IFI3_MOUSE
ID IFI3_MOUSE Reviewed; 408 AA.
AC O35368; Q3T9I1; Q3TEA2; Q3TP57; Q3UMV2; Q8BYE5; Q91VV8;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 148.
DE RecName: Full=Interferon-activable protein 203;
DE Short=Ifi-203;
DE AltName: Full=Interferon-inducible protein p203;
GN Name=Ifi203;
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).
RC STRAIN=BALB/cJ; TISSUE=Fibroblast;
RX PubMed=9363777; DOI=10.1111/j.1432-1033.1997.t01-1-00258.x;
RA Gribaudo G., Ravaglia S., Guandalini L., Riera L., Gariglio M.,
RA Landolfo S.;
RT "Molecular cloning and expression of an interferon-inducible protein
RT encoded by gene 203 from the gene 200 cluster.";
RL Eur. J. Biochem. 249:258-264(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Kidney, Lung, Spleen, 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] (ISOFORM 3).
RC STRAIN=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 INDUCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=17981725; DOI=10.2741/2857;
RA Zhang Y., Tian Q., Du Y., Cao H., Lengyel P., Kong W.;
RT "Multiple splicing results in at least two p203 proteins that are expressed
RT in the liver and down-regulated during liver regeneration.";
RL Front. Biosci. 13:2444-2451(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17981725}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O35368-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O35368-2; Sequence=VSP_033653, VSP_033654;
CC Name=3;
CC IsoId=O35368-3; Sequence=VSP_033652;
CC -!- TISSUE SPECIFICITY: Constitutively expressed in the thymus, bone marrow
CC and spleen. Isoform 1 and isoform 3 are present in liver (at protein
CC level). {ECO:0000269|PubMed:17981725}.
CC -!- INDUCTION: [Isoform 1]: Induced by alpha interferon (at protein level).
CC {ECO:0000269|PubMed:17981725}.
CC -!- INDUCTION: [Isoform 3]: Induced by alpha interferon (at protein level).
CC {ECO:0000269|PubMed:17981725}.
CC -!- SIMILARITY: Belongs to the HIN-200 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE25996.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF022371; AAC53428.1; -; mRNA.
DR EMBL; AK040214; BAC30542.1; -; mRNA.
DR EMBL; AK144663; BAE25996.1; ALT_INIT; mRNA.
DR EMBL; AK164695; BAE37880.1; -; mRNA.
DR EMBL; AK169754; BAE41346.1; -; mRNA.
DR EMBL; AK172505; BAE43039.1; -; mRNA.
DR EMBL; BC008167; AAH08167.1; -; mRNA.
DR RefSeq; NP_001289578.1; NM_001302649.1.
DR RefSeq; NP_001289579.1; NM_001302650.1.
DR RefSeq; NP_001289580.1; NM_001302651.1.
DR AlphaFoldDB; O35368; -.
DR SMR; O35368; -.
DR iPTMnet; O35368; -.
DR PhosphoSitePlus; O35368; -.
DR EPD; O35368; -.
DR jPOST; O35368; -.
DR MaxQB; O35368; -.
DR PRIDE; O35368; -.
DR ProteomicsDB; 273096; -. [O35368-1]
DR ProteomicsDB; 273097; -. [O35368-2]
DR ProteomicsDB; 273098; -. [O35368-3]
DR DNASU; 15950; -.
DR GeneID; 15950; -.
DR KEGG; mmu:15950; -.
DR UCSC; uc007dsj.1; mouse. [O35368-2]
DR CTD; 15950; -.
DR MGI; MGI:96428; Ifi203.
DR eggNOG; ENOG502QTQS; Eukaryota.
DR InParanoid; O35368; -.
DR OrthoDB; 1304994at2759; -.
DR PhylomeDB; O35368; -.
DR BioGRID-ORCS; 15950; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Ifi203; mouse.
DR PRO; PR:O35368; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O35368; protein.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0002218; P:activation of innate immune response; IEA:InterPro.
DR GO; GO:0035458; P:cellular response to interferon-beta; IDA:MGI.
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; 2.
DR Pfam; PF02760; HIN; 1.
DR Pfam; PF02758; PYRIN; 1.
DR SMART; SM01289; PYRIN; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR PROSITE; PS50824; DAPIN; 1.
DR PROSITE; PS50834; HIN_200; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Reference proteome.
FT CHAIN 1..408
FT /note="Interferon-activable protein 203"
FT /id="PRO_0000153720"
FT DOMAIN 1..87
FT /note="Pyrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00061"
FT DOMAIN 190..388
FT /note="HIN-200"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00106"
FT REGION 84..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 183
FT /note="N -> NKKNPVVASFLLASRASTSGAKTREQDILRHKQRPSRKGGFKTTFCE
FT RI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_033652"
FT VAR_SEQ 185..191
FT /note="APRRGTV -> VTLSYPQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033653"
FT VAR_SEQ 192..408
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033654"
FT CONFLICT 51
FT /note="M -> I (in Ref. 2; BAE25996/BAC30542)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="E -> K (in Ref. 2; BAE25996/BAC30542)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="K -> E (in Ref. 2; BAE25996/BAC30542)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="T -> M (in Ref. 2; BAE41346)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="I -> N (in Ref. 2; BAE25996/BAC30542)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="Y -> N (in Ref. 2; BAE25996/BAC30542)"
FT /evidence="ECO:0000305"
FT CONFLICT O35368-3:197
FT /note="R -> Q (in Ref. 3; AAH08167)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 408 AA; 46300 MW; 3BA0E01834D9E5A9 CRC64;
MAEYKNIVLL KGLENMEDYQ FRTVKSLLRK ELKLTKKMQE DYDRIQLADW MEDKFPKDAG
LDKLIKVCEH IKDLKDLAKK LKTEKAKVQE KKKGKCKTAG KKKGQDELSS SESLFINKES
YKSVPSSKKK RKQITKTEGG KKKKLTQEQA QLPETSGTNI KKEEDCLQNP HKSPPTPSSS
SSNKAPRRGT VPKEPSREEG HHQGPKQVMV LKVTEPFTYD FEETKRMFHA TVATETEFFR
VKVFDTALMS KFIPGKIIAI SHYIGCNGFL EIYRASCVSD VNINPTMIIS NTLSESAIAT
PKISYLLSQA KGTFVNGEFV VFKKSERHEC ICYGIGDDTG KMAVVVYGRL TNVRCEPGSK
LRLVCFELTS TKDVCLLRSV RHSYMQVINE GKPLNPDSVR RNSLEPYF
