SLN14_RABIT
ID SLN14_RABIT Reviewed; 915 AA.
AC G1SRW8;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 2.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Protein SLFN14 {ECO:0000305};
DE Contains:
DE RecName: Full=C-terminally truncated SLFN14 endoribonuclease {ECO:0000305};
DE EC=3.1.-.- {ECO:0000269|PubMed:25996083};
DE AltName: Full=Schlafen family member 14 {ECO:0000250|UniProtKB:P0C7P3};
GN Name=SLFN14 {ECO:0000250|UniProtKB:P0C7P3};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke;
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke;
RG The Genome Sequencing Platform;
RA Di Palma F., Heiman D., Young S., Gnerre S., Johnson J., Lander E.S.,
RA Lindblad-Toh K.;
RT "Genome Sequence of Oryctolagus cuniculus (European rabbit).";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, COFACTOR, ASSOCIATION WITH RIBOSOMES, TISSUE SPECIFICITY, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
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 RNAs in a magnesium-, manganese-
CC dependent and ATP-independent manner (PubMed:25996083). Involved in
CC correct maturation of megakaryocytes and especially important for
CC proplatelet extension (By similarity). {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:0000269|PubMed:25996083};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:25996083};
CC Note=C-terminally truncated SLFN14 endoribonuclease: Requires manganese
CC and magnesium for its endoribonuclease activity.
CC {ECO:0000269|PubMed:25996083};
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: [C-terminally truncated SLFN14 endoribonuclease]:
CC Detected in reticulocytes (at protein level) (PubMed:25996083).
CC {ECO:0000269|PubMed:25996083}.
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DR EMBL; AAGW02039188; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_008269350.1; XM_008271128.2.
DR AlphaFoldDB; G1SRW8; -.
DR SMR; G1SRW8; -.
DR STRING; 9986.ENSOCUP00000005950; -.
DR PRIDE; G1SRW8; -.
DR Ensembl; ENSOCUT00000006881; ENSOCUP00000005950; ENSOCUG00000006884.
DR GeneID; 100358198; -.
DR KEGG; ocu:100358198; -.
DR CTD; 342618; -.
DR eggNOG; ENOG502QWKG; Eukaryota.
DR GeneTree; ENSGT00410000025651; -.
DR HOGENOM; CLU_007071_0_0_1; -.
DR InParanoid; G1SRW8; -.
DR OMA; FQVHHAD; -.
DR OrthoDB; 211385at2759; -.
DR TreeFam; TF337168; -.
DR Proteomes; UP000001811; Chromosome 19.
DR Bgee; ENSOCUG00000006884; Expressed in blood and 5 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; IDA:UniProtKB.
DR GO; GO:0071287; P:cellular response to manganese ion; IDA: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; 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.
PE 1: Evidence at protein level;
KW Endonuclease; Hydrolase; Nuclease; Nucleus; Reference proteome.
FT CHAIN 1..915
FT /note="Protein SLFN14"
FT /id="PRO_0000436156"
FT CHAIN 1..?
FT /note="C-terminally truncated SLFN14 endoribonuclease"
FT /id="PRO_0000436157"
FT REGION 157..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..389
FT /note="Required for endoribonuclease activity"
FT /evidence="ECO:0000250|UniProtKB:P0C7P3"
FT REGION 390..569
FT /note="Required for ribosome binding"
FT /evidence="ECO:0000250|UniProtKB:P0C7P3"
SQ SEQUENCE 915 AA; 103736 MW; CAA7C1862AAF7292 CRC64;
MEIPKTGVET LYPEFVVEVG RVTFGEENRK KMTNSCLKRT ENLNIIKATC ALLNSGGGVI
KAEIHDKNYN YQCHGLGHDL ETSFQKLLPF GSQKYLDYMQ QGHELLIFVK SWNPDVSSLL
PLRICSLRSN LYQRDVTSAI NLSASSALEL LREKQHAAQR GRRRLHPPRA SNSNLQEEED
MKMLASEVFK KDRLMYKEKL NFTESTHVEF KRFTTKKVVP RIKEMLPHYV SAFANTQGGY
LIIGVDDKSK EVFGCKKEKV NPDLLKKEIE NCIEKLPTFH FCHEKPKINF ITKILNVYQK
DVLYGYVCVV QVEPFCCAVF AEAPDSWVMR DNAATRLTAE DWVLMMLDIP SAPCNLVTDS
NAHLKSPASS AFRSPVCPTK VLEFKGALQR HLFPVTQKTI QFKPESFCKK LFSDHKGLED
LMKTQTYPYS QGIVVFSRSW AGDVGLRKED RVLCDALLIA LHSPLVLYTV LIDPSWAGGR
EYAWNVALHL KRKLQSVGGY PGKVGIIPRL IQLAGTWCGP GDGSVHYPQS YQLATEDDME
DLLQALVVVS LCSRSLLSDQ LGCEFFNLLI AEQCEVLSQS LQETRELFIH CFPGTRKTAL
AIKTLEKIRD LFRCRPKEIL YVCESDFLRD FVIHQTACLA VTRKTFMQGE FPKIKHIVMD
ETENFCSKYG DWYSKARSIT HPRVRGAGNE DLHHGILWIF LDPFQVRHSD VNGLPPPPAQ
FPRKTITNGI HCAQEIAKVM KGAMKRITEN PPSNMSPHTL ALFREAACGE ALGAHALPGV
CETKADLTVE QIANYVAERC HGLFQCGYLP KDVAILCRRE EDRARYKLAL LRAMELTETH
SATEVVFSQA AGVQGEHIIL DSVHQFSGLH RNIVFGLSPE QRLSEEFHQL CFASKAIKHL
YLLYERGQVS ENYYK
