IFI5B_MOUSE
ID IFI5B_MOUSE Reviewed; 425 AA.
AC P0DOV1; B7ZNS3; P15092; Q08619; Q3TM07; Q3U776; Q3U7F4; Q3U7K5; Q3UCH9;
AC Q8C4X3; Q921V9;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Interferon-activable protein 205-B;
DE Short=Ifi-205-B;
DE AltName: Full=Interferon-inducible protein p205-B;
DE AltName: Full=Myeloid cell nuclear differentiation antigen;
DE AltName: Full=Protein D3;
GN Name=Mnda; Synonyms=Ifi205b;
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] (ISOFORM 1), TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Macrophage;
RX PubMed=7684766; DOI=10.1002/jlb.53.5.563;
RA Tannenbaum C.S., Major J., Ohmori Y., Hamilton T.A.;
RT "A lipopolysaccharide-inducible macrophage gene (D3) is a new member of an
RT interferon-inducible gene cluster and is selectively expressed in
RT mononuclear phagocytes.";
RL J. Leukoc. Biol. 53:563-568(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15342947; DOI=10.1634/stemcells.22-5-832;
RA Dermott J.M., Gooya J.M., Asefa B., Weiler S.R., Smith M., Keller J.R.;
RT "Inhibition of growth by p205: a nuclear protein and putative tumor
RT suppressor expressed during myeloid cell differentiation.";
RL Stem Cells 22:832-848(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RC TISSUE=Bone marrow macrophage, Cerebellum, and Mammary gland;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [5]
RP FUNCTION, AND INTERACTION WITH TP53; RB1; CDK1; CDK2 AND HOXB2.
RX PubMed=16458891; DOI=10.1016/j.febslet.2006.01.032;
RA Asefa B., Dermott J.M., Kaldis P., Stefanisko K., Garfinkel D.J.,
RA Keller J.R.;
RT "p205, a potential tumor suppressor, inhibits cell proliferation via
RT multiple pathways of cell cycle regulation.";
RL FEBS Lett. 580:1205-1214(2006).
RN [6]
RP STRUCTURE BY NMR OF 8-88.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structures of the PAAD_DAPIN domain of Mus musculus interferon-
RT activatable protein 205.";
RL Submitted (FEB-2008) to the PDB data bank.
CC -!- FUNCTION: May act as a transcriptional regulator in the myeloid
CC lineage. Inhibits cell growth via p53/TP53 and RB1-dependent and
CC independent pathways. {ECO:0000269|PubMed:15342947,
CC ECO:0000269|PubMed:16458891}.
CC -!- SUBUNIT: Interacts with TP53, RB1, CDK1, CDK2 and HOXB2.
CC {ECO:0000269|PubMed:16458891}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15342947}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P0DOV1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P0DOV1-2; Sequence=VSP_058589;
CC -!- TISSUE SPECIFICITY: Mononuclear phagocytes.
CC {ECO:0000269|PubMed:7684766}.
CC -!- INDUCTION: By lipopolysaccharides (LPS). {ECO:0000269|PubMed:7684766}.
CC -!- SIMILARITY: Belongs to the HIN-200 family. {ECO:0000305}.
CC -!- CAUTION: The family of genes to which Mnda belongs has undergone a
CC rapid expansion in the mouse. As a consequence, mouse Mnda and human
CC MNDA genes, although belonging to the same family, are not one to one
CC orthologs.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE31364.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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; S62227; AAB26880.1; -; mRNA.
DR EMBL; AK152621; BAE31364.1; ALT_INIT; mRNA.
DR EMBL; AK080485; BAC37930.1; -; mRNA.
DR EMBL; AK152683; BAE31415.1; -; mRNA.
DR EMBL; AK152786; BAE31495.1; -; mRNA.
DR EMBL; AK166217; BAE38635.1; -; mRNA.
DR EMBL; BC132314; AAI32315.1; -; mRNA.
DR EMBL; BC132316; AAI32317.1; -; mRNA.
DR EMBL; BC145397; AAI45398.1; -; mRNA.
DR CCDS; CCDS15532.1; -. [P0DOV1-1]
DR RefSeq; NP_001028622.1; NM_001033450.4. [P0DOV1-1]
DR RefSeq; NP_001288674.1; NM_001301745.1. [P0DOV1-2]
DR PDB; 2YU0; NMR; -; A=8-88.
DR PDBsum; 2YU0; -.
DR AlphaFoldDB; P0DOV1; -.
DR SMR; P0DOV1; -.
DR STRING; 10090.ENSMUSP00000009340; -.
DR iPTMnet; P0DOV1; -.
DR PhosphoSitePlus; P0DOV1; -.
DR EPD; P0DOV1; -.
DR jPOST; P0DOV1; -.
DR PRIDE; P0DOV1; -.
