SND1_PONAB
ID SND1_PONAB Reviewed; 910 AA.
AC Q5REU4;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 87.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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) (By
CC similarity). Interacts with the RISC components AGO2, FMR1 and TNRC6A
CC (By similarity). Interacts with GTF2E1 and GTF2E2 (By similarity).
CC Interacts with PIM1 (By similarity). Interacts with STAT5 (By
CC similarity). Interacts with SYT11 (via C2 2 domain); the interaction
CC with SYT11 is direct (By similarity). {ECO:0000250|UniProtKB:Q78PY7,
CC ECO:0000250|UniProtKB:Q7KZF4}.
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}.
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DR EMBL; CR857422; CAH89713.1; -; mRNA.
DR AlphaFoldDB; Q5REU4; -.
DR SMR; Q5REU4; -.
DR STRING; 9601.ENSPPYP00000020159; -.
DR eggNOG; KOG2039; Eukaryota.
DR InParanoid; Q5REU4; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016442; C:RISC complex; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:InterPro.
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 2: Evidence at transcript 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_0000292280"
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 240
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7KZF4"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7KZF4"
FT MOD_RES 641
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q7KZF4"
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:0000250|UniProtKB:Q7KZF4"
FT CROSSLNK 513
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7KZF4"
SQ SEQUENCE 910 AA; 101993 MW; 7A5CD7C056D54B42 CRC64;
MASSAQSGGS SGGPAVPTVQ RGIVKMVLSG CAIIVRGQPR GGPPPERQIN LSNIRAGNLA
RRAAATQPDA KDTPDEPWAF PAREFLRKKL IGKEVCFTIE NKTPQGREYG MIYLGKDTNG
ENIAESLVAE GLATRREGMR ANNPEQNRLS ECEEQAKAAK KGMWSEGNGS HTIRDLKYTI
ENPRHFVDSH HQKPVNAIIE HVRDGSVVRA LLLPDYYLVT VMLSGIKCPT FRREADGSET
PEPFAAEAKF FTESRLLQRD VQIILESCHN QNILGTILHP NGNITELLLK EGFARCVDWS
IAVYTRGAEK LRAAERFAKE RRLRIWRDYV APTANLDQKD KQFVAKVMQV LNADAIVVKL
NSGDYKTIHL SSIRPPRLEG ENTQDKNKKL RPLYDIPYMF EAREFLRKKL IGKKVNVTVD
YIRPASPATE TVPAFSERTC ATVTIGGINI AEALVSKGLA TVIRYRQDDD QRSSHYDELL
AAEARAIKNG KGLHSKKEVP IHRVADISGD TQKAKQFLPF LQRAGRSEAV VEYVFSGSRL
KLYLPKETCL ITFLLAGIEC PRGARNLPGL VQEGEPFSEE ATLFTKELVL QREVEVEVES
MDKAGNFIGW LHIDGANLSV LLVEHALSKV HFTAERSSYY KSLLSAEEAA KQKKEKVWAH
YEEQPVEEVM PVLEEKERSA SYKPVFVTEI TDDLHFYVQD VETGTQLEKL MENMRNDIAS
HPPVEGSYAP RRGEFCIAKF VDGEWYRARV EKVESPAKIH VFYIDYGNRE VLPSTRLGTL
PPAFSTRVLP AQATEYAFAF IQVPQDDDAR TDAVDSVVRD IQNTQCLLNV EHLSAGCPHV
TLQFADSKGD VGLGLVKEGL VMVEVRKEKQ FQKVITEYLN AQESAKSARL NLWRYGDFRA
DDADEFGYSR
