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Protein

Gamma-interferon-inducible lysosomal thiol reductase

Gene

IFI30

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Lysosomal thiol reductase that can reduce protein disulfide bonds. May facilitate the complete unfolding of proteins destined for lysosomal degradation. Plays an important role in antigen processing. Facilitates the generation of MHC class II-restricted epitodes from disulfide bond-containing antigen by the endocytic reduction of disulfide bonds (By similarity). Facilitates also MHC class I-restricted recognition of exogenous antigens containing disulfide bonds by CD8+ T-cells or crosspresentation (By similarity).By similarity

Kineticsi

Kinetic parameters shown are for mature enzyme.

  1. KM=1200 µM for F(ab')2 fragment when denatured1 Publication
  2. KM=10 µM for F(ab')2 fragment1 Publication

    pH dependencei

    Optimum pH is 4-5.1 Publication

    GO - Molecular functioni

    • oxidoreductase activity, acting on a sulfur group of donors Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Immunity

    Enzyme and pathway databases

    ReactomeiREACT_121399. MHC class II antigen presentation.
    REACT_25078. Interferon gamma signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Gamma-interferon-inducible lysosomal thiol reductase (EC:1.8.-.-)
    Alternative name(s):
    Gamma-interferon-inducible protein IP-30
    Legumaturain
    Gene namesi
    Name:IFI30
    Synonyms:GILT, IP30
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:5398. IFI30.

    Subcellular locationi

    GO - Cellular componenti

    • cell junction Source: HPA
    • cytoplasm Source: HPA
    • extracellular region Source: ProtInc
    • intracellular membrane-bounded organelle Source: HPA
    • lysosomal lumen Source: Reactome
    • lysosome Source: UniProtKB
    • plasma membrane Source: HPA
    Complete GO annotation...

    Keywords - Cellular componenti

    Lysosome, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi72 – 721C → S: Abolishes reducing activity, does not affect dimerization. Abolishes reducing activity; when associated with S-75. 2 Publications
    Mutagenesisi75 – 751C → S: Abolishes reducing activity, does not affect dimerization. Abolishes reducing activity; when associated with S-72. 2 Publications

    Organism-specific databases

    PharmGKBiPA29644.

    Polymorphism and mutation databases

    BioMutaiIFI30.
    DMDMi327478582.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Sequence AnalysisAdd
    BLAST
    Propeptidei27 – 5731Removed in mature form1 PublicationPRO_0000021328Add
    BLAST
    Chaini58 – 232175Gamma-interferon-inducible lysosomal thiol reductasePRO_0000021329Add
    BLAST
    Propeptidei233 – 25018Removed in mature form1 PublicationPRO_0000021330Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi63 – 631N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi72 ↔ 75Redox-active
    Glycosylationi95 – 951N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi108 – 1081N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated. Sugar chains contain mannose-6-phosphate.2 Publications
    Synthesized as a 35 kDa precursor which is then processed into the mature 30 kDa form via cleavage of N-terminal and C-terminal propeptides. Processing of the precursor is mediated by multiple lysosomal proteases.

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP13284.
    PaxDbiP13284.
    PRIDEiP13284.

    PTM databases

    PhosphoSiteiP13284.

    Expressioni

    Inductioni

    Expressed constitutively in antigen-presenting cells and induced by IFN-gamma in other cell types.1 Publication

    Gene expression databases

    BgeeiP13284.
    CleanExiHS_IFI30.
    ExpressionAtlasiP13284. baseline.
    GenevisibleiP13284. HS.

    Organism-specific databases

    HPAiHPA026650.

    Interactioni

    Subunit structurei

    Dimer; disulfide-linked.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    KRTAP4-12Q9BQ663EBI-2868897,EBI-739863
    NOTCH2NLQ7Z3S93EBI-2868897,EBI-945833

    Protein-protein interaction databases

    BioGridi115704. 26 interactions.
    IntActiP13284. 4 interactions.
    STRINGi9606.ENSP00000384886.

