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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

  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
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

  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
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.

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 and differential.
GenevestigatoriP13284.

Organism-specific databases

HPAiHPA026650.

Interactioni

Subunit structurei

Dimer; disulfide-linked.2 Publications

Protein-protein interaction databases

BioGridi115704. 29 interactions.
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.
GeneTreeiENSGT00390000010450.
HOGENOMiHOG000238423.
HOVERGENiHBG005837.
InParanoidiP13284.
KOiK08059.
OMAiWLMVLEI.
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.

Polymorphism databases

DMDMi327478582.

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. 29 interactions.
IntActiP13284. 1 interaction.
STRINGi9606.ENSP00000384886.

PTM databases

PhosphoSiteiP13284.

Polymorphism databases

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.
OMAiWLMVLEI.
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 and differential.
GenevestigatoriP13284.

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(1987) [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(1999) [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 (SEP-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(2003) [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(2003) [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(2003) [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(1999) [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(2013) [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: April 1, 2015
This is version 113 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.