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Details on Person UniProt:P13284 IFI30

Class:IdReferenceGeneProduct:55640
_chainChangeLogsignal peptide:1-26 added on Fri February 6 2015;propeptide:27-57 added on Fri February 6 2015;chain:58-232 added on Fri February 6 2015;propeptide:233-250 added on Fri February 6 2015
_displayNameUniProt:P13284 IFI30
_timestamp2026-02-20 22:10:11
chainsignal peptide:1-26
propeptide:27-57
chain:58-232
propeptide:233-250
checksum54B4950E3788CD5A
commentFUNCTION Lysosomal thiol reductase that catalyzes protein disulfide bonds reduction (PubMed:10639150). Plays an important role in antigen processing and presentation, of namely both major histocompatibility complex (MHC) class I- and class II-restricted antigen by reducing the disulfide bonds of endocytosed proteins and facilitating their unfolding and optimal degradation (PubMed:10639150). Shares with thioredoxin a reduction mechanism in which the N-terminal cysteine thiol group in the CXXC active site motif initiates a nucleophilic attack on the substrate disulfide bond,resulting in the formation of a mixed disulfide-linked enzyme-substrate intermediate (Probable). Subsequent intramolecular attack by the second cysteine thiol group enables the release of the reduced substrate and oxidized enzyme (Probable). Lysosomal cysteine is a physiological reducing agent that is capable of reducing IFI30, so that it can catalyzes the next reaction (PubMed:10852914). Dithiothreitol, cysteine, and cysteinyl glycine, but not glutathione, are capable of regenerating active precursor and mature IFI30 in vitro (PubMed:10639150, PubMed:10852914).CATALYTIC ACTIVITY [protein]-disulfide + 2 L-cysteine = [protein]-dithiol + L-cystineCATALYTIC ACTIVITY 2 L-cysteinylglycine + [protein]-disulfide = L-cystine-bis-glycine + [protein]-dithiolBIOPHYSICOCHEMICAL PROPERTIES Kinetic parameters shown are for mature enzyme.SUBUNIT Dimer; disulfide-linked.INTERACTION A small amount of the precursor can be secreted outside the cell as a dimer.TISSUE SPECIFICITY Expressed constitutively in antigen-presenting cells.INDUCTION Induced by IFN-gamma in other cell types.PTM N-glycosylated. Sugar chains contain mannose-6-phosphate.PTM 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.MISCELLANEOUS Both precursor form and mature form have thiol reductase activity.SIMILARITY Belongs to the GILT family.SEQUENCE CAUTION Extended C-terminus.SEQUENCE CAUTION Chimeric cDNA. N-terminal sequence identical to a region of chromosome 11.SEQUENCE CAUTION Chimeric cDNA. N-terminal sequence identical to a region of chromosome 11.
descriptionrecommendedName: fullName evidence="7"Gamma-interferon-inducible lysosomal thiol reductase ecNumber evidence="3 4"1.8.4.- alternativeName: fullName evidence="11"Gamma-interferon-inducible protein IP-30 alternativeName: Legumaturain
geneNameIFI30
GILT
IP30
identifierP13284
isSequenceChangedFALSE
keywordDirect protein sequencing
Disulfide bond
Glycoprotein
Immunity
Lysosome
Oxidoreductase
Proteomics identification
Redox-active center
Reference proteome
Secreted
Signal
modified[InstanceEdit:9836292] Weiser, Joel, 2023-05-25
[InstanceEdit:9852000] Weiser, Joel, 2023-11-03
[InstanceEdit:9926675] Weiser, Joel, 2024-11-03
[InstanceEdit:9948485] Weiser, Joel, 2025-05-21
[InstanceEdit:9983091] Weiser, Joel, 2026-02-20
nameIFI30
referenceDatabase[ReferenceDatabase:2] UniProt
referenceGene[ReferenceDNASequence:8962195] ENSEMBL:ENSG00000216490 IFI30 [Homo sapiens]
secondaryIdentifierGILT_HUMAN
Q76MF9
Q8NEI4
Q8WU77
Q9UL08
sequenceLength250
species[Species:48887] Homo sapiens
(referenceEntity)[EntityWithAccessionedSequence:1031704] IFI30 [lysosomal lumen] [Homo sapiens]
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No pathways have been reviewed or authored by UniProt:P13284 IFI30 (55640)