SP110_MOUSE
ID SP110_MOUSE Reviewed; 445 AA.
AC Q8BVK9; Q05D41; Q3UCV7; Q80V00;
DT 22-AUG-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Sp110 nuclear body protein;
DE AltName: Full=Intracellular pathogen resistance protein 1;
GN Name=Sp110; Synonyms=Ifi75, Ipr1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISEASE, INDUCTION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C3Heb/FeJ; TISSUE=Lung;
RX PubMed=15815631; DOI=10.1038/nature03419;
RA Pan H., Yan B.-S., Rojas M., Shebzukhov Y.V., Zhou H., Kobzik L.,
RA Higgins D.E., Daly M.J., Bloom B.R., Kramnik I.;
RT "Ipr1 gene mediates innate immunity to tuberculosis.";
RL Nature 434:767-772(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and NMRI; TISSUE=Mammary tumor;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175 AND SER-177, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP STRUCTURE BY NMR OF 353-433.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the SAND domain of the putative nuclear protein
RT homolog (5830484A20RIK).";
RL Submitted (JUN-2004) to the PDB data bank.
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. {ECO:0000269|PubMed:15815631}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00185,
CC ECO:0000255|PROSITE-ProRule:PRU00747}.
CC -!- TISSUE SPECIFICITY: Detected in lung and macrophages.
CC {ECO:0000269|PubMed:15815631}.
CC -!- INDUCTION: Up-regulated after infection with M.tuberculosis.
CC {ECO:0000269|PubMed:15815631}.
CC -!- DISEASE: Note=Defects in Sp110 are a cause of severely impaired
CC resistance to infection by M.tuberculosis.
CC {ECO:0000269|PubMed:15815631}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH18413.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AY845948; AAW32543.1; -; mRNA.
DR EMBL; AK077800; BAC37018.1; -; mRNA.
DR EMBL; AK150373; BAE29505.1; -; mRNA.
DR EMBL; BC018413; AAH18413.1; ALT_SEQ; mRNA.
DR EMBL; BC039938; AAH39938.1; -; mRNA.
DR EMBL; BC094500; AAH94500.1; -; mRNA.
DR CCDS; CCDS35637.1; -.
DR RefSeq; NP_084470.1; NM_030194.1.
DR RefSeq; NP_780606.3; NM_175397.4.
DR PDB; 1UFN; NMR; -; A=353-433.
DR PDBsum; 1UFN; -.
DR AlphaFoldDB; Q8BVK9; -.
DR BMRB; Q8BVK9; -.
DR SMR; Q8BVK9; -.
DR BioGRID; 224528; 2.
DR STRING; 10090.ENSMUSP00000091226; -.
DR iPTMnet; Q8BVK9; -.
DR PhosphoSitePlus; Q8BVK9; -.
DR SwissPalm; Q8BVK9; -.
DR EPD; Q8BVK9; -.
DR jPOST; Q8BVK9; -.
DR MaxQB; Q8BVK9; -.
DR PaxDb; Q8BVK9; -.
DR PeptideAtlas; Q8BVK9; -.
DR PRIDE; Q8BVK9; -.
DR ProteomicsDB; 257546; -.
DR DNASU; 109032; -.
DR Ensembl; ENSMUST00000093508; ENSMUSP00000091226; ENSMUSG00000070034.
DR GeneID; 109032; -.
DR KEGG; mmu:109032; -.
DR UCSC; uc007btz.2; mouse.
DR CTD; 3431; -.
DR MGI; MGI:1923364; Sp110.
DR VEuPathDB; HostDB:ENSMUSG00000070034; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000155124; -.
DR HOGENOM; CLU_015844_2_0_1; -.
DR InParanoid; Q8BVK9; -.
DR OMA; QKARNEC; -.
DR OrthoDB; 377499at2759; -.
DR PhylomeDB; Q8BVK9; -.
DR TreeFam; TF335091; -.
DR BioGRID-ORCS; 109032; 18 hits in 71 CRISPR screens.
DR ChiTaRS; Sp110; mouse.
DR EvolutionaryTrace; Q8BVK9; -.
DR PRO; PR:Q8BVK9; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BVK9; protein.
DR Bgee; ENSMUSG00000070034; Expressed in animal zygote and 67 other tissues.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; IDA:MGI.
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 3D-structure; Apoptosis; DNA-binding; Immunity; Innate immunity; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..445
FT /note="Sp110 nuclear body protein"
FT /id="PRO_0000247960"
FT DOMAIN 1..108
FT /note="HSR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00747"
FT DOMAIN 353..433
FT /note="SAND"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00185"
FT REGION 187..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 251..266
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 195..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..266
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HB58"
FT CONFLICT 154
FT /note="P -> L (in Ref. 3; AAH18413/AAH39938)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="L -> P (in Ref. 3; AAH18413/AAH39938)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="A -> G (in Ref. 3; AAH39938)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="R -> H (in Ref. 3; AAH39938)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="M -> MA (in Ref. 3; AAH39938)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="Q -> L (in Ref. 3; AAH39938)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="T -> A (in Ref. 3; AAH39938)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="E -> G (in Ref. 2; BAE29505)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="G -> R (in Ref. 3; AAH39938)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="R -> C (in Ref. 3; AAH39938)"
FT /evidence="ECO:0000305"
FT CONFLICT 434..435
FT /note="FT -> CI (in Ref. 3; AAH39938)"
FT /evidence="ECO:0000305"
FT HELIX 355..358
FT /evidence="ECO:0007829|PDB:1UFN"
FT STRAND 359..366
FT /evidence="ECO:0007829|PDB:1UFN"
FT STRAND 369..374
FT /evidence="ECO:0007829|PDB:1UFN"
FT HELIX 375..379
FT /evidence="ECO:0007829|PDB:1UFN"
FT HELIX 397..404
FT /evidence="ECO:0007829|PDB:1UFN"
FT HELIX 412..415
FT /evidence="ECO:0007829|PDB:1UFN"
FT HELIX 423..428
FT /evidence="ECO:0007829|PDB:1UFN"
SQ SEQUENCE 445 AA; 50140 MW; A2F442C9ABFB3C5B CRC64;
MFTLTKALEK ALLQHFIYMK VNIAYAINKP FPFFEALRDN SFITERMYKE SLEACQNLVP
LSKVVHNILT SLEQTFHPSV LLTLFSKVNL REYPSLVAIF RSFRNVGYTY EEKNRPPLTL
LEDLANPAEG CSLQTLLPPP RPQISLPSHL SSAPRVCDPR ATAQPIIEIL DEQPSPSPRA
VPLLGCIQEG KTTPVSSRDH QRKDKEDSRE MPHSPSGPES VVKDDSPAAN DLEMAREVPC
TPANKKARRK KRPNWSNSKR RRQKKKPRQD EMMGVASPGH GVQEKLKAVS RRTLWKDDSS
TNVKEVTKTQ RTRMRRAQTS NSQEISKEAS KTSGRKRPST ARRTTQVPEK TKNDAVDFSP
TLPVTCGKAK GTLFQEKLKQ GASKKCIQNE AGDWLTVKEF LNEGGRATSK DWKGVIRCNG
ETLRHLEQKG LLFFTSKSKP QKKGA
