SND1_BOVIN
ID SND1_BOVIN Reviewed; 910 AA.
AC Q863B3; Q3MHZ9;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 131.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 162-167; 745-752 AND
RP 849-867, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Lactating mammary gland;
RX PubMed=11691653; DOI=10.1677/joe.0.1710329;
RA Broadhurst M.K., Wheeler T.T.;
RT "The p100 coactivator is present in the nuclei of mammary epithelial cells
RT and its abundance is increased in response to prolactin in culture and in
RT mammary tissue during lactation.";
RL J. Endocrinol. 171:329-337(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) 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 -!- TISSUE SPECIFICITY: In lactating cows highly expressed in mammary
CC epithelial cells. {ECO:0000269|PubMed:11691653}.
CC -!- INDUCTION: Protein levels increased in response to lactogenic hormones
CC during lactation and correlated with the induction of beta casein gene
CC expression.
CC -!- PTM: Phosphorylated by PIM1 in vitro. {ECO:0000250}.
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; AY273893; AAP31682.1; -; mRNA.
DR EMBL; BC104504; AAI04505.1; -; mRNA.
DR RefSeq; NP_991353.1; NM_205784.1.
DR AlphaFoldDB; Q863B3; -.
DR SMR; Q863B3; -.
DR STRING; 9913.ENSBTAP00000014154; -.
DR PaxDb; Q863B3; -.
DR PeptideAtlas; Q863B3; -.
DR PRIDE; Q863B3; -.
DR Ensembl; ENSBTAT00000014154; ENSBTAP00000014154; ENSBTAG00000010692.
DR GeneID; 404098; -.
DR KEGG; bta:404098; -.
DR CTD; 27044; -.
DR VEuPathDB; HostDB:ENSBTAG00000010692; -.
DR VGNC; VGNC:35063; SND1.
DR eggNOG; KOG2039; Eukaryota.
DR GeneTree; ENSGT00510000047270; -.
DR HOGENOM; CLU_005966_0_0_1; -.
DR InParanoid; Q863B3; -.
DR OMA; FGQEAHD; -.
DR OrthoDB; 227839at2759; -.
DR TreeFam; TF300615; -.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000010692; Expressed in prostate gland and 110 other tissues.
DR ExpressionAtlas; Q863B3; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0097433; C:dense body; IEA:Ensembl.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016442; C:RISC complex; IEA:InterPro.
DR GO; GO:0004521; F:endoribonuclease activity; IEA:Ensembl.
DR GO; GO:0004518; F:nuclease activity; IBA:GO_Central.
DR GO; GO:1905172; F:RISC complex binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:InterPro.
DR GO; GO:0010587; P:miRNA catabolic process; IEA:Ensembl.
DR GO; GO:0006402; P:mRNA catabolic process; IBA:GO_Central.
DR GO; GO:0010564; P:regulation of cell cycle process; IEA:Ensembl.
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; Direct protein sequencing; Endonuclease; Hydrolase;
KW Isopeptide bond; Nuclease; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; 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_0000183179"
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; 101989 MW; E4EC29351E39BE73 CRC64;
MASSAQSGGS SGGPAVPTVQ RGIVKMVLSG CAIIVRGQPR GGPPPERQIN LSNIRAGNLA
RRAAVAQPDA KDTPDEPWAF PAREFLRKKL IGKEVCFTIE NKTPQGREYG MIYLGKDTNG
ENIAESLVAE GLATRREGMR ANNPEQNRLA ECEEQAKASK 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
YIRPASPATD TVPAFSERTC ATVTIGGINI AEALVSKGLA TVIRYRQDDD QRSSHYDELL
AAEARAIKNG KGLHSKKEVP IHRVADISGD TQKAKQFLPF LQRAGRSEAV VEYVFSGSRL
KLYLPKETCL ITFLLAGIEC PRGARNLPGL VQEGEPFSEE ATLFTKELVL QREVEVEVES
MDKAGNFIGW LHIDGANLSV LLVEHALSKV HFTAERSAYY KSLLSAEEAA KQKKEKVWAH
YEEQPVEELM PVLEEKERSA SYKPVFVTEI TDDLHFYVQD VETGTQLEKL MENMRNDIAS
HPPVEGSYAP RRGEFCIAKF VDGEWYRARV EKVESPAKVH VFYIDYGNRE ILPSTRLGTL
PPAFSTRVLP AQATEYAFAF IQVPQDEDAR TDAVDSVVRD IQNTQCLLNV EHLSAGCPHV
TLQFADSKGD VGLGLVKEGL VMVEVRKEKQ FQKVITEYLN AQESAKSARL NLWRYGDFRA
DDADEFGYSR
