IFI27_HUMAN
ID IFI27_HUMAN Reviewed; 122 AA.
AC P40305; A0A087WZF8; A8K0H0; Q53YA6; Q6IEC1; Q7Z5R0; Q7Z5R1; Q7Z5R2; Q96BK3;
AC Q9H4B1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 4.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Interferon alpha-inducible protein 27, mitochondrial {ECO:0000305};
DE Short=p27;
DE AltName: Full=Interferon alpha-induced 11.5 kDa protein;
DE AltName: Full=Interferon-stimulated gene 12a protein {ECO:0000303|PubMed:14728724};
DE Short=ISG12(a) {ECO:0000303|PubMed:14728724};
DE Short=ISG12A {ECO:0000303|PubMed:27673746};
DE Flags: Precursor;
GN Name=IFI27 {ECO:0000312|HGNC:HGNC:5397};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=8358738;
RA Rasmussen U.B., Wolf C., Mattei M.-G., Chenard M.P., Bellocq J.-P.,
RA Chambon P., Rio M.C., Basset P.;
RT "Identification of a new interferon-alpha-inducible gene (p27) on human
RT chromosome 14q32 and its expression in breast carcinoma.";
RL Cancer Res. 53:4096-4101(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum, and Stomach;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Uterus;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-60 (ISOFORM 1), AND SUBCELLULAR LOCATION.
RX PubMed=11722583; DOI=10.1046/j.0014-2956.2001.02545.x;
RA Martensen P.M., Sogaard T.M., Gjermandsen I.M., Buttenschon H.N.,
RA Rossing A.B., Bonnevie-Nielsen V., Rosada C., Simonsen J.L., Justesen J.;
RT "The interferon alpha induced protein ISG12 is localized to the nuclear
RT membrane.";
RL Eur. J. Biochem. 268:5947-5954(2001).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-60 (ISOFORMS 2; 3 AND 4).
RX PubMed=12878323; DOI=10.1016/s0925-4439(03)00087-5;
RA Smidt K.C., Hansen L.L., Soegaard T.M., Petersen L.K., Knudsen U.B.,
RA Martensen P.M.;
RT "A nine-nucleotide deletion and splice variation in the coding region of
RT the interferon induced ISG12 gene.";
RL Biochim. Biophys. Acta 1638:227-234(2003).
RN [10]
RP IDENTIFICATION, AND INDUCTION.
RX PubMed=14728724; DOI=10.1186/1471-2164-5-8;
RA Parker N., Porter A.C.G.;
RT "Identification of a novel gene family that includes the interferon-
RT inducible human genes 6-16 and ISG12.";
RL BMC Genomics 5:8-8(2004).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND TRANSIT PEPTIDE.
RX PubMed=18330707; DOI=10.1007/s10495-008-0190-0;
RA Rosebeck S., Leaman D.W.;
RT "Mitochondrial localization and pro-apoptotic effects of the interferon-
RT inducible protein ISG12a.";
RL Apoptosis 13:562-572(2008).
RN [12]
RP FUNCTION, INTERACTION WITH NR4A1, SUBCELLULAR LOCATION, AND INDUCTION BY
RP INTERFERON.
RX PubMed=22427340; DOI=10.1161/circresaha.111.258814;
RA Papac-Milicevic N., Breuss J.M., Zaujec J., Ryban L., Plyushch T.,
RA Wagner G.A., Fenzl S., Dremsek P., Cabaravdic M., Steiner M., Glass C.K.,
RA Binder C.J., Uhrin P., Binder B.R.;
RT "The interferon stimulated gene 12 inactivates vasculoprotective functions
RT of NR4A nuclear receptors.";
RL Circ. Res. 110:E50-E63(2012).
RN [13]
RP FUNCTION.
RX PubMed=24970806; DOI=10.18632/oncotarget.2067;
RA Liu N., Zuo C., Wang X., Chen T., Yang D., Wang J., Zhu H.;
RT "miR-942 decreases TRAIL-induced apoptosis through ISG12a downregulation
RT and is regulated by AKT.";
RL Oncotarget 5:4959-4971(2014).
RN [14]
RP FUNCTION, INTERACTION WITH SKP2 AND HEPATITIS C VIRUS NON-STRUCTURAL
RP PROTEIN NS5A, AND REGION.
RX PubMed=27194766; DOI=10.1128/jvi.00352-16;
RA Xue B., Yang D., Wang J., Xu Y., Wang X., Qin Y., Tian R., Chen S., Xie Q.,
RA Liu N., Zhu H.;
RT "ISG12a Restricts Hepatitis C Virus Infection through the Ubiquitination-
RT Dependent Degradation Pathway.";
RL J. Virol. 90:6832-6845(2016).
