IN35_MOUSE
ID IN35_MOUSE Reviewed; 286 AA.
AC Q9D8C4; Q3V2E7;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Interferon-induced 35 kDa protein homolog {ECO:0000303|PubMed:29038465};
DE Short=IFP 35 {ECO:0000303|PubMed:29038465};
DE Short=Ifi-35 {ECO:0000303|PubMed:29350881};
GN Name=Ifi35 {ECO:0000312|MGI:MGI:1917360};
GN Synonyms=Ifp35 {ECO:0000303|PubMed:29038465};
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Small intestine, and Stomach;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
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 [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=29038465; DOI=10.1038/s41467-017-00930-9;
RA Xiahou Z., Wang X., Shen J., Zhu X., Xu F., Hu R., Guo D., Li H., Tian Y.,
RA Liu Y., Liang H.;
RT "NMI and IFP35 serve as proinflammatory DAMPs during cellular infection and
RT injury.";
RL Nat. Commun. 8:950-950(2017).
RN [5]
RP FUNCTION.
RX PubMed=29350881; DOI=10.1111/apha.13037;
RA Jian D., Wang W., Zhou X., Jia Z., Wang J., Yang M., Zhao W., Jiang Z.,
RA Hu X., Zhu J.;
RT "Interferon-induced protein 35 inhibits endothelial cell proliferation,
RT migration and re-endothelialization of injured arteries by inhibiting the
RT nuclear factor-kappa B pathway.";
RL Acta Physiol. 223:e13037-e13037(2018).
CC -!- FUNCTION: Acts as a signaling pathway regulator involved in innate
CC immune system response (PubMed:29350881). In response to interferon
CC IFN-alpha, associates in a complex with transcriptional regulator NMI
CC to regulate immune response; the complex formation prevents proteasome-
CC mediated degradation of IFI35 and correlates with IFI35
CC dephosphorylation (By similarity). In complex with NMI, inhibits virus-
CC triggered type I interferon/IFN-beta production (By similarity). In
CC complex with NMI, negatively regulates nuclear factor NF-kappa-B
CC signaling by inhibiting the nuclear translocation, activation and
CC transcription of the NF-kappa-B subunit p65/RELA, resulting in the
CC inhibition of endothelial cell proliferation, migration and re-
CC endothelialization of injured arteries (PubMed:29350881). Beside its
CC role as an intracellular signaling pathway regulator, also functions
CC extracellularly as damage-associated molecular patterns (DAMPs) to
CC promote inflammation when actively released by macrophage to the
CC extracellular space during cell injury and pathogen invasion (By
CC similarity). Macrophage-secreted IFI35 activates NF-kappa-B signaling
CC in adjacent macrophages through Toll-like receptor 4/TLR4 activation,
CC thereby inducing NF-kappa-B translocation from the cytoplasm into the
CC nucleus which promotes the release of pro-inflammatory cytokines (By
CC similarity). {ECO:0000250|UniProtKB:P80217,
CC ECO:0000269|PubMed:29350881}.
CC -!- SUBUNIT: Homodimer. Also interacts with B-ATF. Interacts with TRIM21.
CC Interacts (via NID domains) with NMI (via NID domains); the interaction
CC is direct and is facilitated by TRIM21. {ECO:0000250|UniProtKB:P80217}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P80217}. Nucleus
CC {ECO:0000250|UniProtKB:P80217}. Secreted
CC {ECO:0000250|UniProtKB:P80217}. Note=Cytoplasmic IFI35 localizes in
CC punctate granular structures (By similarity). Nuclear localization
CC increased following IFN-alpha treatment (By similarity). Extracelullar
CC following secretion by macrophage (By similarity).
CC {ECO:0000250|UniProtKB:P80217}.
CC -!- DOMAIN: The NID domain 1 is involved in the negative regulation of
CC p65/RELA transcription and the negative regulation of NF-kappa-B
CC pathway activation. {ECO:0000250|UniProtKB:P80217}.
CC -!- PTM: Phosphorylated. Dephosphorylation correlates with the formation of
CC a complex with NMI. {ECO:0000250|UniProtKB:P80217}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice show decreased inflammatory
CC response when exposed to infection or injury, which can lead to lower
CC inflammation-induced mortality. {ECO:0000269|PubMed:29038465}.
CC -!- SIMILARITY: Belongs to the NMI family. {ECO:0000305}.
