Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Gamma-interferon-inducible lysosomal thiol reductase

Gene

Ifi30

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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. Facilitates also MHC class I-restricted recognition of exogenous antigens containing disulfide bonds by CD8+ T-cells or crosspresentation (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Immunity

Enzyme and pathway databases

ReactomeiREACT_296088. MHC class II antigen presentation.

Names & Taxonomyi

Protein namesi
Recommended name:
Gamma-interferon-inducible lysosomal thiol reductase (EC:1.8.-.-)
Alternative name(s):
Interferon gamma inducible protein 30
Gene namesi
Name:Ifi30
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 16

Organism-specific databases

RGDi1310758. Ifi30.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Propeptidei25 – 5430Removed in mature formBy similarityPRO_0000406227Add
BLAST
Chaini55 – 230176Gamma-interferon-inducible lysosomal thiol reductasePRO_0000406228Add
BLAST
Propeptidei231 – 24818Removed in mature formBy similarityPRO_0000406229Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi60 – 601N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi69 ↔ 72Redox-activeBy similarity
Glycosylationi92 – 921N-linked (GlcNAc...)Sequence Analysis
Glycosylationi105 – 1051N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated. Sugar chains contain mannose-6-phosphate (By similarity).By similarity
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 (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ499T2.

PTM databases

PhosphoSiteiQ499T2.

Expressioni

Gene expression databases

GenevisibleiQ499T2. RN.

Interactioni

Subunit structurei

Dimer; disulfide-linked.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000026225.

Family & Domainsi

Sequence similaritiesi

Belongs to the GILT family.Curated

Keywords - Domaini

Redox-active center, Signal

Phylogenomic databases

eggNOGiNOG315223.
GeneTreeiENSGT00390000010450.
HOGENOMiHOG000238423.
HOVERGENiHBG005837.
InParanoidiQ499T2.
KOiK08059.
OMAiGTELMHE.
OrthoDBiEOG71P2CG.
PhylomeDBiQ499T2.
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.

Q499T2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSCSPLVPFL SLLLLLFLPE VPRAATASLP QGSSEGAATC KAHDLCLFGP
60 70 80 90 100
RRLLSAPPVN VSLYYESLCG ACRYFLVRNL FPTWLMVMEI MNITLVPYGN
110 120 130 140 150
AQERNVSGTW EFTCQHGELE CKLNKVEACL LDKLEKEAAF LTIVCMEEME
160 170 180 190 200
DMEKKLGPCL QLYVPEVSPE SIMECATGKR GTELMHENAQ LTDALQPPHE
210 220 230 240
YVPWVLVNEK PLTDPSQLLS SVCELYQGTE KPDICSSMAD APREVCYK
Length:248
Mass (Da):27,644
Last modified:September 13, 2005 - v1
Checksum:i12A82B9AF6E2E3B4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH474031 Genomic DNA. Translation: EDL90735.1.
BC099774 mRNA. Translation: AAH99774.1.
BC088256 mRNA. Translation: AAH88256.1.
RefSeqiNP_001025197.1. NM_001030026.1.
UniGeneiRn.3370.

Genome annotation databases

EnsembliENSRNOT00000026225; ENSRNOP00000026225; ENSRNOG00000019387.
GeneIDi290644.
KEGGirno:290644.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH474031 Genomic DNA. Translation: EDL90735.1.
BC099774 mRNA. Translation: AAH99774.1.
BC088256 mRNA. Translation: AAH88256.1.
RefSeqiNP_001025197.1. NM_001030026.1.
UniGeneiRn.3370.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000026225.

PTM databases

PhosphoSiteiQ499T2.

Proteomic databases

PaxDbiQ499T2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000026225; ENSRNOP00000026225; ENSRNOG00000019387.
GeneIDi290644.
KEGGirno:290644.

Organism-specific databases

CTDi10437.
RGDi1310758. Ifi30.

Phylogenomic databases

eggNOGiNOG315223.
GeneTreeiENSGT00390000010450.
HOGENOMiHOG000238423.
HOVERGENiHBG005837.
InParanoidiQ499T2.
KOiK08059.
OMAiGTELMHE.
OrthoDBiEOG71P2CG.
PhylomeDBiQ499T2.
TreeFamiTF315141.

Enzyme and pathway databases

ReactomeiREACT_296088. MHC class II antigen presentation.

Miscellaneous databases

NextBioi631392.
PROiQ499T2.

Gene expression databases

GenevisibleiQ499T2. RN.

Family and domain databases

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

Publicationsi

  1. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "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: Prostate.

Entry informationi

Entry nameiGILT_RAT
AccessioniPrimary (citable) accession number: Q499T2
Secondary accession number(s): Q5I0J7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: September 13, 2005
Last modified: June 24, 2015
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Both precursor form and mature form have thiol reductase activity.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.