SLFN9_MOUSE
ID SLFN9_MOUSE Reviewed; 910 AA.
AC B1ARD6; A0A0A0MQG6; Q7TME8; Q7TME9; Q80VG8; Q8C7F7; Q8CB82;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Schlafen family member 9 {ECO:0000305};
DE EC=3.1.-.- {ECO:0000250|UniProtKB:Q5U311};
DE AltName: Full=Schlafen-9 {ECO:0000303|PubMed:15351786};
GN Name=Slfn9 {ECO:0000303|PubMed:15351786, ECO:0000312|MGI:MGI:2445121};
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone, and Liver;
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]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 95-910.
RC STRAIN=Swiss Webster;
RA Tiong J.D.R., Byars-Baker C., Wray S.;
RT "Mouse embryonic cDNA isolated from nasal region after differential screen
RT of nose, tail and limb.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Endoribonuclease that cleaves tRNAs and rRNAs.
CC {ECO:0000250|UniProtKB:Q5U311}.
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. Induced in response to LPS and
CC interferon. {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 -!- SIMILARITY: Belongs to the Schlafen family. Subgroup III subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AL603745; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY261800; AAP30070.1; -; mRNA.
DR EMBL; AY261801; AAP30071.1; -; mRNA.
DR EMBL; AK036579; BAC29489.1; -; mRNA.
DR EMBL; AK050355; BAC34206.2; -; mRNA.
DR EMBL; AL603745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY217035; AAO60168.1; -; mRNA.
DR CCDS; CCDS25154.1; -.
DR RefSeq; NP_766384.2; NM_172796.2.
DR RefSeq; XP_006533298.1; XM_006533235.3.
DR AlphaFoldDB; B1ARD6; -.
DR SMR; B1ARD6; -.
DR IntAct; B1ARD6; 1.
DR STRING; 10090.ENSMUSP00000044435; -.
DR iPTMnet; B1ARD6; -.
DR PhosphoSitePlus; B1ARD6; -.
DR MaxQB; B1ARD6; -.
DR PaxDb; B1ARD6; -.
DR PeptideAtlas; B1ARD6; -.
DR PRIDE; B1ARD6; -.
DR ProteomicsDB; 331264; -.
DR ProteomicsDB; 355173; -.
DR DNASU; 237886; -.
DR Ensembl; ENSMUST00000038211; ENSMUSP00000044435; ENSMUSG00000069793.
DR Ensembl; ENSMUST00000092840; ENSMUSP00000090515; ENSMUSG00000069793.
DR GeneID; 237886; -.
DR KEGG; mmu:237886; -.
DR UCSC; uc007kob.1; mouse.
DR UCSC; uc007koc.1; mouse.
DR CTD; 237886; -.
DR MGI; MGI:2445121; Slfn9.
DR VEuPathDB; HostDB:ENSMUSG00000069793; -.
DR eggNOG; ENOG502QWKG; Eukaryota.
DR GeneTree; ENSGT00410000025651; -.
DR HOGENOM; CLU_007071_0_0_1; -.
DR InParanoid; B1ARD6; -.
DR OMA; TKQQGSC; -.
DR OrthoDB; 211385at2759; -.
DR PhylomeDB; B1ARD6; -.
DR TreeFam; TF337168; -.
DR BioGRID-ORCS; 237886; 3 hits in 71 CRISPR screens.
DR PRO; PR:B1ARD6; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; B1ARD6; protein.
DR Bgee; ENSMUSG00000069793; Expressed in dorsal pancreas and 142 other tissues.
DR ExpressionAtlas; B1ARD6; baseline and differential.
DR Genevisible; Q8CB82; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA: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; ISO:MGI.
DR GO; GO:0000049; F:tRNA binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0051607; P:defense response to virus; IBA:GO_Central.
DR GO; GO:0016075; P:rRNA catabolic process; ISO:MGI.
DR GO; GO:0016078; P:tRNA catabolic process; ISO:MGI.
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; Magnesium; Metal-binding;
KW Nuclease; Nucleotide-binding; Reference proteome; Zinc.
