IF44L_HUMAN
ID IF44L_HUMAN Reviewed; 452 AA.
AC Q53G44; Q86TE1; Q96B64; Q99984;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 3.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Interferon-induced protein 44-like;
GN Name=IFI44L; Synonyms=C1orf29; ORFNames=GS3686;
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 1), AND VARIANTS ARG-73 AND THR-235.
RC TISSUE=Cancellous bone;
RA Ohno I., Hashimoto J., Takaoka K., Ochi T., Okubo K., Matsubara K.;
RT "The cloning of a cDNA for novel genes expressed in human osteoblast.";
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ARG-73;
RP ILE-217 AND CYS-296.
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ARG-73.
RC TISSUE=Spinal cord;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP FUNCTION, AND INDUCTION.
RX PubMed=21478870; DOI=10.1038/nature09907;
RA Schoggins J.W., Wilson S.J., Panis M., Murphy M.Y., Jones C.T.,
RA Bieniasz P., Rice C.M.;
RT "A diverse range of gene products are effectors of the type I interferon
RT antiviral response.";
RL Nature 472:481-485(2011).
RN [7]
RP FUNCTION, AND INTERACTION WITH FKBP5.
RX PubMed=31434731; DOI=10.1128/jvi.01159-19;
RA DeDiego M.L., Martinez-Sobrido L., Topham D.J.;
RT "Novel Functions of IFI44L as a Feedback Regulator of Host Antiviral
RT Responses.";
RL J. Virol. 93:0-0(2019).
RN [8]
RP FUNCTION.
RX PubMed=32611756; DOI=10.1128/jvi.00297-20;
RA Busse D.C., Habgood-Coote D., Clare S., Brandt C., Bassano I., Kaforou M.,
RA Herberg J., Levin M., Eleouet J.F., Kellam P., Tregoning J.S.;
RT "Interferon-Induced Protein 44 and Interferon-Induced Protein 44-Like
RT Restrict Replication of Respiratory Syncytial Virus.";
RL J. Virol. 94:0-0(2020).
RN [9]
RP FUNCTION, AND INDUCTION BY M.TUBERCULOSIS INFECTION.
RX PubMed=34722780; DOI=10.1155/2021/5599408;
RA Jiang H., Tsang L., Wang H., Liu C.;
RT "IFI44L as a Forward Regulator Enhancing Host Antituberculosis Responses.";
RL J. Immunol. Res. 2021:5599408-5599408(2021).
CC -!- FUNCTION: Type I interferon-stimulated gene (ISG) that plays a critical
CC role in antiviral and antibacterial activity (PubMed:34722780). During
CC bacterial infection, promotes macrophage differentiation and
CC facilitates inflammatory cytokine secretion (PubMed:34722780). Plays a
CC role in the control of respiratory syncytial virus/RSV infection,
CC reducing the ability of the virus to replicate (PubMed:32611756).
CC Exhibits a low antiviral activity against hepatitis C virus
CC (PubMed:21478870). Acts also as a feedback regulator of IFN responses
CC by negatively regulating IKBKB and IKBKE kinase activities through
CC interaction with FKBP5 (PubMed:31434731). {ECO:0000269|PubMed:21478870,
CC ECO:0000269|PubMed:31434731, ECO:0000269|PubMed:32611756,
CC ECO:0000269|PubMed:34722780}.
CC -!- SUBUNIT: Interacts with FKBP5; this interaction modulates IKBKB and
CC IKBKE kinase activities. {ECO:0000269|PubMed:31434731}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q53G44-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q53G44-2; Sequence=VSP_036554, VSP_036555;
CC -!- INDUCTION: By type I interferons (PubMed:21478870). By M. tuberculosis
CC infection (PubMed:34722780). {ECO:0000269|PubMed:21478870,
CC ECO:0000269|PubMed:34722780}.
CC -!- SIMILARITY: Belongs to the IFI44 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH15932.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA19056.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD96807.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB000115; BAA19056.1; ALT_FRAME; mRNA.
DR EMBL; AK223087; BAD96807.1; ALT_INIT; mRNA.
DR EMBL; AL832618; CAD90004.1; -; mRNA.
DR EMBL; AC104837; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015932; AAH15932.1; ALT_INIT; mRNA.
DR CCDS; CCDS687.2; -. [Q53G44-1]
DR RefSeq; NP_006811.2; NM_006820.3. [Q53G44-1]
DR RefSeq; XP_011538841.1; XM_011540539.2.
DR AlphaFoldDB; Q53G44; -.
DR BioGRID; 116163; 11.
DR IntAct; Q53G44; 1.
DR STRING; 9606.ENSP00000359787; -.
DR PhosphoSitePlus; Q53G44; -.
DR BioMuta; IFI44L; -.
DR DMDM; 224471886; -.
DR jPOST; Q53G44; -.
DR MassIVE; Q53G44; -.
DR PaxDb; Q53G44; -.
