR EMBL; AK153062; BAE31688.1; -; mRNA.
DR EMBL; AK153077; BAE31702.1; -; mRNA.
DR EMBL; AK153078; BAE31703.1; -; mRNA.
DR EMBL; AK153232; BAE31825.1; -; mRNA.
DR EMBL; AK153234; BAE31827.1; -; mRNA.
DR EMBL; AK153306; BAE31887.1; -; mRNA.
DR EMBL; AK153318; BAE31898.1; -; mRNA.
DR EMBL; AK153324; BAE31903.1; -; mRNA.
DR EMBL; AK153435; BAE31992.1; -; mRNA.
DR EMBL; AK153556; BAE32092.1; -; mRNA.
DR EMBL; AK159147; BAE34854.1; -; mRNA.
DR EMBL; CT010378; CAJ18585.1; -; mRNA.
DR EMBL; BC057868; AAH57868.1; -; mRNA.
DR EMBL; AF442152; AAL50054.1; -; mRNA.
DR CCDS; CCDS25848.1; -.
DR RefSeq; NP_067359.2; NM_021384.4.
DR PDB; 5VSL; X-ray; 1.97 A; A/B=45-362.
DR PDB; 5VSM; X-ray; 1.70 A; A/B=45-362.
DR PDB; 6Q2P; X-ray; 1.45 A; A/B=45-362.
DR PDB; 6Q2Q; X-ray; 1.89 A; A/B=45-362.
DR PDBsum; 5VSL; -.
DR PDBsum; 5VSM; -.
DR PDBsum; 6Q2P; -.
DR PDBsum; 6Q2Q; -.
DR AlphaFoldDB; Q8CBB9; -.
DR SMR; Q8CBB9; -.
DR BioGRID; 208378; 11.
DR STRING; 10090.ENSMUSP00000020970; -.
DR iPTMnet; Q8CBB9; -.
DR PhosphoSitePlus; Q8CBB9; -.
DR SwissPalm; Q8CBB9; -.
DR MaxQB; Q8CBB9; -.
DR PaxDb; Q8CBB9; -.
DR PRIDE; Q8CBB9; -.
DR ProteomicsDB; 257042; -.
DR Antibodypedia; 12336; 205 antibodies from 32 providers.
DR DNASU; 58185; -.
DR Ensembl; ENSMUST00000020970; ENSMUSP00000020970; ENSMUSG00000020641.
DR GeneID; 58185; -.
DR KEGG; mmu:58185; -.
DR UCSC; uc007nfh.2; mouse.
DR CTD; 91543; -.
DR MGI; MGI:1929628; Rsad2.
DR VEuPathDB; HostDB:ENSMUSG00000020641; -.
DR eggNOG; ENOG502QQMH; Eukaryota.
DR GeneTree; ENSGT00390000013670; -.
DR HOGENOM; CLU_049058_2_1_1; -.
DR InParanoid; Q8CBB9; -.
DR OMA; FRWKCFQ; -.
DR OrthoDB; 1098093at2759; -.
DR PhylomeDB; Q8CBB9; -.
DR TreeFam; TF300085; -.
DR BioGRID-ORCS; 58185; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q8CBB9; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8CBB9; protein.
DR Bgee; ENSMUSG00000020641; Expressed in blood and 163 other tissues.
DR ExpressionAtlas; Q8CBB9; baseline and differential.
DR Genevisible; Q8CBB9; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:CACAO.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0035710; P:CD4-positive, alpha-beta T cell activation; IMP:UniProtKB.
DR GO; GO:0043367; P:CD4-positive, alpha-beta T cell differentiation; IMP:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0050709; P:negative regulation of protein secretion; ISS:UniProtKB.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IMP:UniProtKB.
DR GO; GO:0001503; P:ossification; ISO:MGI.
DR GO; GO:0050778; P:positive regulation of immune response; IBA:GO_Central.
DR GO; GO:2000553; P:positive regulation of T-helper 2 cell cytokine production; IMP:UniProtKB.
DR GO; GO:0034157; P:positive regulation of toll-like receptor 7 signaling pathway; IMP:UniProtKB.
DR GO; GO:0034165; P:positive regulation of toll-like receptor 9 signaling pathway; IMP:UniProtKB.
DR GO; GO:0030278; P:regulation of ossification; ISO:MGI.
DR GO; GO:0009615; P:response to virus; IMP:UniProtKB.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR007197; rSAM.
DR Pfam; PF04055; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Acetylation; Antiviral defense;
KW Endoplasmic reticulum; Golgi apparatus; Immunity; Innate immunity; Iron;
KW Iron-sulfur; Isopeptide bond; Lipid droplet; Lyase; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Mitochondrion outer membrane; Reference proteome; S-adenosyl-L-methionine;
KW Ubl conjugation.