RN [15]
RP FUNCTION, SUBUNIT, INTERACTION WITH BCL-2, SUBCELLULAR LOCATION,
RP ALTERNATIVE SPLICING, AND MUTAGENESIS OF PHE-56 AND ALA-96.
RX PubMed=27673746; DOI=10.1111/boc.201600034;
RA Gytz H., Hansen M.F., Skovbjerg S., Kristensen A.C., Hoerlyck S.,
RA Jensen M.B., Fredborg M., Markert L.D., McMillan N.A., Christensen E.I.,
RA Martensen P.M.;
RT "Apoptotic properties of the type 1 interferon induced family of human
RT mitochondrial membrane ISG12 proteins.";
RL Biol. Cell 109:94-112(2017).
RN [16]
RP FUNCTION, AND INDUCTION BY INTERFERON.
RX PubMed=27777077; DOI=10.1016/j.virusres.2016.10.013;
RA Chen Y., Jiao B., Yao M., Shi X., Zheng Z., Li S., Chen L.;
RT "ISG12a inhibits HCV replication and potentiates the anti-HCV activity of
RT IFN-alpha through activation of the Jak/STAT signaling pathway independent
RT of autophagy and apoptosis.";
RL Virus Res. 227:231-239(2017).
CC -!- FUNCTION: Probable adapter protein involved in different biological
CC processes (PubMed:22427340, PubMed:27194766). Part of the signaling
CC pathways that lead to apoptosis (PubMed:18330707, PubMed:27673746,
CC PubMed:24970806). Involved in type-I interferon-induced apoptosis
CC characterized by a rapid and robust release of cytochrome C from the
CC mitochondria and activation of BAX and caspases 2, 3, 6, 8 and 9
CC (PubMed:18330707, PubMed:27673746). Also functions in TNFSF10-induced
CC apoptosis (PubMed:24970806). May also have a function in the nucleus,
CC where it may be involved in the interferon-induced negative regulation
CC of the transcriptional activity of NR4A1, NR4A2 and NR4A3 through the
CC enhancement of XPO1-mediated nuclear export of these nuclear receptors
CC (PubMed:22427340). May thereby play a role in the vascular response to
CC injury (By similarity). In the innate immune response, has an antiviral
CC activity towards hepatitis C virus/HCV (PubMed:27194766,
CC PubMed:27777077). May prevent the replication of the virus by
CC recruiting both the hepatitis C virus non-structural protein 5A/NS5A
CC and the ubiquitination machinery via SKP2, promoting the ubiquitin-
CC mediated proteasomal degradation of NS5A (PubMed:27194766,
CC PubMed:27777077). {ECO:0000250|UniProtKB:Q8R412,
CC ECO:0000269|PubMed:18330707, ECO:0000269|PubMed:22427340,
CC ECO:0000269|PubMed:24970806, ECO:0000269|PubMed:27194766,
CC ECO:0000269|PubMed:27673746, ECO:0000269|PubMed:27777077}.
CC -!- SUBUNIT: Homodimer (PubMed:27673746). Interacts with hepatitis C
CC virus/HCV non-structural protein NS5A; promotes the ubiquitin-mediated
CC proteasomal degradation of NS5A (PubMed:27194766). Interacts with SKP2;
CC promotes the ubiquitin-mediated proteasomal degradation of NS5A
CC (PubMed:27194766). Interacts with NR4A1 (PubMed:22427340). May interact
CC with BCL2 (PubMed:27673746). {ECO:0000269|PubMed:22427340,
CC ECO:0000269|PubMed:27194766, ECO:0000269|PubMed:27673746}.
CC -!- INTERACTION:
CC P40305-1; P55056: APOC4; NbExp=3; IntAct=EBI-23832675, EBI-18302142;
CC P40305-2; P22736: NR4A1; NbExp=8; IntAct=EBI-27124263, EBI-721550;
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:18330707, ECO:0000269|PubMed:27673746}; Multi-pass
CC membrane protein {ECO:0000255}. Nucleus inner membrane
CC {ECO:0000269|PubMed:11722583, ECO:0000269|PubMed:22427340}; Multi-pass
CC membrane protein {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:22427340}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Exclusive localizations in either the nucleus or
CC the mitochondrion have been reported. {ECO:0000269|PubMed:22427340,
CC ECO:0000269|PubMed:27673746}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=ISG12 {ECO:0000303|PubMed:12878323}, ISG12A
CC {ECO:0000303|PubMed:27673746};
CC IsoId=P40305-2; Sequence=Displayed;
CC Name=2; Synonyms=ISG12delta {ECO:0000303|PubMed:12878323}, ISG12Adelta
CC {ECO:0000303|PubMed:27673746};
CC IsoId=P40305-1; Sequence=VSP_059909;
CC Name=3; Synonyms=ISG12-S {ECO:0000303|PubMed:12878323}, ISG12A-S
CC {ECO:0000303|PubMed:27673746};
CC IsoId=P40305-3; Sequence=VSP_059908;
CC Name=4; Synonyms=ISG12-Sdelta {ECO:0000303|PubMed:12878323},
CC ISG12A-Sdelta {ECO:0000303|PubMed:27673746};
CC IsoId=P40305-4; Sequence=VSP_059907;
CC -!- INDUCTION: Up-regulated by type-I and type-II interferons.
