SND1_RAT
ID SND1_RAT Reviewed; 909 AA.
AC Q66X93; P97693; Q6IN40;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 133.
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=SND p102;
DE AltName: Full=p100 co-activator;
DE AltName: Full=p105 coactivator;
GN Name=Snd1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Palacios L., Fresnedo O., Ochoa B.;
RT "Cellular localization of cloned StaphylocoCCal nuclease domain containing
RT rat p102.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 18-909.
RA Kassessinoff T., Amouzadeh H., Accili D., Beaven M.A., Sagi-Eisenberg R.;
RT "Rat p105 homologous to human B-cell p100 co-activator.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-908, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [5]
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 (By similarity). {ECO:0000250|UniProtKB:Q78PY7,
CC ECO:0000250|UniProtKB:Q7KZF4}.
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). Interacts
CC with the RISC components AGO2, FMR1 and TNRC6A (PubMed:24882364).
CC Interacts with GTF2E1 and GTF2E2 (By similarity). Interacts with PIM1
CC (By similarity). Interacts with STAT5 (By similarity). Interacts with
CC SYT11 (via C2 2 domain); the interaction with SYT11 is direct
CC (PubMed:24882364). {ECO:0000250|UniProtKB:Q78PY7,
CC ECO:0000250|UniProtKB:Q7KZF4, ECO:0000269|PubMed:24882364}.
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=AAB41439.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY697864; AAU05374.1; -; mRNA.
DR EMBL; BC072471; AAH72471.2; -; mRNA.
DR EMBL; U83883; AAB41439.1; ALT_INIT; mRNA.
DR RefSeq; NP_073185.2; NM_022694.2.
DR AlphaFoldDB; Q66X93; -.
DR SMR; Q66X93; -.
DR BioGRID; 249173; 2.
DR IntAct; Q66X93; 6.
DR MINT; Q66X93; -.
DR STRING; 10116.ENSRNOP00000041531; -.
DR iPTMnet; Q66X93; -.
DR PhosphoSitePlus; Q66X93; -.
DR jPOST; Q66X93; -.
DR PaxDb; Q66X93; -.
DR PRIDE; Q66X93; -.
DR GeneID; 64635; -.
DR KEGG; rno:64635; -.
DR UCSC; RGD:631340; rat.
DR CTD; 27044; -.
DR RGD; 631340; Snd1.
DR VEuPathDB; HostDB:ENSRNOG00000031173; -.
DR eggNOG; KOG2039; Eukaryota.
DR HOGENOM; CLU_005966_0_0_1; -.
DR InParanoid; Q66X93; -.
DR OMA; FGQEAHD; -.
DR OrthoDB; 227839at2759; -.
DR PhylomeDB; Q66X93; -.
DR PRO; PR:Q66X93; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000031173; Expressed in liver and 20 other tissues.
DR ExpressionAtlas; Q66X93; baseline and differential.
DR Genevisible; Q66X93; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0097433; C:dense body; ISO:RGD.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0016442; C:RISC complex; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; ISO:RGD.
DR GO; GO:0004521; F:endoribonuclease activity; ISO:RGD.
DR GO; GO:0004518; F:nuclease activity; IBA:GO_Central.
DR GO; GO:1905172; F:RISC complex binding; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; ISO:RGD.
DR GO; GO:0003713; F:transcription coactivator activity; TAS:RGD.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:InterPro.
DR GO; GO:0010587; P:miRNA catabolic process; ISO:RGD.
DR GO; GO:0006402; P:mRNA catabolic process; IBA:GO_Central.
DR GO; GO:0010564; P:regulation of cell cycle process; ISO:RGD.
