ID   RSAD2_ONCMY             Reviewed;         348 AA.
AC   O93384;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Radical S-adenosyl methionine domain-containing protein 2;
DE   AltName: Full=Viperin;
DE   AltName: Full=Virus inhibitory protein, endoplasmic reticulum-associated, interferon-inducible;
GN   Name=rsad2 {ECO:0000250|UniProtKB:Q5RH95};
GN   Synonyms=vig1 {ECO:0000312|EMBL:AAC27319.1};
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAC27319.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=9971762; DOI=10.1128/jvi.73.3.1846-1852.1999;
RA   Boudinot P., Massin P., Blanco M., Riffault S., Benmansour A.;
RT   "vig-1, a new fish gene induced by the rhabdovirus glycoprotein, has a
RT   virus-induced homologue in humans and shares conserved motifs with the MoaA
RT   family.";
RL   J. Virol. 73:1846-1852(1999).
CC   -!- FUNCTION: Interferon-inducible iron-sulfur (4FE-4S) cluster-binding
CC       antiviral protein which plays a major role in the cell antiviral state
CC       induced by type I and type II interferon. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:Q8CBB9};
CC       Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000250|UniProtKB:Q8CBB9};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed at low levels in spleen and head kidney.
CC       {ECO:0000269|PubMed:9971762}.
CC   -!- INDUCTION: By interferon type I, type II and LPS. Induced by infection
CC       with viral hemorrhagic septicemia virus (VHSV), presumably through type
CC       I interferon pathway. {ECO:0000269|PubMed:9971762}.
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. RSAD2 family.
CC       {ECO:0000305}.
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; AF076620; AAC27319.1; -; mRNA.
DR   RefSeq; NP_001117725.1; NM_001124253.1.
DR   AlphaFoldDB; O93384; -.
DR   SMR; O93384; -.
DR   GeneID; 100135876; -.
DR   KEGG; omy:100135876; -.
DR   CTD; 100135876; -.
DR   OrthoDB; 1098093at2759; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   4Fe-4S; Antiviral defense; Endoplasmic reticulum; Immunity;
KW   Innate immunity; Iron; Iron-sulfur; Membrane; Metal-binding;
KW   S-adenosyl-L-methionine.
FT   CHAIN           1..348
FT                   /note="Radical S-adenosyl methionine domain-containing
FT                   protein 2"
FT                   /id="PRO_0000309589"
FT   DOMAIN          56..276
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   BINDING         70
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CBB9"
FT   BINDING         74
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CBB9"
FT   BINDING         77
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CBB9"
SQ   SEQUENCE   348 AA;  40002 MW;  F40BB10B9F3277EE CRC64;
     MFLQRCMSFL QCIFAAVLAW IGVRGQQVHG ASQFSSTGKV NPATIKVVNN VISQASATPS
     SVNYHFTRQC NYKCGFCFHT AKTSFVLPIE EAKRGLQLLK ESGLEKINFS GGEPFIHDRG
     DFLGKLVQYC KHDLQLPSVS IVSNGSMIRE KWFQTYGEYL DILAISCDSF DEDTNQTIGR
     AQGRKSHLDN LFKVRDWCRK YKVAFKINSV INTFNVDEDM RENITELNPV RWKVFQCLLI
     DGENAGENSL REAERFLISD QQFQDFLERH SSISCLVPES NQKMRDSYLI LDEYMRFLDC
     REGRKDPSKS ILDVGVEEAI QFSGFDEKMF LKRGGKYVWS KADMRLEW