SLFN8_MOUSE
ID SLFN8_MOUSE Reviewed; 910 AA.
AC B1ARD8; A0A0A0MQG0; F6RTS1; Q3UBN9; Q7TMF1;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Schlafen family member 8 {ECO:0000305};
DE EC=3.1.-.- {ECO:0000269|PubMed:29563550};
DE AltName: Full=Schlafen-8 {ECO:0000303|PubMed:15351786};
DE Short=mSLFN8 {ECO:0000303|PubMed:29563550};
GN Name=Slfn8 {ECO:0000303|PubMed:15351786, ECO:0000312|MGI:MGI:2672859};
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]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=129/SvJ, and C57BL/6J;
RX PubMed=15351786; DOI=10.1093/intimm/dxh155;
RA Geserick P., Kaiser F., Klemm U., Kaufmann S.H.E., Zerrahn J.;
RT "Modulation of T cell development and activation by novel members of the
RT Schlafen (slfn) gene family harbouring an RNA helicase-like motif.";
RL Int. Immunol. 16:1535-1548(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 108-910.
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29528433; DOI=10.1093/intimm/dxx079;
RA Nakagawa K., Matsuki T., Zhao L., Kuniyoshi K., Tanaka H., Ebina I.,
RA Yoshida K.J., Nabeshima H., Fukushima K., Kanemaru H., Yamane F.,
RA Kawasaki T., Machida T., Naito H., Takakura N., Satoh T., Akira S.;
RT "Schlafen-8 is essential for lymphatic endothelial cell activation in
RT experimental autoimmune encephalomyelitis.";
RL Int. Immunol. 30:69-78(2018).
RN [5]
RP FUNCTION.
RX PubMed=29563550; DOI=10.1038/s41467-018-03544-x;
RA Yang J.Y., Deng X.Y., Li Y.S., Ma X.C., Feng J.X., Yu B., Chen Y.,
RA Luo Y.L., Wang X., Chen M.L., Fang Z.X., Zheng F.X., Li Y.P., Zhong Q.,
RA Kang T.B., Song L.B., Xu R.H., Zeng M.S., Chen W., Zhang H., Xie W.,
RA Gao S.;
RT "Structure of Schlafen13 reveals a new class of tRNA/rRNA- targeting RNase
RT engaged in translational control.";
RL Nat. Commun. 9:1165-1165(2018).
CC -!- FUNCTION: Endoribonuclease that cleaves tRNAs and rRNAs
CC (PubMed:29563550). Cleaves tRNAs 11 nucleotides from the 3'-terminus at
CC the acceptor stem (PubMed:29563550). May be involved in immune system
CC via regulation of inflammation (PubMed:29528433).
CC {ECO:0000269|PubMed:29528433, ECO:0000269|PubMed:29563550}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q5U311};
CC Note=Can also use Mn(2+). {ECO:0000250|UniProtKB:Q5U311};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q68D06}.
CC -!- TISSUE SPECIFICITY: In T-cells, expressed at relatively constant levels
CC during development: expressed in immature CD3(-)CD4(-)CD8(-) T-cells
CC (DN stage), in CD4(+)CD8(+) double-positive stage (DP) and mature
CC CD4(+) or CD8(+) thymocytes. Expression is slightly reduced at the DP
CC stage. {ECO:0000269|PubMed:15351786}.
CC -!- INDUCTION: Induced following infection. {ECO:0000269|PubMed:15351786}.
CC -!- DOMAIN: Shows a pseudo-dimeric U-pillow-shaped architecture of the
CC SLFN13 N'-domain that may clamp base-paired RNAs.
CC {ECO:0000250|UniProtKB:Q5U311}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype in normal conditions. Mice
CC are resistant in experimental autoimmune encephalomyelitis (EAE) model,
CC a T-cell-mediated autoimmune model. The expression of pro-inflammatory
CC mediators is severely reduced in EAE. No dysfunction of T-cells, or
CC other leukocytes is detected. {ECO:0000269|PubMed:29528433}.
CC -!- SIMILARITY: Belongs to the Schlafen family. Subgroup III subfamily.
CC {ECO:0000305}.
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DR EMBL; AY261798; AAP30068.1; -; mRNA.
DR EMBL; AL603745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK150875; BAE29925.1; -; mRNA.
DR CCDS; CCDS25155.1; -.
DR RefSeq; NP_853523.2; NM_181545.4.
DR RefSeq; XP_006533547.1; XM_006533484.3.
DR AlphaFoldDB; B1ARD8; -.
DR SMR; B1ARD8; -.
DR STRING; 10090.ENSMUSP00000040060; -.
DR iPTMnet; B1ARD8; -.
DR PhosphoSitePlus; B1ARD8; -.
DR PaxDb; B1ARD8; -.
DR PeptideAtlas; B1ARD8; -.
DR PRIDE; B1ARD8; -.
DR ProteomicsDB; 340832; -.
DR ProteomicsDB; 352912; -.
DR ProteomicsDB; 371565; -.
DR DNASU; 276950; -.
DR Ensembl; ENSMUST00000038141; ENSMUSP00000040060; ENSMUSG00000035208.