    Structurei

    3D structure databases

    ProteinModelPortaliP13284.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GILT family.Curated

    Keywords - Domaini

    Redox-active center, Signal

    Phylogenomic databases

    eggNOGiNOG315223.
    GeneTreeiENSGT00390000010450.
    HOGENOMiHOG000238423.
    HOVERGENiHBG005837.
    InParanoidiP13284.
    KOiK08059.
    OMAiMHANAQR.
    PhylomeDBiP13284.
    TreeFamiTF315141.

    Family and domain databases

    InterProiIPR004911. Interferon-induced_GILT.
    [Graphical view]
    PANTHERiPTHR13234. PTHR13234. 1 hit.
    PfamiPF03227. GILT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P13284-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTLSPLLLFL PPLLLLLDVP TAAVQASPLQ ALDFFGNGPP VNYKTGNLYL
    60 70 80 90 100
    RGPLKKSNAP LVNVTLYYEA LCGGCRAFLI RELFPTWLLV MEILNVTLVP
    110 120 130 140 150
    YGNAQEQNVS GRWEFKCQHG EEECKFNKVE ACVLDELDME LAFLTIVCME
    160 170 180 190 200
    EFEDMERSLP LCLQLYAPGL SPDTIMECAM GDRGMQLMHA NAQRTDALQP
    210 220 230 240 250
    PHEYVPWVTV NGKPLEDQTQ LLTLVCQLYQ GKKPDVCPSS TSSLRSVCFK
    Length:250
    Mass (Da):27,964
    Last modified:April 5, 2011 - v3
    Checksum:i54B4950E3788CD5A
    GO

    Sequence cautioni

    The sequence AAA36105.1 differs from that shown.Chimeric cDNA. N-terminal sequence identical to a region of chromosome 11.Curated
    The sequence AAA36105.1 differs from that shown. Reason: Frameshift at positions 146 and 174. Curated
    The sequence AAA36105.1 differs from that shown. Reason: Erroneous termination at position 251. Translated as stop.Curated
    The sequence AAF04618.1 differs from that shown.Chimeric cDNA. N-terminal sequence identical to a region of chromosome 11.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti76 – 761R → Q in AAH31020 (PubMed:15489334).Curated
    Sequence conflicti98 – 981L → S in AAA36105 (PubMed:3136170).Curated
    Sequence conflicti119 – 1191H → L in AAA36105 (PubMed:3136170).Curated
    Sequence conflicti148 – 1481C → WHG in AAA36105 (PubMed:3136170).Curated
    Sequence conflicti223 – 2231T → A in BAC98466 (Ref. 3) Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J03909 mRNA. Translation: AAA36105.1. Sequence problems.
    AF097362 mRNA. Translation: AAF04618.1. Sequence problems.
    AB049659 mRNA. Translation: BAC98466.1.
    AC007192 Genomic DNA. No translation available.
    AC093080 Genomic DNA. No translation available.
    AC068499 Genomic DNA. No translation available.
    CH471106 Genomic DNA. Translation: EAW84662.1.
    BC021136 mRNA. Translation: AAH21136.1.
    BC031020 mRNA. Translation: AAH31020.1.
    CCDSiCCDS46015.1.
    PIRiA43708.
    RefSeqiNP_006323.2. NM_006332.4.
    UniGeneiHs.14623.

    Genome annotation databases

    EnsembliENST00000407280; ENSP00000384886; ENSG00000216490.
    GeneIDi10437.
    KEGGihsa:10437.
    UCSCiuc002nic.1. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J03909 mRNA. Translation: AAA36105.1. Sequence problems.
    AF097362 mRNA. Translation: AAF04618.1. Sequence problems.
    AB049659 mRNA. Translation: BAC98466.1.
    AC007192 Genomic DNA. No translation available.
    AC093080 Genomic DNA. No translation available.
    AC068499 Genomic DNA. No translation available.
    CH471106 Genomic DNA. Translation: EAW84662.1.
    BC021136 mRNA. Translation: AAH21136.1.
    BC031020 mRNA. Translation: AAH31020.1.
    CCDSiCCDS46015.1.
    PIRiA43708.
    RefSeqiNP_006323.2. NM_006332.4.
    UniGeneiHs.14623.