CC {ECO:0000269|PubMed:14728724, ECO:0000269|PubMed:18330707,
CC ECO:0000269|PubMed:22427340, ECO:0000269|PubMed:27777077}.
CC -!- MISCELLANEOUS: [Isoform 3]: Major isoform in blood and cervix.
CC {ECO:0000269|PubMed:12878323}.
CC -!- SIMILARITY: Belongs to the IFI6/IFI27 family. {ECO:0000305}.
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DR EMBL; X67325; CAA47739.1; -; mRNA.
DR EMBL; BT006781; AAP35427.1; -; mRNA.
DR EMBL; AK289535; BAF82224.1; -; mRNA.
DR EMBL; AK312089; BAG35025.1; -; mRNA.
DR EMBL; AM393107; CAL37985.1; -; mRNA.
DR EMBL; AL079302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL121838; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF573698; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW81556.1; -; Genomic_DNA.
DR EMBL; CH471061; EAW81557.1; -; Genomic_DNA.
DR EMBL; CH471061; EAW81558.1; -; Genomic_DNA.
DR EMBL; BC015492; AAH15492.1; -; mRNA.
DR EMBL; AJ294851; CAC10503.2; -; mRNA.
DR EMBL; AY126456; AAM95743.1; -; mRNA.
DR EMBL; AY126457; AAM95744.1; -; mRNA.
DR EMBL; AY126458; AAM95745.1; -; mRNA.
DR EMBL; BN000227; CAE00394.1; -; mRNA.
DR CCDS; CCDS32148.1; -. [P40305-2]
DR PIR; I38081; I38081.
DR RefSeq; NP_001123552.1; NM_001130080.2. [P40305-2]
DR RefSeq; NP_001275881.1; NM_001288952.1. [P40305-2]
DR RefSeq; NP_001275883.1; NM_001288954.1. [P40305-1]
DR RefSeq; NP_001275885.1; NM_001288956.1. [P40305-2]
DR RefSeq; NP_001275886.1; NM_001288957.1. [P40305-1]
DR RefSeq; NP_001275887.1; NM_001288958.1. [P40305-1]
DR RefSeq; NP_001275888.1; NM_001288959.1. [P40305-3]
DR RefSeq; NP_001275889.1; NM_001288960.1. [P40305-4]
DR RefSeq; NP_001275924.1; NM_001288995.1. [P40305-1]
DR RefSeq; NP_005523.3; NM_005532.4. [P40305-1]
DR AlphaFoldDB; P40305; -.
DR BioGRID; 109655; 7.
DR IntAct; P40305; 17.
DR STRING; 9606.ENSP00000483430; -.
DR iPTMnet; P40305; -.
DR PhosphoSitePlus; P40305; -.
DR BioMuta; IFI27; -.
DR DMDM; 116242590; -.
DR jPOST; P40305; -.
DR MassIVE; P40305; -.
DR MaxQB; P40305; -.
DR PaxDb; P40305; -.
DR PeptideAtlas; P40305; -.
DR PRIDE; P40305; -.
DR ProteomicsDB; 55359; -.
DR ProteomicsDB; 69349; -.
DR Antibodypedia; 27000; 122 antibodies from 18 providers.
DR DNASU; 3429; -.
DR Ensembl; ENST00000612813.4; ENSP00000483430.1; ENSG00000165949.13. [P40305-2]
DR Ensembl; ENST00000612838.4; ENSP00000483932.1; ENSG00000275214.4. [P40305-2]
DR Ensembl; ENST00000613997.4; ENSP00000484089.1; ENSG00000275214.4. [P40305-2]
DR Ensembl; ENST00000615978.4; ENSP00000483291.1; ENSG00000275214.4. [P40305-3]
DR Ensembl; ENST00000616764.5; ENSP00000477753.1; ENSG00000165949.13. [P40305-2]
DR Ensembl; ENST00000618863.1; ENSP00000482635.1; ENSG00000165949.13. [P40305-3]
DR Ensembl; ENST00000621160.5; ENSP00000483498.1; ENSG00000165949.13. [P40305-2]
DR Ensembl; ENST00000627111.2; ENSP00000486608.1; ENSG00000275214.4. [P40305-2]
DR GeneID; 3429; -.