DR ProteomicsDB; 267272; -. [P0DOV1-1]
DR ProteomicsDB; 267273; -. [P0DOV1-2]
DR Ensembl; ENSMUST00000009340; ENSMUSP00000009340; ENSMUSG00000026536. [P0DOV1-1]
DR GeneID; 381308; -.
DR KEGG; mmu:381308; -.
DR CTD; 381308; -.
DR MGI; MGI:3041120; Mnda.
DR VEuPathDB; HostDB:ENSMUSG00000026536; -.
DR eggNOG; ENOG502QTQS; Eukaryota.
DR GeneTree; ENSGT00390000013296; -.
DR OrthoDB; 1304994at2759; -.
DR PhylomeDB; P0DOV1; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 381308; 2 hits in 39 CRISPR screens.
DR ChiTaRS; Ifi211; mouse.
DR PRO; PR:P0DOV1; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P0DOV1; protein.
DR Bgee; ENSMUSG00000026536; Expressed in zone of skin and 45 other tissues.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0034399; C:nuclear periphery; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0002218; P:activation of innate immune response; IBA:GO_Central.
DR GO; GO:0050853; P:B cell receptor signaling pathway; ISO:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0035458; P:cellular response to interferon-beta; IBA:GO_Central.
DR GO; GO:0030889; P:negative regulation of B cell proliferation; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; IBA:GO_Central.
DR Gene3D; 1.10.533.10; -; 1.
DR Gene3D; 2.40.50.140; -; 2.
DR InterPro; IPR004020; DAPIN.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR040205; HIN-200.
DR InterPro; IPR004021; HIN200/IF120x.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR PANTHER; PTHR12200; PTHR12200; 1.
DR Pfam; PF02760; HIN; 1.
DR Pfam; PF02758; PYRIN; 1.
DR SMART; SM01289; PYRIN; 1.
DR PROSITE; PS50824; DAPIN; 1.
DR PROSITE; PS50834; HIN_200; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation.
FT CHAIN 1..425
FT /note="Interferon-activable protein 205-B"
FT /id="PRO_0000153722"
FT DOMAIN 1..88
FT /note="Pyrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00061"
FT REPEAT 129..135
FT /note="1"
FT REPEAT 136..142
FT /note="2"
FT REPEAT 143..149
FT /note="3"
FT REPEAT 150..156
FT /note="4"
FT DOMAIN 213..413
FT /note="HIN-200"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00106"
FT REGION 86..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..177
FT /note="4 X 7 AA tandem repeats of T-S-T-A-Q-A-[GR]"
FT COMPBIAS 93..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 89..90
FT /note="Missing (in isoform 2)"
FT /id="VSP_058589"
FT CONFLICT 142
FT /note="G -> R (in Ref. 3; BAE38635)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="A -> E (in Ref. 3; BAE38635)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="K -> E (in Ref. 3; BAE31415)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="F -> S (in Ref. 3; BAE38635)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="K -> N (in Ref. 3; BAE38635)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="S -> R (in Ref. 1; AAB26880)"
FT /evidence="ECO:0000305"
FT TURN 10..16
FT /evidence="ECO:0007829|PDB:2YU0"
FT HELIX 19..30
FT /evidence="ECO:0007829|PDB:2YU0"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:2YU0"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:2YU0"
FT HELIX 45..55
FT /evidence="ECO:0007829|PDB:2YU0"
FT TURN 57..61
FT /evidence="ECO:0007829|PDB:2YU0"
FT HELIX 62..71
FT /evidence="ECO:0007829|PDB:2YU0"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:2YU0"
FT HELIX 76..86
FT /evidence="ECO:0007829|PDB:2YU0"
SQ SEQUENCE 425 AA; 46977 MW; 4CC601557C946E2B CRC64;
MVNEYKRIVL LRGLECINKH YFSLFKSLLA RDLNLERDNQ EQYTTIQIAN MMEEKFPADS
GLGKLIEFCE EVPALRKRAE ILKKERSEVT GETSLEKNGQ EAGPATPTST TSHMLASERG
ETSATQEETS TAQAGTSTAQ AGTSTAQAGT STAQKRKSMR EEETGVKKSK AAKEPDQPPC
CEEPTAMCQS PILHSSSSAS SNILSAKNQK SQPQNQNIPR GAVLHSEPLT VMVLTATDPF
EYESPEHEVK NMFHATVATV SQYFHVKVFN IDLKEKFTKN NFITISNYFE SKGILEINET
SSVLEAAPKQ MIEVPNCITR NANASPKICD IQKGTSGTVF YGVFTLHKKK VKTQNTSYEI
KDGSGSIEVV GSGQWHNINC KEGDKLHLFC FHLKRERGQP KLVCGDHSFV KVTKAGKKKE
ASTVQ