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DR EMBL; AK008161; BAB25503.1; -; mRNA.
DR EMBL; AK131884; BAE20851.1; -; mRNA.
DR EMBL; BC008158; AAH08158.1; -; mRNA.
DR CCDS; CCDS25471.1; -.
DR RefSeq; NP_081596.1; NM_027320.4.
DR AlphaFoldDB; Q9D8C4; -.
DR BioGRID; 213868; 1.
DR IntAct; Q9D8C4; 2.
DR STRING; 10090.ENSMUSP00000010502; -.
DR iPTMnet; Q9D8C4; -.
DR PhosphoSitePlus; Q9D8C4; -.
DR EPD; Q9D8C4; -.
DR jPOST; Q9D8C4; -.
DR MaxQB; Q9D8C4; -.
DR PaxDb; Q9D8C4; -.
DR PeptideAtlas; Q9D8C4; -.
DR PRIDE; Q9D8C4; -.
DR ProteomicsDB; 267131; -.
DR Antibodypedia; 29492; 340 antibodies from 25 providers.
DR DNASU; 70110; -.
DR Ensembl; ENSMUST00000010502; ENSMUSP00000010502; ENSMUSG00000010358.
DR GeneID; 70110; -.
DR KEGG; mmu:70110; -.
DR UCSC; uc007lox.1; mouse.
DR CTD; 3430; -.
DR MGI; MGI:1917360; Ifi35.
DR VEuPathDB; HostDB:ENSMUSG00000010358; -.
DR eggNOG; ENOG502QUNN; Eukaryota.
DR GeneTree; ENSGT00530000063686; -.
DR HOGENOM; CLU_047262_1_1_1; -.
DR InParanoid; Q9D8C4; -.
DR OMA; YMSGKIQ; -.
DR OrthoDB; 1133123at2759; -.
DR PhylomeDB; Q9D8C4; -.
DR TreeFam; TF332752; -.
DR BioGRID-ORCS; 70110; 6 hits in 74 CRISPR screens.
DR PRO; PR:Q9D8C4; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9D8C4; protein.
DR Bgee; ENSMUSG00000010358; Expressed in small intestine Peyer's patch and 216 other tissues.
DR ExpressionAtlas; Q9D8C4; baseline and differential.
DR Genevisible; Q9D8C4; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0002281; P:macrophage activation involved in immune response; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IMP:UniProtKB.
DR GO; GO:0045089; P:positive regulation of innate immune response; IMP:UniProtKB.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IMP:UniProtKB.
DR GO; GO:0034145; P:positive regulation of toll-like receptor 4 signaling pathway; ISS:UniProtKB.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR034460; IFP35.
DR InterPro; IPR009909; Nmi/IFP35_dom.
DR InterPro; IPR009938; Nmi/IFP35_N.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR PANTHER; PTHR15225:SF1; PTHR15225:SF1; 1.
DR Pfam; PF07334; IFP_35_N; 1.
DR Pfam; PF07292; NID; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; Immunity; Innate immunity; Nucleus; Phosphoprotein;
KW Reference proteome; Secreted.
FT CHAIN 1..286
FT /note="Interferon-induced 35 kDa protein homolog"
FT /id="PRO_0000159705"
FT DOMAIN 81..170
FT /note="NID 1"
FT /evidence="ECO:0000255"
FT DOMAIN 183..266
FT /note="NID 2"
FT /evidence="ECO:0000255"
FT REGION 5..26
FT /note="Leucine-zipper"
FT CONFLICT 108
FT /note="R -> W (in Ref. 2; AAH08158)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 286 AA; 31876 MW; 51EB0BAAD7054454 CRC64;
MSVTLQTVLY SLQEEQARLK MRLQELQQLK RERTGSPGAK IPFSVPEVPL VFQGQTKQGR
QVPKFVVSNL KVCCPLPEGS ALVTFEDPKV VDRLLQQKEH RVNLEDCRLR VQVQPLELPV
VTNIQVSSQP DNHRVLVSGF PAGLRLSEEE LLDKLEIFFG KAKNGGGDVE TREMLQGTVM
LGFADEEVAQ HLCQIGQFRV PLDRQQVLLR VSPYVSGEIQ KAEIKFQQAP HSVLVTNIPD
VMDAQELHDI LEIHFQKPTR GGGEVEALTV VPSGQQGLAI FTSESS
