GILT_MOUSE
ID GILT_MOUSE Reviewed; 248 AA.
AC Q9ESY9; G3X911; Q3U0F9; Q9EP56;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Gamma-interferon-inducible lysosomal thiol reductase;
DE EC=1.8.-.- {ECO:0000250|UniProtKB:P13284};
DE AltName: Full=Gamma-interferon-inducible protein IP-30;
DE AltName: Full=Lysosomal thiol reductase IP30;
DE Flags: Precursor;
GN Name=Ifi30; Synonyms=Gilt, Ip30;
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 [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, AND FUNCTION.
RC STRAIN=129/SvJ, and C57BL/6J;
RX PubMed=11701933; DOI=10.1126/science.1065500;
RA Maric M., Arunachalam B., Phan U.T., Dong C., Garrett W.S., Cannon K.S.,
RA Alfonso C., Karlsson L., Flavell R.A., Cresswell P.;
RT "Defective antigen processing in GILT-free mice.";
RL Science 294:1361-1365(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Weber D.A., Jun J., Jensen P.E.;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Spleen;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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 [7]
RP DISRUPTION PHENOTYPE, AND FUNCTION IN LISTERIA MONOCYTOGENES INFECTION.
RX PubMed=18815593; DOI=10.1038/nature07344;
RA Singh R., Jamieson A., Cresswell P.;
RT "GILT is a critical host factor for Listeria monocytogenes infection.";
RL Nature 455:1244-1247(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen, and
RC 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 [9]
RP DISRUPTION PHENOTYPE, AND FUNCTION IN CROSS-PRESENTATION OF VIRAL ANTIGEN.
RX PubMed=20538950; DOI=10.1126/science.1189176;
RA Singh R., Cresswell P.;
RT "Defective cross-presentation of viral antigens in GILT-free mice.";
RL Science 328:1394-1398(2010).
CC -!- FUNCTION: Lysosomal thiol reductase that can reduce protein disulfide
CC bonds. May facilitate the complete unfolding of proteins destined for
CC lysosomal degradation. Plays an important role in antigen processing.
CC Facilitates the generation of MHC class II-restricted epitodes from
CC disulfide bond-containing antigen by the endocytic reduction of
CC disulfide bonds. Facilitates also MHC class I-restricted recognition of
CC exogenous antigens containing disulfide bonds by CD8+ T-cells or
CC crosspresentation. {ECO:0000269|PubMed:11701933,
CC ECO:0000269|PubMed:18815593, ECO:0000269|PubMed:20538950}.
CC -!- SUBUNIT: Dimer; disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Lysosome
CC {ECO:0000269|PubMed:11701933}.
CC -!- PTM: N-glycosylated. Sugar chains contain mannose-6-phosphate (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Synthesized as a 35 kDa precursor which is then processed into the
CC mature 30 kDa form via cleavage of N-terminal and C-terminal
CC propeptides. Processing of the precursor is mediated by multiple
CC lysosomal proteases (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice lacking GILT are deficient in generating
CC major histocompatibility complex class-II-restricted CD4(+) T-cell
CC responses to protein antigens that contain disulfide bonds. Mice are
CC partially protected from Listeria monocytogenes infection, they exhibit
CC reduced bacterial replication in spleen and liver. Bacterial escape
CC from the phagosome is impaired in the macrophages of these mice.
CC {ECO:0000269|PubMed:11701933, ECO:0000269|PubMed:18815593,
CC ECO:0000269|PubMed:20538950}.
CC -!- MISCELLANEOUS: Both precursor form and mature form have thiol reductase
CC activity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GILT family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG00598.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF309649; AAG34681.1; -; mRNA.
DR EMBL; AF309650; AAG34682.1; -; Genomic_DNA.
DR EMBL; AF290973; AAG00598.1; ALT_INIT; mRNA.
DR EMBL; AK156914; BAE33895.1; -; mRNA.
DR EMBL; AC162446; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466569; EDL28872.1; -; Genomic_DNA.
DR EMBL; BC054852; AAH54852.1; -; mRNA.
DR RefSeq; NP_075552.2; NM_023065.3.
DR PDB; 6NWX; X-ray; 2.00 A; A/B=49-240.
DR PDBsum; 6NWX; -.
DR AlphaFoldDB; Q9ESY9; -.
DR SMR; Q9ESY9; -.
DR STRING; 10090.ENSMUSP00000034299; -.
DR GlyGen; Q9ESY9; 2 sites.
DR PhosphoSitePlus; Q9ESY9; -.