FT CHAIN 1..362
FT /note="Radical S-adenosyl methionine domain-containing
FT protein 2"
FT /id="PRO_0000309584"
FT DOMAIN 70..290
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT REGION 47..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 84
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000269|PubMed:28607080,
FT ECO:0007744|PDB:5VSL, ECO:0007744|PDB:5VSM"
FT BINDING 88
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000269|PubMed:28607080,
FT ECO:0007744|PDB:5VSL, ECO:0007744|PDB:5VSM"
FT BINDING 91
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000269|PubMed:28607080,
FT ECO:0007744|PDB:5VSL, ECO:0007744|PDB:5VSM"
FT MOD_RES 198
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXG1"
FT CROSSLNK 207
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q8WXG1"
FT CONFLICT 15
FT /note="S -> R (in Ref. 2; BAE31578/BAE30379/BAE29807/
FT BAE29764)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="S -> C (in Ref. 2; BAE30676)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="S -> G (in Ref. 2; BAE31898/BAE31903)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="R -> P (in Ref. 2; BAE30920)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="P -> L (in Ref. 1; AAF60314, 3; CAJ18585, 4;
FT AAH57868 and 5; AAL50054)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="D -> E (in Ref. 1; AAF60314, 3; CAJ18585, 4;
FT AAH57868 and 5; AAL50054)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="P -> R (in Ref. 1; AAF60314, 3; CAJ18585, 4;
FT AAH57868 and 5; AAL50054)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="P -> T (in Ref. 2; BAE31898)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="T -> K (in Ref. 2; BAE30826/BAE32092)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="G -> E (in Ref. 2; BAE29848)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="L -> Q (in Ref. 2; BAE31064)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="A -> S (in Ref. 2; BAE30826)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="R -> Q (in Ref. 1; AAF60314 and 5; AAL50054)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="W -> R (in Ref. 2; BAE31565/BAE31383/BAE30737)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="L -> Q (in Ref. 2; BAE31898/BAE31903)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="K -> E (in Ref. 2; BAE30673/BAE30203)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="D -> G (in Ref. 2; BAE30726)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="F -> L (in Ref. 2; BAE31348)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="S -> G (in Ref. 2; BAE31064)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="F -> Y (in Ref. 2; BAE30676/BAE30787/BAE30790/
FT BAE30920/BAE30927)"
FT /evidence="ECO:0000305"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:6Q2P"
FT HELIX 103..115
FT /evidence="ECO:0007829|PDB:6Q2P"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:6Q2P"
FT HELIX 128..134
FT /evidence="ECO:0007829|PDB:6Q2P"
FT HELIX 135..146
FT /evidence="ECO:0007829|PDB:6Q2P"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:6Q2P"
FT HELIX 164..170
FT /evidence="ECO:0007829|PDB:6Q2P"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:6Q2P"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:6Q2P"
FT HELIX 186..192
FT /evidence="ECO:0007829|PDB:6Q2P"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:5VSM"
FT HELIX 201..215
FT /evidence="ECO:0007829|PDB:6Q2P"
FT STRAND 218..225
FT /evidence="ECO:0007829|PDB:6Q2P"
FT TURN 227..231
FT /evidence="ECO:0007829|PDB:6Q2P"
FT HELIX 235..241
FT /evidence="ECO:0007829|PDB:6Q2P"
FT STRAND 244..250
FT /evidence="ECO:0007829|PDB:6Q2P"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:6Q2P"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:6Q2P"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:6Q2P"
FT HELIX 274..283
FT /evidence="ECO:0007829|PDB:6Q2P"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:6Q2P"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:6Q2P"
FT HELIX 295..298
FT /evidence="ECO:0007829|PDB:6Q2P"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:6Q2P"
FT STRAND 309..313
FT /evidence="ECO:0007829|PDB:6Q2P"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:6Q2P"
FT HELIX 325..328
FT /evidence="ECO:0007829|PDB:6Q2P"
FT HELIX 330..334
FT /evidence="ECO:0007829|PDB:6Q2P"
FT HELIX 341..346
FT /evidence="ECO:0007829|PDB:6Q2P"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:6Q2P"
SQ SEQUENCE 362 AA; 41524 MW; F56F0BBEC9F20E50 CRC64;
MGMLVPTALA ARLLSLFQQQ LGSLWSGLAI LFCWLRIALG WLDPGKEQPQ VRGEPEDTQE
TQEDGNSTQP TTPVSVNYHF TRQCNYKCGF CFHTAKTSFV LPLEEAKRGL LLLKQAGLEK
INFSGGEPFL QDRGEYLGKL VRFCKEELAL PSVSIVSNGS LIRERWFKDY GEYLDILAIS
CDSFDEQVNA LIGRGQGKKN HVENLQKLRR WCRDYKVAFK INSVINRFNV DEDMNEHIKA
LSPVRWKVFQ CLLIEGENSG EDALREAERF LISNEEFETF LERHKEVSCL VPESNQKMKD
SYLILDEYMR FLNCTGGRKD PSKSILDVGV EEAIKFSGFD EKMFLKRGGK YVWSKADLKL
DW