DR PeptideAtlas; Q53G44; -.
DR PRIDE; Q53G44; -.
DR ProteomicsDB; 62472; -. [Q53G44-1]
DR ProteomicsDB; 62473; -. [Q53G44-2]
DR Antibodypedia; 33500; 133 antibodies from 20 providers.
DR DNASU; 10964; -.
DR Ensembl; ENST00000370751.10; ENSP00000359787.4; ENSG00000137959.17. [Q53G44-1]
DR GeneID; 10964; -.
DR KEGG; hsa:10964; -.
DR MANE-Select; ENST00000370751.10; ENSP00000359787.4; NM_006820.4; NP_006811.2.
DR UCSC; uc010oro.2; human. [Q53G44-1]
DR CTD; 10964; -.
DR DisGeNET; 10964; -.
DR GeneCards; IFI44L; -.
DR HGNC; HGNC:17817; IFI44L.
DR HPA; ENSG00000137959; Tissue enhanced (salivary).
DR MIM; 613975; gene.
DR neXtProt; NX_Q53G44; -.
DR OpenTargets; ENSG00000137959; -.
DR PharmGKB; PA25615; -.
DR VEuPathDB; HostDB:ENSG00000137959; -.
DR eggNOG; ENOG502QQ57; Eukaryota.
DR GeneTree; ENSGT00940000163189; -.
DR HOGENOM; CLU_049888_3_0_1; -.
DR InParanoid; Q53G44; -.
DR OMA; MDDIPHI; -.
DR OrthoDB; 570957at2759; -.
DR PhylomeDB; Q53G44; -.
DR TreeFam; TF328728; -.
DR PathwayCommons; Q53G44; -.
DR SignaLink; Q53G44; -.
DR BioGRID-ORCS; 10964; 11 hits in 1073 CRISPR screens.
DR ChiTaRS; IFI44L; human.
DR GenomeRNAi; 10964; -.
DR Pharos; Q53G44; Tbio.
DR PRO; PR:Q53G44; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q53G44; protein.
DR Bgee; ENSG00000137959; Expressed in monocyte and 186 other tissues.
DR ExpressionAtlas; Q53G44; baseline and differential.
DR Genevisible; Q53G44; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR024644; IFI44_fam.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006571; TLDc_dom.
DR PANTHER; PTHR14241:SF2; PTHR14241:SF2; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51886; TLDC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Antiviral defense; Cytoplasm; Reference proteome.
FT CHAIN 1..452
FT /note="Interferon-induced protein 44-like"
FT /id="PRO_0000337845"
FT DOMAIN 1..159
FT /note="TLDc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01234"
FT VAR_SEQ 161
FT /note="I -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_036554"
FT VAR_SEQ 162..452
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_036555"
FT VARIANT 73
FT /note="H -> R (in dbSNP:rs273259)"
FT /evidence="ECO:0000269|PubMed:17974005, ECO:0000269|Ref.1,
FT ECO:0000269|Ref.2"
FT /id="VAR_054648"
FT VARIANT 104
FT /note="A -> T (in dbSNP:rs34932081)"
FT /id="VAR_054649"
FT VARIANT 148
FT /note="R -> C (in dbSNP:rs273258)"
FT /id="VAR_054650"
FT VARIANT 217
FT /note="V -> I (in dbSNP:rs3820093)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_054651"
FT VARIANT 235
FT /note="I -> T (in dbSNP:rs987495)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_054652"
FT VARIANT 296
FT /note="R -> C (in dbSNP:rs1981071)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_054653"
FT VARIANT 390
FT /note="M -> I (in dbSNP:rs35466823)"
FT /id="VAR_043726"
FT CONFLICT 54
FT /note="A -> V (in Ref. 3; CAD90004)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="E -> G (in Ref. 3; CAD90004)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 452 AA; 51322 MW; E12E2DAF00547D7F CRC64;
MEVTTRLTWN DENHLRKLLG NVSLSLLYKS SVHGGSIEDM VERCSRQGCT ITMAYIDYNM
IVAFMLGNYI NLHESSTEPN DSLWFSLQKK NDTTEIETLL LNTAPKIIDE QLVCRLSKTD
IFIICRDNKI YLDKMITRNL KLRFYGHRQY LECEVFRVEG IKDNLDDIKR IIKAREHRNR
LLADIRDYRP YADLVSEIRI LLVGPVGSGK SSFFNSVKSI FHGHVTGQAV VGSDITSITE
RYRIYSVKDG KNGKSLPFML CDTMGLDGAE GAGLCMDDIP HILKGCMPDR YQFNSRKPIT
PEHSTFITSP SLKDRIHCVA YVLDINSIDN LYSKMLAKVK QVHKEVLNCG IAYVALLTKV
DDCSEVLQDN FLNMSRSMTS QSRVMNVHKM LGIPISNILM VGNYASDLEL DPMKDILILS
ALRQMLRAAD DFLEDLPLEE TGAIERALQP CI
