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   27-MAR-2024, entry version 156.
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   GlyGen; Q8BVK9; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q8BVK9; -.
DR   PhosphoSitePlus; Q8BVK9; -.
DR   SwissPalm; Q8BVK9; -.
DR   EPD; Q8BVK9; -.
DR   jPOST; Q8BVK9; -.
DR   MaxQB; Q8BVK9; -.
DR   PaxDb; 10090-ENSMUSP00000091226; -.
DR   PeptideAtlas; Q8BVK9; -.
DR   ProteomicsDB; 257546; -.
DR   DNASU; 109032; -.
DR   Ensembl; ENSMUST00000093508.7; ENSMUSP00000091226.7; ENSMUSG00000070034.14.
DR   GeneID; 109032; -.
DR   KEGG; mmu:109032; -.
DR   UCSC; uc007btz.2; mouse.
DR   AGR; MGI:1923364; -.
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; 38708at2759; -.
DR   PhylomeDB; Q8BVK9; -.
DR   TreeFam; TF335091; -.
DR   BioGRID-ORCS; 109032; 18 hits in 77 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 cell types or tissues.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
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; SAND domain-like; 1.
DR   InterPro; IPR004865; HSR_dom.
DR   InterPro; IPR010919; SAND-like_dom_sf.
DR   InterPro; IPR000770; SAND_dom.
DR   InterPro; IPR043563; Sp110/Sp140/Sp140L-like.
DR   PANTHER; PTHR46386; NUCLEAR BODY PROTEIN SP140; 1.
DR   PANTHER; PTHR46386:SF7; SP110 NUCLEAR BODY PROTEIN; 1.
DR   Pfam; PF03172; HSR; 1.
DR   Pfam; PF01342; SAND; 1.
DR   SMART; SM00258; SAND; 1.
DR   SUPFAM; SSF63763; SAND domain-like; 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
//