SND1_MOUSE
ID SND1_MOUSE Reviewed; 910 AA.
AC Q78PY7; Q3TT46; Q922L5; Q9R0S1;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Staphylococcal nuclease domain-containing protein 1;
DE EC=3.1.31.1 {ECO:0000250|UniProtKB:Q7KZF4};
DE AltName: Full=100 kDa coactivator;
DE AltName: Full=p100 co-activator;
GN Name=Snd1;
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].
RA Tsuchiya N., Fukuda H., Yamaguchi A., Sugimura T., Nagao M., Nakagama H.;
RT "Cloning and characterization of a cDNA encoding a mouse p100 co-
RT activator.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Pituitary, and Thymus;
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 MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, AND INTERACTION WITH STAT5.
RX PubMed=12819296; DOI=10.1210/me.2002-0256;
RA Paukku K., Yang J., Silvennoinen O.;
RT "Tudor and nuclease-like domains containing protein p100 function as
RT coactivators for signal transducer and activator of transcription 5.";
RL Mol. Endocrinol. 17:1805-1814(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-909, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-235; SER-426 AND SER-909, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-641, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [8]
RP INTERACTION WITH AGO2 AND SYT11.
RX PubMed=24882364; DOI=10.1016/j.febslet.2014.05.031;
RA Milochau A., Lagree V., Benassy M.N., Chaignepain S., Papin J.,
RA Garcia-Arcos I., Lajoix A., Monterrat C., Coudert L., Schmitter J.M.,
RA Ochoa B., Lang J.;
RT "Synaptotagmin 11 interacts with components of the RNA-induced silencing
RT complex RISC in clonal pancreatic beta-cells.";
RL FEBS Lett. 588:2217-2222(2014).
CC -!- FUNCTION: Endonuclease that mediates miRNA decay of both protein-free
CC and AGO2-loaded miRNAs (By similarity). As part of its function in
CC miRNA decay, regulates mRNAs involved in G1-to-S phase transition (By
CC similarity). Functions as a bridging factor between STAT6 and the basal
CC transcription factor (By similarity). Plays a role in PIM1 regulation
CC of MYB activity (By similarity). Functions as a transcriptional
CC coactivator for STAT5 (PubMed:12819296). {ECO:0000250|UniProtKB:Q7KZF4,
CC ECO:0000269|PubMed:12819296}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-
CC phosphooligonucleotide end-products.; EC=3.1.31.1;
CC Evidence={ECO:0000250|UniProtKB:Q7KZF4};
CC -!- SUBUNIT: Forms a ternary complex with STAT6 and POLR2A (By similarity).
CC Associates with the RNA-induced silencing complex (RISC)
CC (PubMed:24882364). Interacts with the RISC components AGO2, FMR1 and
CC TNRC6A. Interacts with GTF2E1 and GTF2E2 (By similarity). Interacts
CC with PIM1 (By similarity). Interacts with STAT5 (PubMed:12819296).
CC Interacts with SYT11 (via C2 2 domain); the interaction with SYT11 is
CC direct (PubMed:24882364). {ECO:0000250|UniProtKB:Q7KZF4,
CC ECO:0000269|PubMed:12819296, ECO:0000269|PubMed:24882364}.
CC -!- INTERACTION:
CC Q78PY7; Q80WJ7: Mtdh; NbExp=4; IntAct=EBI-529864, EBI-774530;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7KZF4}. Nucleus
CC {ECO:0000250|UniProtKB:Q7KZF4}. Melanosome
CC {ECO:0000250|UniProtKB:Q7KZF4}. Note=In IL-4 stimulated cells
CC colocalizes with STAT6 in the nucleus. {ECO:0000250|UniProtKB:Q7KZF4}.
CC -!- PTM: Phosphorylated by PIM1 in vitro. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA84944.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB021491; BAA84944.1; ALT_INIT; mRNA.
DR EMBL; AK088028; BAC40105.1; -; mRNA.
DR EMBL; AK161591; BAE36479.1; -; mRNA.
DR EMBL; BC007126; AAH07126.3; -; mRNA.
DR CCDS; CCDS19953.1; -.
DR RefSeq; NP_062750.2; NM_019776.2.
DR AlphaFoldDB; Q78PY7; -.
DR SMR; Q78PY7; -.
DR BioGRID; 208002; 30.
DR DIP; DIP-32118N; -.
DR IntAct; Q78PY7; 6.
DR MINT; Q78PY7; -.
DR STRING; 10090.ENSMUSP00000001460; -.
DR iPTMnet; Q78PY7; -.
DR PhosphoSitePlus; Q78PY7; -.
DR SwissPalm; Q78PY7; -.
DR EPD; Q78PY7; -.
DR jPOST; Q78PY7; -.
DR MaxQB; Q78PY7; -.
DR PaxDb; Q78PY7; -.
DR PRIDE; Q78PY7; -.
DR ProteomicsDB; 261286; -.
DR Antibodypedia; 1126; 288 antibodies from 32 providers.
DR DNASU; 56463; -.
DR Ensembl; ENSMUST00000001460; ENSMUSP00000001460; ENSMUSG00000001424.
DR GeneID; 56463; -.
DR KEGG; mmu:56463; -.
DR UCSC; uc009bct.1; mouse.
DR CTD; 27044; -.
DR MGI; MGI:1929266; Snd1.
DR VEuPathDB; HostDB:ENSMUSG00000001424; -.
DR eggNOG; KOG2039; Eukaryota.
DR GeneTree; ENSGT00510000047270; -.
