Entry sw: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   18-JAN-2017, entry version 106.
DE   RecName: Full=Staphylococcal nuclease domain-containing protein 1;
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;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; 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
RT   cells and its abundance is increased in response to prolactin in
RT   culture and in 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: Functions as a bridging factor between STAT6 and the
CC       basal transcription factor. Plays a role in PIM1 regulation of MYB
CC       activity. Plays a role in cell viability. Functions as a
CC       transcriptional coactivator for STAT5. Plays a role in cell
CC       viability (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with GTF2E1 and GTF2E2. Forms a ternary complex
CC       with STAT6 and POLR2A. Interacts with STAT5 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000250}. Melanosome {ECO:0000250}. Note=In IL-4 stimulated
CC       cells colocalizes with STAT6 in the nucleus. {ECO:0000250}.
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
CC       hormones during lactation and correlated with the induction of
CC       beta casein gene expression.
CC   -!- PTM: Phosphorylated by PIM1 in vitro. {ECO:0000250}.
CC   -!- SIMILARITY: Contains 4 TNase-like domains. {ECO:0000255|PROSITE-
CC       ProRule:PRU00272}.
CC   -!- SIMILARITY: Contains 1 Tudor domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00211}.
DR   EMBL; AY273893; AAP31682.1; -; mRNA.
DR   EMBL; BC104504; AAI04505.1; -; mRNA.
DR   RefSeq; NP_991353.1; NM_205784.1.
DR   UniGene; Bt.61314; -.
DR   ProteinModelPortal; 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   eggNOG; KOG2039; Eukaryota.
DR   eggNOG; COG1525; LUCA.
DR   GeneTree; ENSGT00510000047270; -.
DR   HOGENOM; HOG000173592; -.
DR   HOVERGEN; HBG057234; -.
DR   InParanoid; Q863B3; -.
DR   KO; K15979; -.
DR   OMA; IQVPQDD; -.
DR   OrthoDB; EOG091G027G; -.
DR   TreeFam; TF300615; -.
DR   Proteomes; UP000009136; Chromosome 4.
DR   Bgee; ENSBTAG00000010692; -.
DR   GO; GO:0005913; C:cell-cell adherens junction; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0097433; C:dense body; IEA:Ensembl.
DR   GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016442; C:RISC complex; IEA:InterPro.
DR   GO; GO:0004518; F:nuclease activity; IBA:GO_Central.
DR   GO; GO:0044822; F:poly(A) RNA binding; IEA:Ensembl.
DR   GO; GO:0098609; P:cell-cell adhesion; IEA:GOC.
DR   GO; GO:0031047; P:gene silencing by RNA; IEA:InterPro.
DR   GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006401; P:RNA catabolic process; IBA:GO_Central.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.50.90; -; 5.
DR   InterPro; IPR016685; Silence_cplx_Nase-comp_TudorSN.
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; 6.
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; Complete proteome; Cytoplasm; Direct protein sequencing;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW   Transcription regulation.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:Q7KZF4}.
FT   CHAIN         2    910       Staphylococcal nuclease domain-containing
FT                                protein 1.
FT                                /FTId=PRO_0000183179.
FT   DOMAIN       18    166       TNase-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00272}.
FT   DOMAIN      193    328       TNase-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00272}.
FT   DOMAIN      341    496       TNase-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00272}.
FT   DOMAIN      525    660       TNase-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00272}.
FT   DOMAIN      729    787       Tudor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00211}.
FT   MOTIF       321    325       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   MOTIF       388    392       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000250|UniProtKB:Q7KZF4}.
FT   MOD_RES     103    103       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q7KZF4}.
FT   MOD_RES     193    193       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q7KZF4}.
FT   MOD_RES     240    240       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q7KZF4}.
FT   MOD_RES     426    426       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q7KZF4}.
FT   MOD_RES     641    641       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q7KZF4}.
FT   MOD_RES     645    645       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q7KZF4}.
FT   MOD_RES     779    779       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q7KZF4}.
FT   MOD_RES     785    785       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q7KZF4}.
FT   MOD_RES     909    909       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q7KZF4}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       220    327       ipfam:SNase [T]
FT   MYHIT       368    495       ipfam:SNase [T]
FT   MYHIT       553    659       ipfam:SNase [T]
FT   MYHIT        18    166       iprf:TNASE_3 [T]
FT   MYHIT        61    166       ipfam:SNase [T]
FT   MYHIT       341    496       ismart:SNc [T]
FT   MYHIT       728    785       ismart:TUDOR [T]
FT   MYHIT       848    894       ipfam:SNase [T]
FT   MYHIT       193    328       ismart:SNc [T]
FT   MYHIT       679    797       ipfam:TUDOR [T]
FT   MYHIT       193    328       iprf:TNASE_3 [T]
FT   MYHIT       525    660       iprf:TNASE_3 [T]
FT   MYHIT       729    787       iprf:TUDOR [T]
FT   MYHIT       103    113       ipat:TNASE_2 [T]
FT   MYHIT       525    660       ismart:SNc [T]
FT   MYHIT        18    166       ismart:SNc [T]
FT   MYHIT       341    496       iprf:TNASE_3 [T]
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
//