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P13284 (GILT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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):
Gamma-interferon-inducible protein IP-30
Legumaturain
Gene names
Name:IFI30
Synonyms:GILT, IP30
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length250 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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 By similarity. 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. Ref.1 Ref.8

Subcellular location

Secreted. Lysosome Ref.1 Ref.2.

Induction

Expressed constitutively in antigen-presenting cells and induced by IFN-gamma in other cell types. Ref.1

Post-translational modification

N-glycosylated. Sugar chains contain mannose-6-phosphate. Ref.2 Ref.8

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.

Sequence similarities

Belongs to the GILT family.

Biophysicochemical properties

Kinetic parameters:

Kinetic parameters shown are for mature enzyme.

KM=1200 µM for F(ab')2 fragment when denatured Ref.2

KM=10 µM for F(ab')2 fragment

pH dependence:

Optimum pH is 4-5.

Sequence caution

The sequence AAA36105.1 differs from that shown. Reason: Erroneous termination at position 251. Translated as stop.

The sequence AAA36105.1 differs from that shown. Reason: Frameshift at positions 146 and 174.

The sequence AAA36105.1 differs from that shown. Reason: Chimeric cDNA. N-terminal sequence identical to a region of chromosome 11.

The sequence AAF04618.1 differs from that shown. Reason: Chimeric cDNA. N-terminal sequence identical to a region of chromosome 11.

Ontologies

Keywords
   Biological processImmunity
   Cellular componentLysosome
Secreted
   DomainRedox-active center
Signal
   Molecular functionOxidoreductase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processantigen processing and presentation of exogenous peptide antigen via MHC class I

Inferred from sequence or structural similarity. Source: UniProtKB

antigen processing and presentation of exogenous peptide antigen via MHC class II

Traceable author statement. Source: Reactome

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

interferon-gamma-mediated signaling pathway

Traceable author statement. Source: Reactome

negative regulation of fibroblast proliferation

Inferred from electronic annotation. Source: Ensembl

protein stabilization

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell junction

Inferred from direct assay. Source: HPA

cytoplasm

Inferred from direct assay. Source: HPA

extracellular region

Traceable author statement Ref.1. Source: ProtInc

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

lysosomal lumen

Traceable author statement. Source: Reactome

lysosome

Inferred from direct assay Ref.2. Source: UniProtKB

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionoxidoreductase activity, acting on a sulfur group of donors

Inferred from mutant phenotype Ref.2. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Propeptide27 – 5731Removed in mature form
PRO_0000021328
Chain58 – 232175Gamma-interferon-inducible lysosomal thiol reductase
PRO_0000021329
Propeptide233 – 25018Removed in mature form
PRO_0000021330

Amino acid modifications

Glycosylation631N-linked (GlcNAc...) Potential
Glycosylation951N-linked (GlcNAc...) Potential
Glycosylation1081N-linked (GlcNAc...) Potential
Disulfide bond72 ↔ 75Redox-active

Experimental info

Mutagenesis721C → S: Abolishes reducing activity, does not affect dimerization. Abolishes reducing activity; when associated with S-75. Ref.2 Ref.8
Mutagenesis751C → S: Abolishes reducing activity, does not affect dimerization. Abolishes reducing activity; when associated with S-72. Ref.2 Ref.8
Sequence conflict761R → Q in AAH31020. Ref.7
Sequence conflict981L → S in AAA36105. Ref.1
Sequence conflict1191H → L in AAA36105. Ref.1
Sequence conflict1481C → WHG in AAA36105. Ref.1
Sequence conflict2231T → A in BAC98466. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P13284 [UniParc].

Last modified April 5, 2011. Version 3.
Checksum: 54B4950E3788CD5A

FASTA25027,964
        10         20         30         40         50         60 
MTLSPLLLFL PPLLLLLDVP TAAVQASPLQ ALDFFGNGPP VNYKTGNLYL RGPLKKSNAP 

        70         80         90        100        110        120 
LVNVTLYYEA LCGGCRAFLI RELFPTWLLV MEILNVTLVP YGNAQEQNVS GRWEFKCQHG 

       130        140        150        160        170        180 
EEECKFNKVE ACVLDELDME LAFLTIVCME EFEDMERSLP LCLQLYAPGL SPDTIMECAM 

       190        200        210        220        230        240 
GDRGMQLMHA NAQRTDALQP PHEYVPWVTV NGKPLEDQTQ LLTLVCQLYQ GKKPDVCPSS 

       250 
TSSLRSVCFK 

« Hide

References

« Hide 'large scale' references
[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(1988) [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(2000) [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 (OCT-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. expand/collapse author list , 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(2004) [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. expand/collapse author list , 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(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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(2004) [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(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-72 AND CYS-75, GLYCOSYLATION.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA43708.
RefSeqNP_006323.2. NM_006332.4.
UniGeneHs.14623.

3D structure databases

ProteinModelPortalP13284.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP13284. 1 interaction.
STRING9606.ENSP00000384886.

PTM databases

PhosphoSiteP13284.

Polymorphism databases

DMDM327478582.

Proteomic databases

PaxDbP13284.
PRIDEP13284.

Protocols and materials databases

DNASU10437.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000407280; ENSP00000384886; ENSG00000216490.
GeneID10437.
KEGGhsa:10437.
UCSCuc002nic.1. human.

Organism-specific databases

CTD10437.
GeneCardsGC19P018284.
HGNCHGNC:5398. IFI30.
HPAHPA026650.
MIM604664. gene.
neXtProtNX_P13284.
PharmGKBPA29644.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG315223.
HOGENOMHOG000238423.
HOVERGENHBG005837.
InParanoidP13284.
KOK08059.
OMAVNVSLYY.
PhylomeDBP13284.
TreeFamTF315141.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

BgeeP13284.
CleanExHS_IFI30.
GenevestigatorP13284.

Family and domain databases

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

Other

GeneWikiIFI30.
GenomeRNAi10437.
NextBio39558.
PROP13284.
SOURCESearch...

Entry information

Entry nameGILT_HUMAN
AccessionPrimary (citable) accession number: P13284
Secondary accession number(s): Q76MF9 expand/collapse secondary AC list , Q8NEI4, Q8WU77, Q9UL08
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: April 5, 2011
Last modified: April 16, 2014
This is version 103 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM