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P13284

- GILT_HUMAN

UniProt

P13284 - GILT_HUMAN

Protein

Gamma-interferon-inducible lysosomal thiol reductase

Gene

IFI30

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 3 (05 Apr 2011)
      Previous versions | rss
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    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

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

    GO - Biological processi

    1. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: UniProtKB
    2. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
    3. cytokine-mediated signaling pathway Source: Reactome
    4. interferon-gamma-mediated signaling pathway Source: Reactome
    5. negative regulation of fibroblast proliferation Source: Ensembl
    6. protein stabilization Source: Ensembl

    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: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:5398. IFI30.

    Subcellular locationi

    GO - Cellular componenti

    1. cell junction Source: HPA
    2. cytoplasm Source: HPA
    3. extracellular region Source: ProtInc
    4. intracellular membrane-bounded organelle Source: HPA
    5. lysosomal lumen Source: Reactome
    6. lysosome Source: UniProtKB
    7. plasma membrane Source: HPA

    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.

    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.
    GenevestigatoriP13284.

    Organism-specific databases

    HPAiHPA026650.

    Interactioni

    Subunit structurei

    Dimer; disulfide-linked.2 Publications

    Protein-protein interaction databases

    IntActiP13284. 1 interaction.
    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.
    HOGENOMiHOG000238423.
    HOVERGENiHBG005837.
    InParanoidiP13284.
    KOiK08059.
    OMAiHGEQECK.
    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

    MTLSPLLLFL PPLLLLLDVP TAAVQASPLQ ALDFFGNGPP VNYKTGNLYL    50
    RGPLKKSNAP LVNVTLYYEA LCGGCRAFLI RELFPTWLLV MEILNVTLVP 100
    YGNAQEQNVS GRWEFKCQHG EEECKFNKVE ACVLDELDME LAFLTIVCME 150
    EFEDMERSLP LCLQLYAPGL SPDTIMECAM GDRGMQLMHA NAQRTDALQP 200
    PHEYVPWVTV NGKPLEDQTQ LLTLVCQLYQ GKKPDVCPSS TSSLRSVCFK 250
    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. Reason: Chimeric cDNA. N-terminal sequence identical to a region of chromosome 11.
    The sequence AAF04618.1 differs from that shown. Reason: Chimeric cDNA. N-terminal sequence identical to a region of chromosome 11.
    The sequence AAA36105.1 differs from that shown. Reason: Frameshift at positions 146 and 174.
    The sequence AAA36105.1 differs from that shown. Reason: Erroneous termination at position 251. Translated as stop.

    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. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi327478582.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS46015.1.
    PIRi A43708.
    RefSeqi NP_006323.2. NM_006332.4.
    UniGenei Hs.14623.

    3D structure databases

    ProteinModelPortali P13284.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P13284. 1 interaction.
    STRINGi 9606.ENSP00000384886.

    PTM databases

    PhosphoSitei P13284.

    Polymorphism databases

    DMDMi 327478582.

    Proteomic databases

    MaxQBi P13284.
    PaxDbi P13284.
    PRIDEi P13284.

    Protocols and materials databases

    DNASUi 10437.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000407280 ; ENSP00000384886 ; ENSG00000216490 .
    GeneIDi 10437.
    KEGGi hsa:10437.
    UCSCi uc002nic.1. human.

    Organism-specific databases

    CTDi 10437.
    GeneCardsi GC19P018284.
    HGNCi HGNC:5398. IFI30.
    HPAi HPA026650.
    MIMi 604664. gene.
    neXtProti NX_P13284.
    PharmGKBi PA29644.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG315223.
    HOGENOMi HOG000238423.
    HOVERGENi HBG005837.
    InParanoidi P13284.
    KOi K08059.
    OMAi HGEQECK.
    PhylomeDBi P13284.
    TreeFami TF315141.

    Enzyme and pathway databases

    Reactomei REACT_121399. MHC class II antigen presentation.
    REACT_25078. Interferon gamma signaling.

    Miscellaneous databases

    GeneWikii IFI30.
    GenomeRNAii 10437.
    NextBioi 39558.
    PROi P13284.
    SOURCEi Search...

    Gene expression databases

    Bgeei P13284.
    CleanExi HS_IFI30.
    Genevestigatori P13284.

    Family and domain databases

    InterProi IPR004911. Interferon-induced_GILT.
    [Graphical view ]
    PANTHERi PTHR13234. PTHR13234. 1 hit.
    Pfami PF03227. GILT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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].

    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: October 1, 2014
    This is version 108 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