FT CHAIN 1..910
FT /note="Schlafen family member 9"
FT /id="PRO_0000444608"
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 140
FT /note="V -> G (in Ref. 1; AAP30071)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="P -> S (in Ref. 1; AAP30071)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="L -> F (in Ref. 1; AAP30071)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="S -> A (in Ref. 1; AAP30071)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="Q -> R (in Ref. 1; AAP30071)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="Y -> H (in Ref. 2; BAC34206)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="V -> F (in Ref. 2; BAC29489)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="K -> E (in Ref. 2; BAC34206)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="R -> H (in Ref. 1; AAP30071)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="Y -> H (in Ref. 1; AAP30071)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="K -> N (in Ref. 1; AAP30071)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="R -> C (in Ref. 1; AAP30071)"
FT /evidence="ECO:0000305"
FT CONFLICT 523..528
FT /note="NKTSGG -> IETSGS (in Ref. 1; AAP30071)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="G -> D (in Ref. 1; AAP30071)"
FT /evidence="ECO:0000305"
FT CONFLICT 558
FT /note="L -> F (in Ref. 2; BAC29489)"
FT /evidence="ECO:0000305"
FT CONFLICT 573..574
FT /note="VL -> IV (in Ref. 1; AAP30071)"
FT /evidence="ECO:0000305"
FT CONFLICT 674
FT /note="N -> D (in Ref. 1; AAP30071)"
FT /evidence="ECO:0000305"
FT CONFLICT 796
FT /note="K -> R (in Ref. 1; AAP30071)"
FT /evidence="ECO:0000305"
FT CONFLICT 843
FT /note="E -> A (in Ref. 1; AAP30070/AAP30071)"
FT /evidence="ECO:0000305"
FT CONFLICT 904
FT /note="Q -> H (in Ref. 1; AAP30070/AAP30071)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 910 AA; 103992 MW; F05ECEFD4763FD92 CRC64;
METYLSLVVK RSYPDLIIYA GEVTLGEKVR NKKDSKKRKL EKTRITQAAC ALLNSGGGVI
VIQMANQSEQ PERMGQDLET SLRNLIPSLD LQAFFETKQQ EDKFYIFVKS WSSSPEDDST
KPRICSLGTS LYCRSLTSKV AMDSRDAFYF LKKKKAYIKC SPTDDRAPPA KIPRTMSQKS
LESNPAFEIF QSKKLEYGQR LLFSESTSIE FKQFDTENAQ KYMKDIIPEY ISAFANTQGG
YLFIGVDDKS IILGCPKDNV DPDSLKIVAN EAISKLPVFH FCSSKDKNKV SYETRVIDVF
QEGNLYGYLC VIKVEPFCCA VFSEAPISWM VDKEKGVYTL NTEEWVRMMV DVGPEAASND
LSRDFECQLS LSDSPPHCRP VYSKKGLEHK VDLQQRLFQV SPDCLKYTPE SLWSELCSQH
ERLEDLVKQQ IRSFSCGLLI LSRSWAVDLN LEEKQEVICD ALLIAQNSPP ILYTILGEQD
EQGQDYCTRT AFTLKQKLVN TGGYTGRVCV MTKVLCLSSQ NNNKTSGGSV SPIDYPSSYN
LANIQEMQGL LQALVIVLLN FRSFLSDQLG CEVLNLLTAQ QYEILSKSLR KTRELFVHGL
PGSGKTIIAM KIMEKIRNTF HCETDRILYI CENQPLRDFI QAKNICQAVT RKTFMNYKFK
TERFQHIIID EAQNFRTEDG NWYEKAKGIT RGMKNCPGIL WIFLDYFQTS HLQESGLPDF
SLQYPKEELT QVVRNADKIA EFLQQELQKI RDNPPCSIPQ ESLNILHEFK WSQGVSGTYE
ITYLTLEKMV SYITDKCDVF LSKGYSPQDI AVLFSTDREK KAYEHMFLRE MRKRRRASHM
NDESVCHSNM FDSIRRFSGL ERSIVFGINP IATEQPISHN LLLCLASRAM KHLYILYLST
PEGQSSMVAC