DR Ensembl; ENSMUST00000092838; ENSMUSP00000090513; ENSMUSG00000035208.
DR GeneID; 276950; -.
DR KEGG; mmu:276950; -.
DR UCSC; uc007kod.2; mouse.
DR CTD; 276950; -.
DR MGI; MGI:2672859; Slfn8.
DR VEuPathDB; HostDB:ENSMUSG00000035208; -.
DR eggNOG; ENOG502QWKG; Eukaryota.
DR GeneTree; ENSGT00410000025651; -.
DR HOGENOM; CLU_034558_0_0_1; -.
DR InParanoid; B1ARD8; -.
DR OMA; ACMIRVK; -.
DR OrthoDB; 211385at2759; -.
DR PhylomeDB; B1ARD8; -.
DR TreeFam; TF337168; -.
DR BioGRID-ORCS; 276950; 2 hits in 69 CRISPR screens.
DR PRO; PR:B1ARD8; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; B1ARD8; protein.
DR Bgee; ENSMUSG00000035208; Expressed in spleen and 45 other tissues.
DR ExpressionAtlas; B1ARD8; baseline and differential.
DR Genevisible; Q7TMF1; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0090734; C:site of DNA damage; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:MGI.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IBA:GO_Central.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0016075; P:rRNA catabolic process; IDA:UniProtKB.
DR GO; GO:0016078; P:tRNA catabolic process; IDA:UniProtKB.
DR Gene3D; 3.30.950.30; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029684; Schlafen.
DR InterPro; IPR007421; Schlafen_AlbA_2_dom.
DR InterPro; IPR038461; Schlafen_AlbA_2_dom_sf.
DR InterPro; IPR018647; SLFN_3-like_DNA/RNA_helicase.
DR InterPro; IPR027785; UvrD-like_helicase_C.
DR PANTHER; PTHR12155; PTHR12155; 1.
DR Pfam; PF04326; AlbA_2; 1.
DR Pfam; PF09848; DUF2075; 1.
DR Pfam; PF13538; UvrD_C_2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Endonuclease; Hydrolase; Immunity; Magnesium;
KW Metal-binding; Nuclease; Nucleotide-binding; Reference proteome; Zinc.
FT CHAIN 1..910
FT /note="Schlafen family member 8"
FT /id="PRO_0000444607"
FT REGION 1..354
FT /note="N'-domain region"
FT /evidence="ECO:0000250|UniProtKB:Q5U311"
FT ACT_SITE 205
FT /evidence="ECO:0000250|UniProtKB:Q5U311"
FT ACT_SITE 210
FT /evidence="ECO:0000250|UniProtKB:Q5U311"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q5U311"
FT BINDING 282
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q5U311"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q5U311"
FT BINDING 599..606
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 191
FT /note="Q -> R (in Ref. 3; BAE29925)"
FT /evidence="ECO:0000305"
FT CONFLICT 899
FT /note="S -> P (in Ref. 1; AAP30068)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 910 AA; 104264 MW; CEB49E7AA3F48CAE CRC64;
METHPSLAVK WSCPDLTIYA GEVTIGEEDR NKMDSKKRKL EKTRITEAAC ALLNSGGGLI
AMQMTNKSEH PVEMGQDLEK SLRELIMSPN MQAFFETKQQ EDQFYIFVKS WSCRPEDGST
KPRICSLGSS LYCRSITSKV AMDSREAFEF LKDKKACIKY RPTDDGAPPA KIPRAMCQNS
LESNPAFEIF QSKKLEYGQC LLFSESTSIE FKQFSTKHVQ AYMKNIIPEY ISAFANTQGG
YLFIGVDDKR IILGCPKDNV DRDSLKTVAN ETISKVPVFH FCSSKDKDKV SYETRVIDVF
QEGNLYGYLC VIKVEPFCCA VFSEAPISWM VDKEKGVYRL NTEEWVRMMV DFGPEASSKD
LSKDFECQLS LCNSPPHCRP VYSKKGLQHK VDLQQRLFQV SPDCLKYTPE SLWKELCSQH
KRLKGLVKQQ IRSFSCGLLI LYRSWAVDLN LKEKQEVICD ALLIAQNSPP ILYTILGEQD
EQGQDYCNHT AFTLKQKLVN TGGYTGRVCV MTKVLCLSSQ NNIETNGGSV SPINYPSSYN
LANIQEMQDL LQALVIVLLN FRSFLSDQLG CEILNLLTAQ QYEILSKSLR KTRELFVHGL
PGSGKTIIAM KIMEKIRNTF HCETDSILYI CENQPLRDFI RAKRICQAVT RKTFMNYRFK
TNSFQHIIVD EAQNFRTEDG NWYGKAKAIS RRVKSCPGMF WIFLDYFQTS HLKESGLPDF
SRQYPREELT QVVRNGDKIA EFLQKELQKI RDNPPCSIPR QSLNIVHEFK WSQSVSGNIK
TEQFTLEDMV IYVADKCYDF LRKGYSLQDI AVLFSTDKEK KTYESMFLGE MRKRRRASEM
NHAYLCDSNM FDSIRRFSGL ERSIVFGINP IATEQPISHN LLLCLASRAM KHLYILYFST
PEGHSSTEAC