    3D structure databases

    ProteinModelPortaliP13284.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi115704. 26 interactions.
    IntActiP13284. 4 interactions.
    STRINGi9606.ENSP00000384886.

    PTM databases

    PhosphoSiteiP13284.

    Polymorphism and mutation databases

    BioMutaiIFI30.
    DMDMi327478582.

    Proteomic databases

    MaxQBiP13284.
    PaxDbiP13284.
    PRIDEiP13284.

    Protocols and materials databases

    DNASUi10437.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000407280; ENSP00000384886; ENSG00000216490.
    GeneIDi10437.
    KEGGihsa:10437.
    UCSCiuc002nic.1. human.

    Organism-specific databases

    CTDi10437.
    GeneCardsiGC19P018401.
    HGNCiHGNC:5398. IFI30.
    HPAiHPA026650.
    MIMi604664. gene.
    neXtProtiNX_P13284.
    PharmGKBiPA29644.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiNOG315223.
    GeneTreeiENSGT00390000010450.
    HOGENOMiHOG000238423.
    HOVERGENiHBG005837.
    InParanoidiP13284.
    KOiK08059.
    OMAiMHANAQR.
    PhylomeDBiP13284.
    TreeFamiTF315141.

    Enzyme and pathway databases

    ReactomeiREACT_121399. MHC class II antigen presentation.
    REACT_25078. Interferon gamma signaling.

    Miscellaneous databases

    GeneWikiiIFI30.
    GenomeRNAii10437.
    NextBioi39558.
    PROiP13284.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP13284.
    CleanExiHS_IFI30.
    ExpressionAtlasiP13284. baseline.
    GenevisibleiP13284. HS.

    Family and domain databases

    InterProiIPR004911. Interferon-induced_GILT.
    [Graphical view]
    PANTHERiPTHR13234. PTHR13234. 1 hit.
    PfamiPF03227. GILT. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Molecular and biochemical characterization of a novel gamma-interferon-inducible protein."
      Luster A.D., Weinshank R.L., Feinman R., Ravetch J.V.
      J. Biol. Chem. 263:12036-12043(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, SUBCELLULAR LOCATION, SUBUNIT.
    2. "Enzymatic reduction of disulfide bonds in lysosomes: characterization of a gamma-interferon-inducible lysosomal thiol reductase (GILT)."
      Arunachalam B., Phan U.T., Geuze H.J., Cresswell P.
      Proc. Natl. Acad. Sci. U.S.A. 97:745-750(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION BY MASS SPECTROMETRY, PROTEIN SEQUENCE OF N-TERMINUS, GLYCOSYLATION, MUTAGENESIS OF CYS-72 AND CYS-75.
    3. "A novel Asn-bond specific endoproteolytic enzyme from Human."
      Arahira M., Fukazawa C.
      Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Placenta.
    5. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Skin.
    8. "Gamma-interferon-inducible lysosomal thiol reductase (GILT). Maturation, activity, and mechanism of action."
      Phan U.T., Arunachalam B., Cresswell P.
      J. Biol. Chem. 275:25907-25914(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-72 AND CYS-75, GLYCOSYLATION.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiGILT_HUMAN
    AccessioniPrimary (citable) accession number: P13284
    Secondary accession number(s): Q76MF9
    , Q8NEI4, Q8WU77, Q9UL08
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: April 5, 2011
    Last modified: July 22, 2015
    This is version 117 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Both precursor form and mature form have thiol reductase activity.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.