ID   RSAD2_SINCH             Reviewed;         354 AA.
AC   Q6EE23;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 58.
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};
OS   Siniperca chuatsi (Mandarin fish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Centrarchiformes; Centrarchoidei; Sinipercidae; Siniperca.
OX   NCBI_TaxID=119488;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAS77258.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=15350746; DOI=10.1016/j.vetimm.2004.04.013;
RA   Sun B.J., Nie P.;
RT   "Molecular cloning of the viperin gene and its promoter region from the
RT   mandarin fish Siniperca chuatsi.";
RL   Vet. Immunol. Immunopathol. 101:161-170(2004).
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: Constitutively expressed in spleen, head kidney and
CC       trunk kidney. Following viral infection, detected in most organs
CC       including liver, gill, intestine, heart, muscle and brain.
CC       {ECO:0000269|PubMed:15350746}.
CC   -!- INDUCTION: By interferon type I, type II and LPS. Induced by infection
CC       with Infectious spleen and kidney necrosis virus (ISKNV), presumably
CC       through type I interferon pathway. {ECO:0000269|PubMed:15350746}.
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. RSAD2 family.
CC       {ECO:0000305}.
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DR   EMBL; AY395718; AAS77258.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6EE23; -.
DR   SMR; Q6EE23; -.
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..354
FT                   /note="Radical S-adenosyl methionine domain-containing
FT                   protein 2"
FT                   /id="PRO_0000309590"
FT   DOMAIN          62..282
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   BINDING         76
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         80
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         83
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   354 AA;  40377 MW;  9B2804F7AC21D403 CRC64;
     MQFSPVVASP KLLLQLCIST LHCIMASIIS TVCYWTAGAC KGTTSPVPPV DSNLDQRKVQ
     NAMTPTSVNY HFTRKCNYKC GFCFHTAKTS FVLPLEEAKR GLKLLKESGM EKINFSGGEP
     FLHEKGEFLG KLVQFCKLDL QLPSVSIVSN GSMIKEKWFQ KYGDYLDILA ISCDSFDEAT
     NQLIGRTQGR KSHVDNLHKI RNWCQQYKVA FKINSVINTF NMDEDMTEPI TQLNPVRWKV
     FQCLLIDGEN AGEEALREAE RFVISDQLFQ EFLDRHSSIS CLVPESNEKM RNSYLILDEY
     MRFLDCRAGR KDPSKSILDV GVKDAISFSG FDEKMFLKRG GKYVWSKANM KLQW