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 CHAIN 1..909
FT /note="Staphylococcal nuclease domain-containing protein 1"
FT /id="PRO_0000183182"
FT DOMAIN 17..165
FT /note="TNase-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT DOMAIN 192..327
FT /note="TNase-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT DOMAIN 340..495
FT /note="TNase-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT DOMAIN 524..659
FT /note="TNase-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT DOMAIN 728..786
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT MOTIF 320..324
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 387..391
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOD_RES 102
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7KZF4"
FT MOD_RES 192
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q7KZF4"
FT MOD_RES 234
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q78PY7"
FT MOD_RES 239
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7KZF4"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7KZF4"
FT MOD_RES 640
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q7KZF4"
FT MOD_RES 644
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7KZF4"
FT MOD_RES 784
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7KZF4"
FT MOD_RES 908
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CROSSLNK 512
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7KZF4"
FT CONFLICT 32
FT /note="I -> M (in Ref. 3; AAB41439)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="Q -> L (in Ref. 3; AAB41439)"
FT /evidence="ECO:0000305"
FT CONFLICT 41..43
FT /note="GPP -> TA (in Ref. 3; AAB41439)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="A -> DT (in Ref. 3; AAB41439)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="A -> R (in Ref. 3; AAB41439)"
FT /evidence="ECO:0000305"
FT CONFLICT 133..137
FT /note="SRREG -> PGES (in Ref. 3; AAB41439)"
FT /evidence="ECO:0000305"
FT CONFLICT 167..173
FT /note="NGSHTIR -> TGHTHP (in Ref. 3; AAB41439)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="N -> S (in Ref. 3; AAB41439)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="A -> T (in Ref. 3; AAB41439)"
FT /evidence="ECO:0000305"
FT CONFLICT 637
FT /note="A -> G (in Ref. 3; AAB41439)"
FT /evidence="ECO:0000305"
FT CONFLICT 726..728
FT /note="AYA -> LR (in Ref. 3; AAB41439)"
FT /evidence="ECO:0000305"
FT CONFLICT 752
FT /note="V -> E (in Ref. 3; AAB41439)"
FT /evidence="ECO:0000305"
FT CONFLICT 777
FT /note="Missing (in Ref. 3; AAB41439)"
FT /evidence="ECO:0000305"
FT CONFLICT 802
FT /note="V -> W (in Ref. 3; AAB41439)"
FT /evidence="ECO:0000305"
FT CONFLICT 814..818
FT /note="DSVVR -> TVCA (in Ref. 3; AAB41439)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 909 AA; 101952 MW; CD032114A1051784 CRC64;
MASAQSSGSS GGPAVPTVQR GIVKMVLSGC AIIVRGQPRG GPPPERQINL SNIRAGNLAR
RAAATQPDGK DTPDEPWAFP AREFLRKKLI GKEVCFTIEN KTPQGREYGM IYLGKDTNGE
NIAESLVAEG LASRREGMRA NNPEQNRLSE CEEQAKASKK GMWSEGNGSH TIRDLKYTIE
NPRHFVDSHH QKPVNAIIEH VRDGSVVRAL LLPDHYLVTV MLSGIKCPTF RRETDGSETP
EPFAAEAKFF TESRLLQRDV QIILESCHNQ NILGTILHPN GNITELLLKE GFARCVDWSI
AVYTRGAEKL RAAERFAKER RLRIWRDYVP PTANLDQKDK QFVAKVMQVL NADAIVVKLN
SGDYKTIHLS SIRPPRLEGD NIQDKNKKLR PLYDIPYMFE AREFLRKKLI GKKVSVTVDY
IRPASPATET VPAFSERTCA TVTIGGINIA EALVSKGLAT VIRYRQDDDQ RSSHYDELLA
AEARAIKNGK GLHSKKEVPI HRVADISGDT QKAKQFLPFL QRAGRSEAVV EYVFSGSRLK
LYLPKETCLI TFLLAGIECP RGARNLPGLV QEGEPFSEEA TLFTKELVLQ REVEVEVESM
DKAGNFIGWL HMDGANLSVL LVEHALSKVH FTAERSAYYK PLLSAEEAAK QRKEKVWAHY
EEQPVEEVMP VLEEKERSAS YKPVFVTEIT DDLHFYVQDV ETGTQLEKLM ENMRSDISSH
PPVEGAYAPR RGEFCIAKFV DGEWYRARVE KVESPAKVHV FYIDYGNREI LPSTRLGALP
PAFSTRVLPA QATEYAFAFI QVPQDEDART DAVDSVVRDI QNTQCLLNVE HLSASCPHVT
LQFADSKGDV GLGLVKEGLV MVEVRKEKQF QKVITEYLNA QESAKSARLN LWRYGDFRAD
DADEFGYSR
