SLN14_MOUSE
ID SLN14_MOUSE Reviewed; 899 AA.
AC V9GXG1;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Protein SLFN14 {ECO:0000305};
DE Contains:
DE RecName: Full=C-terminally truncated SLFN14 endoribonuclease {ECO:0000305};
DE EC=3.1.-.- {ECO:0000250|UniProtKB:G1SRW8};
DE AltName: Full=Schlafen family member 14 {ECO:0000312|MGI:MGI:2684866};
GN Name=Slfn14 {ECO:0000312|MGI:MGI:2684866};
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 [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 [2]
RP TISSUE SPECIFICITY.
RX PubMed=19619625; DOI=10.1016/j.gene.2009.07.006;
RA Bustos O., Naik S., Ayers G., Casola C., Perez-Lamigueiro M.A.,
RA Chippindale P.T., Pritham E.J., de la Casa-Esperon E.;
RT "Evolution of the Schlafen genes, a gene family associated with embryonic
RT lethality, meiotic drive, immune processes and orthopoxvirus virulence.";
RL Gene 447:1-11(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION, AND ASSOCIATION WITH RIBOSOMES.
RX PubMed=25996083; DOI=10.1021/acs.biochem.5b00302;
RA Pisareva V.P., Muslimov I.A., Tcherepanov A., Pisarev A.V.;
RT "Characterization of novel ribosome-associated endoribonuclease SLFN14 from
RT rabbit reticulocytes.";
RL Biochemistry 54:3286-3301(2015).
CC -!- FUNCTION: [Protein SLFN14]: Shows no ribosome-associated and
CC endoribonuclease activities. {ECO:0000269|PubMed:25996083}.
CC -!- FUNCTION: [C-terminally truncated SLFN14 endoribonuclease]: Displays
CC polysome-associated endoribonuclease activity towards mRNAs and rRNAs
CC (PubMed:25996083). May play a role in RNA surveillance pathways by
CC recognizing stalled ribosomes and triggering endonucleolytic cleavage
CC of aberrant mRNAs (Probable). Cleaves different types of rRNAs and
CC mRNAs in a magnesium- and manganese-dependent and ATP-independent
CC manner. Involved in correct maturation of megakaryocytes and especially
CC important for proplatelet extension (By similarity).
CC {ECO:0000250|UniProtKB:G1SRW8, ECO:0000250|UniProtKB:P0C7P3,
CC ECO:0000269|PubMed:25996083, ECO:0000305|PubMed:25996083}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:G1SRW8};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:G1SRW8};
CC Note=C-terminally truncated SLFN14 endoribonuclease: Requires manganese
CC and magnesium for its endoribonuclease activity.
CC {ECO:0000250|UniProtKB:G1SRW8};
CC -!- SUBUNIT: [C-terminally truncated SLFN14 endoribonuclease]: Associates
CC with ribosomes in an ATP-independent manner (PubMed:25996083).
CC {ECO:0000269|PubMed:25996083}.
CC -!- SUBCELLULAR LOCATION: [Protein SLFN14]: Nucleus
CC {ECO:0000250|UniProtKB:P0C7P3}.
CC -!- TISSUE SPECIFICITY: Expressed in spleen (PubMed:19619625).
CC {ECO:0000269|PubMed:19619625}.
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DR EMBL; AL603711; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS70269.1; -.
DR RefSeq; NP_001159500.1; NM_001166028.1.
DR AlphaFoldDB; V9GXG1; -.
DR SMR; V9GXG1; -.
DR STRING; 10090.ENSMUSP00000139132; -.
DR iPTMnet; V9GXG1; -.
DR PhosphoSitePlus; V9GXG1; -.
DR PRIDE; V9GXG1; -.
DR ProteomicsDB; 257199; -.
DR Antibodypedia; 43976; 73 antibodies from 18 providers.
DR Ensembl; ENSMUST00000163961; ENSMUSP00000139132; ENSMUSG00000082101.
DR GeneID; 237890; -.
DR KEGG; mmu:237890; -.
DR UCSC; uc011ybg.1; mouse.
DR CTD; 342618; -.
DR MGI; MGI:2684866; Slfn14.
DR VEuPathDB; HostDB:ENSMUSG00000082101; -.