DR HOGENOM; CLU_005966_0_0_1; -.
DR InParanoid; Q78PY7; -.
DR OMA; FGQEAHD; -.
DR OrthoDB; 227839at2759; -.
DR PhylomeDB; Q78PY7; -.
DR TreeFam; TF300615; -.
DR BioGRID-ORCS; 56463; 0 hits in 79 CRISPR screens.
DR ChiTaRS; Snd1; mouse.
DR PRO; PR:Q78PY7; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q78PY7; protein.
DR Bgee; ENSMUSG00000001424; Expressed in ectoplacental cone and 262 other tissues.
DR ExpressionAtlas; Q78PY7; baseline and differential.
DR Genevisible; Q78PY7; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0097433; C:dense body; IDA:MGI.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0016442; C:RISC complex; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; ISO:MGI.
DR GO; GO:0004521; F:endoribonuclease activity; ISO:MGI.
DR GO; GO:0004518; F:nuclease activity; IBA:GO_Central.
DR GO; GO:1905172; F:RISC complex binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:InterPro.
DR GO; GO:0010587; P:miRNA catabolic process; ISO:MGI.
DR GO; GO:0006402; P:mRNA catabolic process; IBA:GO_Central.
DR GO; GO:0010564; P:regulation of cell cycle process; ISO:MGI.
DR CDD; cd04508; TUDOR; 1.
DR Gene3D; 2.40.50.90; -; 5.
DR InterPro; IPR016685; Silence_cplx_Nase-comp_TudorSN.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR016071; Staphylococal_nuclease_OB-fold.
DR InterPro; IPR002071; Thermonucl_AS.
DR InterPro; IPR002999; Tudor.
DR Pfam; PF00565; SNase; 5.
DR Pfam; PF00567; TUDOR; 1.
DR PIRSF; PIRSF017179; RISC-Tudor-SN; 1.
DR SMART; SM00318; SNc; 4.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF50199; SSF50199; 5.
DR PROSITE; PS01284; TNASE_2; 1.
DR PROSITE; PS50830; TNASE_3; 4.
DR PROSITE; PS50304; TUDOR; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Endonuclease; Hydrolase; Isopeptide bond; Nuclease;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q7KZF4"
FT CHAIN 2..910
FT /note="Staphylococcal nuclease domain-containing protein 1"
FT /id="PRO_0000183181"
FT DOMAIN 18..166
FT /note="TNase-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT DOMAIN 193..328
FT /note="TNase-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT DOMAIN 341..496
FT /note="TNase-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT DOMAIN 525..660
FT /note="TNase-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT DOMAIN 729..787
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT MOTIF 321..325
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 388..392
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q7KZF4"
FT MOD_RES 103
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7KZF4"
FT MOD_RES 193
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q7KZF4"
FT MOD_RES 235
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 240
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7KZF4"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 641
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7KZF4"
FT MOD_RES 779
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7KZF4"
FT MOD_RES 785
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7KZF4"
FT MOD_RES 909
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CROSSLNK 513
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7KZF4"
FT CONFLICT 208
FT /note="V -> A (in Ref. 1; BAA84944)"
FT /evidence="ECO:0000305"
FT CONFLICT 908..910
FT /note="Missing (in Ref. 1; BAA84944)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 910 AA; 102088 MW; 7A31459E9274D0B6 CRC64;
MASSAQSSGS SGGPAVPTVQ RGIVKMVLSG CAIIVRGQPR GGPPPERQIN LSNIRAGNLA
RRAAATQPDG KDTPDEPWAF PAREFLRKKL IGKEVCFTIE NKTPQGREYG MIYLGKDTNG
ENIAESLVAE GLATRREGMR ANNPEQNRLS ECEEQAKASK KGMWSEGNGS HTIRDLKYTI
ENPRHFVDSH HQKPVNAIIE HVRDGSVVRA LLLPGHHLVT VMLSGIKCPT FRRETDGSET
PEPFAAEAKF FTESRLLQRD VQIILESCHN QNLLGTILHP NGNITELLLK EGFARCVDWS
IAVYTRGAEK LRAAERFAKE RRLRIWRDYV PPTANLDQKD KQFVAKVMQV LNADAIVVKL
NSGDYKTIHL SSIRPPRLEG DNIQDKNKKL RPLYDIPYMF EAREFLRKKL IGKKVNVTVD
YIRPASPATE TVPAFSERTC ATVTIGGINI AEALVSKGLA TVIRYRQDDD QRSSHYDELL
AAEARAIKNG KGLHSKKEVP IHRVADISGD TQKAKQFLPF LQRAGRSEAV VEYVFSGSRL
KLYLPKETCL ITFLLAGIEC PRGARNLPGL VQEGEPFSEE ATLFTKELVL QREVEVEVES
MDKAGNFIGW LHMDGANLSV LLVEQALSKV HFTAERSAYY KPLLSAEEAA KQRKEKVWAH
YEERPVEEVM PVLEEKERSA SYKPVFVTEI TDDLHFYVQD VETGTQLEKL MENMRNDISS
HPPVEGSYAP RRGEFCIAKF VDGEWYRARV EKVESPAKVH VFYIDYGNRE ILPSTRLGTL
PPAFSTRVLP AQATEYAFAF IQVPQDEDAR TDAVDSVVRD IQNTQCLLNV EHLSASCPHV
TLQFADSKGD VGLGLVKEGL VMVEVRKEKQ FQKVITEYLN AQESAKSARL NLWRYGDFRA
DDADEFGYSR