DR EPD; Q9ESY9; -.
DR MaxQB; Q9ESY9; -.
DR PaxDb; Q9ESY9; -.
DR PeptideAtlas; Q9ESY9; -.
DR PRIDE; Q9ESY9; -.
DR ProteomicsDB; 267793; -.
DR Antibodypedia; 27932; 173 antibodies from 29 providers.
DR DNASU; 65972; -.
DR Ensembl; ENSMUST00000222087; ENSMUSP00000159394; ENSMUSG00000031838.
DR GeneID; 65972; -.
DR KEGG; mmu:65972; -.
DR UCSC; uc009mbm.1; mouse.
DR CTD; 10437; -.
DR MGI; MGI:2137648; Ifi30.
DR eggNOG; KOG3160; Eukaryota.
DR GeneTree; ENSGT00390000010450; -.
DR HOGENOM; CLU_066886_0_0_1; -.
DR InParanoid; Q9ESY9; -.
DR OMA; EACVLDQ; -.
DR OrthoDB; 803513at2759; -.
DR PhylomeDB; Q9ESY9; -.
DR TreeFam; TF315141; -.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR BioGRID-ORCS; 65972; 3 hits in 68 CRISPR screens.
DR ChiTaRS; Ifi30; mouse.
DR PRO; PR:Q9ESY9; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9ESY9; protein.
DR Bgee; ENSMUSG00000031838; Expressed in spleen and 71 other tissues.
DR Genevisible; Q9ESY9; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; TAS:MGI.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016667; F:oxidoreductase activity, acting on a sulfur group of donors; ISS:UniProtKB.
DR GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IEA:InterPro.
DR GO; GO:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; IMP:UniProtKB.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IMP:MGI.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:MGI.
DR GO; GO:0050821; P:protein stabilization; IMP:MGI.
DR InterPro; IPR004911; Interferon-induced_GILT.
DR PANTHER; PTHR13234; PTHR13234; 1.
DR Pfam; PF03227; GILT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Immunity; Lysosome;
KW Oxidoreductase; Redox-active center; Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PROPEP 27..54
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P13284"
FT /id="PRO_0000406221"
FT CHAIN 55..230
FT /note="Gamma-interferon-inducible lysosomal thiol
FT reductase"
FT /id="PRO_0000406222"
FT PROPEP 231..248
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P13284"
FT /id="PRO_0000406223"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 69..72
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:P13284"
FT CONFLICT 42
FT /note="A -> V (in Ref. 1; AAG34681/AAG34682, 2; AAG00598
FT and 6; AAH54852)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="F -> Y (in Ref. 3; BAE33895)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="V -> C (in Ref. 2; AAG00598)"
FT /evidence="ECO:0000305"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:6NWX"
FT HELIX 70..78
FT /evidence="ECO:0007829|PDB:6NWX"
FT HELIX 80..87
FT /evidence="ECO:0007829|PDB:6NWX"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:6NWX"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:6NWX"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:6NWX"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:6NWX"
FT HELIX 118..133
FT /evidence="ECO:0007829|PDB:6NWX"
FT HELIX 136..147
FT /evidence="ECO:0007829|PDB:6NWX"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:6NWX"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:6NWX"
FT HELIX 156..163
FT /evidence="ECO:0007829|PDB:6NWX"
FT HELIX 169..177
FT /evidence="ECO:0007829|PDB:6NWX"
FT HELIX 179..193
FT /evidence="ECO:0007829|PDB:6NWX"
FT STRAND 200..207
FT /evidence="ECO:0007829|PDB:6NWX"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:6NWX"
FT HELIX 218..225
FT /evidence="ECO:0007829|PDB:6NWX"
FT HELIX 233..238
FT /evidence="ECO:0007829|PDB:6NWX"
SQ SEQUENCE 248 AA; 27784 MW; 41BE0390FDAADFC8 CRC64;
MSWSPILPFL SLLLLLFPLE VPRAATASLS QASSEGTTTC KAHDVCLLGP RPLPPSPPVR
VSLYYESLCG ACRYFLVRDL FPTWLMVMEI MNITLVPYGN AQERNVSGTW EFTCQHGELE
CRLNMVEACL LDKLEKEAAF LTIVCMEEMD DMEKKLGPCL QVYAPEVSPE SIMECATGKR
GTQLMHENAQ LTDALHPPHE YVPWVLVNEK PLKDPSELLS IVCQLYQGTE KPDICSSIAD
SPRKVCYK
