IFI30
entrez
10437
canonical
uniprot
P13284
canonical
ensembl
ENSG00000216490
resolver
ensp
ENSP00000384886
resolver
enst
ENST00000407280
resolver
genesymbol
IFI30
resolver
genesymbol_syn
GILT
resolver
genesymbol_syn
IP30
resolver
hgnc
HGNC:5398
resolver
uniprot
Q76MF9
resolver
uniprot
Q8NEI4
resolver
uniprot
Q8WU77
resolver
uniprot
Q9UL08
resolver
uniprot_entry
GILT_HUMAN
resolver
uniprot_sec
Q76MF9
resolver
uniprot_sec
Q8NEI4
resolver
uniprot_sec
Q8WU77
resolver
uniprot_sec
Q9UL08
resolver
amino_acid_sequence
MTLSPLLLFLPPLLLLLDVPTAAVQASPLQALDFFGNGPPVNYKTGNLYLRGPLKKSNAPLVNVTLYYEALCGGCRAFLIRELFPTWLLVMEILNVTLVPYGNAQEQNVSGRWEFKCQHGEEECKFNKVEACVLDELDMELAFLTIVCMEEFEDMERSLPLCLQLYAPGLSPDTIMECAMGDRGMQLMHANAQRTDALQPPHEYVPWVTVNGKPLEDQTQLLTLVCQLYQGKKPDVCPSSTSSLRSVCFK
uniprot
proteins
ec_number
1.8.4.-
uniprot
proteins
function
FUNCTION: 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). {ECO:0000269|PubMed:10639150, ECO:0000269|PubMed:10852914, ECO:0000305|PubMed:10852914}.
uniprot
proteins
mass_dalton
27964
uniprot
proteins
mutagenesis
MUTAGEN 72; /note="C->S: Abolishes reducing activity, does not affect dimerization. Abolishes reducing activity; when associated with S-75."; /evidence="ECO:0000269|PubMed:10639150, ECO:0000269|PubMed:10852914"; MUTAGEN 75; /note="C->S: Abolishes reducing activity, does not affect dimerization. Abolishes reducing activity; when associated with S-72."; /evidence="ECO:0000269|PubMed:10639150, ECO:0000269|PubMed:10852914
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. Sugar chains contain mannose-6-phosphate. {ECO:0000269|PubMed:10639150, ECO:0000269|PubMed:10852914}.; 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. {ECO:0000269|PubMed:10639150}.
uniprot
proteins
protein_family
GILT family
uniprot
proteins
pubmed
10639150
uniprot
proteins
pubmed
10852914
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
3136170
uniprot
proteins
sequence_length
250
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10639150, ECO:0000269|PubMed:10852914, ECO:0000269|PubMed:3136170}. Lysosome {ECO:0000269|PubMed:10639150, ECO:0000269|PubMed:3136170}. Note=A small amount of the precursor can be secreted outside the cell as a dimer. {ECO:0000269|PubMed:10639150}.
uniprot
proteins