DR eggNOG; ENOG502QWKG; Eukaryota.
DR GeneTree; ENSGT00410000025651; -.
DR HOGENOM; CLU_007071_0_0_1; -.
DR OMA; FQVHHAD; -.
DR OrthoDB; 211385at2759; -.
DR PhylomeDB; V9GXG1; -.
DR BioGRID-ORCS; 237890; 1 hit in 67 CRISPR screens.
DR PRO; PR:V9GXG1; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; V9GXG1; protein.
DR Bgee; ENSMUSG00000082101; Expressed in bone marrow and 13 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
DR GO; GO:0071286; P:cellular response to magnesium ion; ISS:UniProtKB.
DR GO; GO:0071287; P:cellular response to manganese ion; ISS:UniProtKB.
DR GO; GO:0006402; P:mRNA catabolic process; IDA:UniProtKB.
DR GO; GO:0036345; P:platelet maturation; ISS:UniProtKB.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IDA:UniProtKB.
DR GO; GO:0016075; P:rRNA catabolic process; IDA:UniProtKB.
DR Gene3D; 3.30.950.30; -; 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; IPR029677; SLFN14.
DR PANTHER; PTHR12155; PTHR12155; 1.
DR PANTHER; PTHR12155:SF30; PTHR12155:SF30; 1.
DR Pfam; PF04326; AlbA_2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Endonuclease; Hydrolase; Nuclease; Nucleus; Reference proteome.
FT CHAIN 1..899
FT /note="Protein SLFN14"
FT /id="PRO_0000436154"
FT CHAIN 1..?
FT /note="C-terminally truncated SLFN14 endoribonuclease"
FT /id="PRO_0000436155"
FT REGION 195..382
FT /note="Required for endoribonuclease activity"
FT /evidence="ECO:0000250|UniProtKB:P0C7P3"
FT REGION 383..562
FT /note="Required for ribosome binding"
FT /evidence="ECO:0000250|UniProtKB:P0C7P3"
SQ SEQUENCE 899 AA; 101690 MW; 3AF7738155B2DE04 CRC64;
MPYAEITVNL GKVTLGEENR KKMTNSCLKR HENSSLVQAV CALLNSGGGV IKAEINDKSY
SYRCHGLGQD LETSFQKLLP SGSQKHLDYM QQNHDLLIFV KSWSPDASSL PLRICSLRSN
LYQRDVTSAI NLCANGALEL LREKESRAQR GTPRLHSQDH ILNRTIQEEE DIKMCALEFL
KKDKLNFKEK LSFTESTHVE FKRFTTKKIV PRIKETLAHY VSAFANTQGG YIIIGVDDKS
KEVFGCKKEK VNPDSLKTEI KNCIEKLPTY HFCREKPKVN FTTKILKVYQ KEALYGFVCV
VQVEPFCCVV FAEDPDSWIM ENNIVTRLKV QQWVEMMLDI QSDPSSGFPT INDSAHLMTP
ALSAPRRPAY LTKVLEHKET LQRHFFSVTQ ENLQFQPESL CKKLFSDHEG LEDLLKAQTH
PCSHGIVIFS RSWAGDIGLM REEKVLCDAL LVAVGSPLVL YTILTDPSST GRADYTQNTA
LQLKRQLQTL GGYPGKICVI PRVIYLASRG SRPDQPPVYY PRPYTLSSKA EVEDLLQGLV
LVSLCSRSVL SDQLGCEFFK QCLEEQANTL SRNLQESREL FIHCLPGTRK TALAIKMVEK
IKDVFHCKPK EILFVCENDS LRDFVMQQVT CRAVTRRTFM REEFPKIKHI VMDETENFCS
RHGDWYVKAK STTHPKANGA ANEHPHHGIL WLFLDPFQVR HADGSGLPVP SAQFPRKMIT
SEIHCAVEIA KVMKDEMKRM QENPPSMGLP DTLATFQEAP YEEAMRAGAL PGVCEIKANL
TPEQIANYVA EKCHSLFHEG YLPQDIAILY RRREDRGQYK DVLLKAMARG TTEVAFNSAA
DVCADGIILD SVEQFSGMVR NIVFGLCPES VHSEGVHKLC FASKAIKHLY LLYGGRTAF
