SP110_RAT
ID SP110_RAT Reviewed; 478 AA.
AC Q3KRF1;
DT 22-AUG-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Sp110 nuclear body protein;
DE AltName: Full=Intracellular pathogen resistance protein 1;
GN Name=Sp110; Synonyms=Ipr1;
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 [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305, 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).
CC -!- FUNCTION: May act as a transcription factor. Plays a role in the innate
CC immunity against intracellular pathogens. Required for resistance to
CC M.tuberculosis and L.monocytogenes. Promotes apoptosis of infected
CC cells (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00185,
CC ECO:0000255|PROSITE-ProRule:PRU00747}.
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DR EMBL; BC105751; AAI05752.1; -; mRNA.
DR RefSeq; NP_001029309.1; NM_001034137.1.
DR AlphaFoldDB; Q3KRF1; -.
DR SMR; Q3KRF1; -.
DR STRING; 10116.ENSRNOP00000053828; -.
DR iPTMnet; Q3KRF1; -.
DR PhosphoSitePlus; Q3KRF1; -.
DR PaxDb; Q3KRF1; -.
DR Ensembl; ENSRNOT00000056995; ENSRNOP00000053828; ENSRNOG00000033747.
DR GeneID; 301570; -.
DR KEGG; rno:301570; -.
DR UCSC; RGD:1310173; rat.
DR CTD; 3431; -.
DR RGD; 1310173; Sp110.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; Q3KRF1; -.
DR OrthoDB; 377499at2759; -.
DR PhylomeDB; Q3KRF1; -.
DR TreeFam; TF335091; -.
DR PRO; PR:Q3KRF1; -.
DR Proteomes; UP000002494; Chromosome 9.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR Gene3D; 3.10.390.10; -; 1.
DR InterPro; IPR004865; HSR_dom.
DR InterPro; IPR010919; SAND-like_dom_sf.
DR InterPro; IPR000770; SAND_dom.
DR InterPro; IPR043563; Sp110/Sp140/Sp140L.
DR PANTHER; PTHR46386; PTHR46386; 2.
DR Pfam; PF03172; HSR; 1.
DR Pfam; PF01342; SAND; 1.
DR SMART; SM00258; SAND; 1.
DR SUPFAM; SSF63763; SSF63763; 1.
DR PROSITE; PS51414; HSR; 1.
DR PROSITE; PS50864; SAND; 1.
PE 1: Evidence at protein level;
KW Apoptosis; DNA-binding; Immunity; Innate immunity; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..478
FT /note="Sp110 nuclear body protein"
FT /id="PRO_0000247962"
FT DOMAIN 1..108
FT /note="HSR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00747"
FT DOMAIN 385..466
FT /note="SAND"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00185"
FT REGION 131..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 279..294
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 131..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..297
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BVK9"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BVK9"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HB58"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 478 AA; 53205 MW; DE3FB12100B37478 CRC64;
MFTLTKALEK ALLQHFIYTK LDIAYAINKP FPFFEALRDN SFITERMYKE SLEACQNLVP
LSKVVHNILT SLEQTFDPSM LLILFSKVNL REYPSLGAIC RSFRNVGNAY EGRNRPAPTL
LGASTNPAEG CSFQTLLPQP RSQALPPSHL SSGLRIRDPG TTSLQITEIL DEQPSPSHPA
APLPGYIREG KTTPVSSRDH QRKDKEDSQE MPHHPSGPEA VVKDILTSKT NNRDDSGAQP
PGSPGTMHVV QDNSPAPNDP EVPQEAPCTP ANKKARKRKS CIWSNSKRRR QKKKPPQHKM
MGVASPGPGV QEKLKVVGQR TLNQDDSTRN VKVVTRTLRE RTRCAQTSSS QEISKEASKP
RARKRPQKRP HTAGRTIHVP EKSKDDAVDF LSPTLSVTCG EARGTLFKEK LKQGSSEKCI
QNEAGAWLTV KEFLKKGGKA TSKDWKKAIR CNKKTLRSLE QDGFLFCTSK SKPQKECD
