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Q499T2 (GILT_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gamma-interferon-inducible lysosomal thiol reductase

EC=1.8.-.-
Alternative name(s):
Interferon gamma inducible protein 30
Gene names
Name:Ifi30
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length248 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Subunit structure

Dimer; disulfide-linked By similarity.

Subcellular location

Secreted By similarity. Lysosome By similarity.

Post-translational modification

N-glycosylated. Sugar chains contain mannose-6-phosphate 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.

Miscellaneous

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

Sequence similarities

Belongs to the GILT family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Propeptide25 – 5430Removed in mature form By similarity
PRO_0000406227
Chain55 – 230176Gamma-interferon-inducible lysosomal thiol reductase
PRO_0000406228
Propeptide231 – 24818Removed in mature form By similarity
PRO_0000406229

Amino acid modifications

Glycosylation601N-linked (GlcNAc...) Potential
Glycosylation921N-linked (GlcNAc...) Potential
Glycosylation1051N-linked (GlcNAc...) Potential
Disulfide bond69 ↔ 72Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q499T2 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 12A82B9AF6E2E3B4

FASTA24827,644
        10         20         30         40         50         60 
MSCSPLVPFL SLLLLLFLPE VPRAATASLP QGSSEGAATC KAHDLCLFGP RRLLSAPPVN 

        70         80         90        100        110        120 
VSLYYESLCG ACRYFLVRNL FPTWLMVMEI MNITLVPYGN AQERNVSGTW EFTCQHGELE 

       130        140        150        160        170        180 
CKLNKVEACL LDKLEKEAAF LTIVCMEEME DMEKKLGPCL QLYVPEVSPE SIMECATGKR 

       190        200        210        220        230        240 
GTELMHENAQ LTDALQPPHE YVPWVLVNEK PLTDPSQLLS SVCELYQGTE KPDICSSMAD 


APREVCYK 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH474031 Genomic DNA. Translation: EDL90735.1.
BC099774 mRNA. Translation: AAH99774.1.
BC088256 mRNA. Translation: AAH88256.1.
RefSeqNP_001025197.1. NM_001030026.1.
UniGeneRn.3370.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000026225.

PTM databases

PhosphoSiteQ499T2.

Proteomic databases

PaxDbQ499T2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000026225; ENSRNOP00000026225; ENSRNOG00000019387.
GeneID290644.
KEGGrno:290644.

Organism-specific databases

CTD10437.
RGD1310758. Ifi30.

Phylogenomic databases

eggNOGNOG315223.
GeneTreeENSGT00390000010450.
HOGENOMHOG000238423.
HOVERGENHBG005837.
InParanoidQ5I0J7.
KOK08059.
OMAVNVSLYY.
OrthoDBEOG71P2CG.
PhylomeDBQ499T2.
TreeFamTF315141.

Gene expression databases

GenevestigatorQ499T2.

Family and domain databases

InterProIPR004911. Interferon-induced_GILT.
[Graphical view]
PANTHERPTHR13234. PTHR13234. 1 hit.
PfamPF03227. GILT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio631392.
PROQ499T2.

Entry information

Entry nameGILT_RAT
AccessionPrimary (citable) accession number: Q499T2
Secondary accession number(s): Q5I0J7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: September 13, 2005
Last modified: April 16, 2014
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families