ID RSAD2_DANRE Reviewed; 359 AA.
AC Q5RH95; A0FJI6;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE RecName: Full=S-adenosylmethionine-dependent nucleotide dehydratase RSAD2 {ECO:0000303|PubMed:36387278};
DE Short=SAND {ECO:0000303|PubMed:36387278};
DE AltName: Full=Radical S-adenosyl methionine domain-containing protein 2;
DE AltName: Full=Virus inhibitory protein, endoplasmic reticulum-associated, interferon-inducible;
DE Short=Viperin;
GN Name=rsad2 {ECO:0000312|ZFIN:ZDB-GENE-050913-129};
GN Synonyms=vig1 {ECO:0000312|EMBL:ABJ97316.1};
GN ORFNames=si:ch211-276e8.2, zgc:112342;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABJ97316.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX PubMed=17371995; DOI=10.4049/jimmunol.178.7.4385;
RA Levraud J.-P., Boudinot P., Colin I., Benmansour A., Peyrieras N.,
RA Herbomel P., Lutfalla G.;
RT "Identification of the zebrafish IFN receptor: implications for the origin
RT of the vertebrate IFN system.";
RL J. Immunol. 178:4385-4394(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3] {ECO:0000312|EMBL:CAI11967.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NOMENCLATURE.
RX PubMed=36387278; DOI=10.3389/fmolb.2022.1032220;
RA Ji Y., Wei L., Da A., Stark H., Hagedoorn P.-L., Ciofi-Baffoni S.,
RA Cowley S.A., Louro R.O., Todorovic S., Mroginski M.A., Nicolet Y.,
RA Roessler M.M., Le Brun N.E., Piccioli M., James W.S., Hagen W.R.,
RA Ebrahimi K.H.;
RT "Radical-SAM dependent nucleotide dehydratase (SAND), rectification of the
RT names of an ancient iron-sulfur enzyme using NC-IUBMB recommendations.";
RL Front. Mol. Biosci. 9:0-0(2022).
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 -!- INDUCTION: By interferon type I, type II and LPS. Induced by infection
CC with spring viremia of carp virus, presumably through type I interferon
CC pathway. {ECO:0000269|PubMed:17371995}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. RSAD2 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABJ97316.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; EF014961; ABJ97316.1; ALT_INIT; mRNA.
DR EMBL; BX571665; CAI11967.1; -; Genomic_DNA.
DR EMBL; BC096889; AAH96889.1; -; mRNA.
DR RefSeq; NP_001020727.1; NM_001025556.1.
DR AlphaFoldDB; Q5RH95; -.
DR SMR; Q5RH95; -.
DR STRING; 7955.ENSDARP00000015681; -.
DR PaxDb; 7955-ENSDARP00000015681; -.
DR GeneID; 570456; -.
DR KEGG; dre:570456; -.
DR AGR; ZFIN:ZDB-GENE-050913-129; -.
DR CTD; 91543; -.
DR ZFIN; ZDB-GENE-050913-129; rsad2.
DR eggNOG; ENOG502QQMH; Eukaryota.
DR HOGENOM; CLU_049058_2_1_1; -.
DR InParanoid; Q5RH95; -.
DR OMA; ERWFKKY; -.
DR OrthoDB; 3671494at2759; -.
DR PhylomeDB; Q5RH95; -.
DR TreeFam; TF300085; -.
DR PRO; PR:Q5RH95; -.
DR Proteomes; UP000000437; Chromosome 17.
DR Bgee; ENSDARG00000004952; Expressed in spleen and 14 other cell types or tissues.
DR ExpressionAtlas; Q5RH95; differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005811; C:lipid droplet; IEA:InterPro.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0050778; P:positive regulation of immune response; IBA:GO_Central.
DR GO; GO:0009615; P:response to virus; IDA:ZFIN.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR026372; RSAD2.
DR InterPro; IPR007197; rSAM.
DR NCBIfam; TIGR04278; viperin; 1.
DR NCBIfam; NF038283; viperin_w_prok; 1.
DR PANTHER; PTHR21339; RADICAL S-ADENOSYL METHIONINE DOMAIN-CONTAINING PROTEIN 2; 1.
DR PANTHER; PTHR21339:SF0; RADICAL S-ADENOSYL METHIONINE DOMAIN-CONTAINING PROTEIN 2; 1.
DR Pfam; PF13353; Fer4_12; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SFLD; SFLDG01067; SPASM/twitch_domain_containing; 1.
DR SFLD; SFLDF00318; Viperin; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 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 Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..359
FT /note="S-adenosylmethionine-dependent nucleotide
FT dehydratase RSAD2"
FT /id="PRO_0000309588"
FT DOMAIN 67..287
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT REGION 43..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 81
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 85
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 88
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 359 AA; 41475 MW; A56821E369A5B5A4 CRC64;
MVTSNQLGFA RLLMQLCVKN VQSFFLALLR WLSMQVSGAH VQQTPARKIS RPESRTSKQK
EGSRAPFTTP SSVNYHFTRQ CNYKCGFCFH TAKTSFVLPI EEAKRGLRLL KEAGMEKINF
SGGEPFVHQK GSFLGELVLY CKQELQLPSV SIVSNGSLIR ESWFQKYGDY LDILAISCDS
FIEETNQLIG RAQGRKSHLD NLHKVRNWCR EYKVAFKINS VINTYNVEED MTEQITALNP
VRWKVFQCLL IEGENAGENS LREAEKFVIS DQQFQDFLER HQSIQCLVPE SNQKMRDSYL
ILDEYMRFLD CREGRKDPSK SILDVGVEEA IKFSGFDEKM FLMRGGKYVW SKADMKLEW
//