DR KEGG; hsa:3429; -.
DR UCSC; uc032bkg.2; human.
DR UCSC; uc032bkj.2; human.
DR UCSC; uc059erm.1; human.
DR CTD; 3429; -.
DR DisGeNET; 3429; -.
DR GeneCards; IFI27; -.
DR HGNC; HGNC:5397; IFI27.
DR HPA; ENSG00000165949; Low tissue specificity.
DR MIM; 600009; gene.
DR neXtProt; NX_P40305; -.
DR OpenTargets; ENSG00000165949; -.
DR PharmGKB; PA29643; -.
DR VEuPathDB; HostDB:ENSG00000165949; -.
DR eggNOG; ENOG502S85T; Eukaryota.
DR GeneTree; ENSGT00940000164233; -.
DR HOGENOM; CLU_142338_3_0_1; -.
DR InParanoid; P40305; -.
DR OMA; SHCAHAV; -.
DR PhylomeDB; P40305; -.
DR TreeFam; TF340510; -.
DR PathwayCommons; P40305; -.
DR Reactome; R-HSA-909733; Interferon alpha/beta signaling.
DR SignaLink; P40305; -.
DR BioGRID-ORCS; 3429; 5 hits in 1082 CRISPR screens.
DR ChiTaRS; IFI27; human.
DR GeneWiki; IFI27; -.
DR GenomeRNAi; 3429; -.
DR Pharos; P40305; Tbio.
DR PRO; PR:P40305; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P40305; protein.
DR Bgee; ENSG00000165949; Expressed in right lung and 98 other tissues.
DR ExpressionAtlas; P40305; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0005637; C:nuclear inner membrane; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0005521; F:lamin binding; IDA:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:MGI.
DR GO; GO:0006915; P:apoptotic process; IDA:UniProtKB.
DR GO; GO:0097190; P:apoptotic signaling pathway; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
DR GO; GO:0044827; P:modulation by host of viral genome replication; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IMP:UniProtKB.
DR GO; GO:0046825; P:regulation of protein export from nucleus; IGI:MGI.
DR GO; GO:0060337; P:type I interferon signaling pathway; IMP:UniProtKB.
DR Gene3D; 6.10.110.10; -; 1.
DR InterPro; IPR009311; IFI6/IFI27-like.
DR InterPro; IPR038213; IFI6/IFI27-like_sf.
DR PANTHER; PTHR16932; PTHR16932; 1.
DR Pfam; PF06140; Ifi-6-16; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Antiviral defense; Apoptosis; Endoplasmic reticulum;
KW Host-virus interaction; Immunity; Innate immunity; Membrane; Mitochondrion;
KW Nucleus; Reference proteome; Transcription; Transcription regulation;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000305|PubMed:18330707"
FT CHAIN 34..122
FT /note="Interferon alpha-inducible protein 27,
FT mitochondrial"
FT /id="PRO_0000147372"
FT TRANSMEM 34..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 76..122
FT /note="Mediates interaction with SKP2 and hepatitis C virus
FT non-structural protein NS5A"
FT /evidence="ECO:0000269|PubMed:27194766"
FT REGION 103..112
FT /note="Required for hepatitis C virus non-structural
FT protein NS5A degradation"
FT /evidence="ECO:0000269|PubMed:27194766"
FT VAR_SEQ 1..48
FT /note="Missing (in isoform 4)"
FT /id="VSP_059907"
FT VAR_SEQ 1..43
FT /note="Missing (in isoform 3)"
FT /id="VSP_059908"
FT VAR_SEQ 43..45
FT /note="Missing (in isoform 2)"
FT /id="VSP_059909"
FT VARIANT 109
FT /note="S -> F (in dbSNP:rs2227974)"
FT /id="VAR_028066"
FT MUTAGEN 56
FT /note="F->D: Increased pro-apoptotic activity; when
FT associated with D-96."
FT /evidence="ECO:0000269|PubMed:27673746"
FT MUTAGEN 96
FT /note="A->D: Increased pro-apoptotic activity; when
FT associated with D-56."
FT /evidence="ECO:0000269|PubMed:27673746"
FT CONFLICT 89
FT /note="A -> G (in Ref. 1; CAA47739)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 122 AA; 11542 MW; A424B2EDEAA678A3 CRC64;
MEASALTSSA VTSVAKVVRV ASGSAVVLPL ARIATVVIGG VVAMAAVPMV LSAMGFTAAG
IASSSIAAKM MSAAAIANGG GVASGSLVAT LQSLGATGLS GLTKFILGSI GSAIAAVIAR
FY
