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P13284

- GILT_HUMAN

UniProt

P13284 - GILT_HUMAN

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Protein

Gamma-interferon-inducible lysosomal thiol reductase

Gene

IFI30

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

Kineticsi

Kinetic parameters shown are for mature enzyme.

  1. KM=1200 µM for F(ab')2 fragment when denatured1 Publication
  2. KM=10 µM for F(ab')2 fragment1 Publication

pH dependencei

Optimum pH is 4-5.1 Publication

GO - Molecular functioni

  1. oxidoreductase activity, acting on a sulfur group of donors Source: UniProtKB

GO - Biological processi

  1. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: UniProtKB
  2. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
  3. cytokine-mediated signaling pathway Source: Reactome
  4. interferon-gamma-mediated signaling pathway Source: Reactome
  5. negative regulation of fibroblast proliferation Source: Ensembl
  6. protein stabilization Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Immunity

Enzyme and pathway databases

ReactomeiREACT_121399. MHC class II antigen presentation.
REACT_25078. Interferon gamma signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Gamma-interferon-inducible lysosomal thiol reductase (EC:1.8.-.-)
Alternative name(s):
Gamma-interferon-inducible protein IP-30
Legumaturain
Gene namesi
Name:IFI30
Synonyms:GILT, IP30
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:5398. IFI30.

Subcellular locationi

GO - Cellular componenti

  1. cell junction Source: HPA
  2. cytoplasm Source: HPA
  3. extracellular region Source: ProtInc
  4. intracellular membrane-bounded organelle Source: HPA
  5. lysosomal lumen Source: Reactome
  6. lysosome Source: UniProtKB
  7. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi72 – 721C → S: Abolishes reducing activity, does not affect dimerization. Abolishes reducing activity; when associated with S-75. 2 Publications
Mutagenesisi75 – 751C → S: Abolishes reducing activity, does not affect dimerization. Abolishes reducing activity; when associated with S-72. 2 Publications

Organism-specific databases

PharmGKBiPA29644.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence AnalysisAdd
BLAST
Propeptidei27 – 5731Removed in mature form1 PublicationPRO_0000021328Add
BLAST
Chaini58 – 232175Gamma-interferon-inducible lysosomal thiol reductasePRO_0000021329Add
BLAST
Propeptidei233 – 25018Removed in mature form1 PublicationPRO_0000021330Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi63 – 631N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi72 ↔ 75Redox-active
Glycosylationi95 – 951N-linked (GlcNAc...)Sequence Analysis
Glycosylationi108 – 1081N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated. Sugar chains contain mannose-6-phosphate.2 Publications
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.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP13284.
PaxDbiP13284.
PRIDEiP13284.

PTM databases

PhosphoSiteiP13284.

Expressioni

Inductioni

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

Gene expression databases

BgeeiP13284.
CleanExiHS_IFI30.
ExpressionAtlasiP13284. baseline.
GenevestigatoriP13284.

Organism-specific databases

HPAiHPA026650.

Interactioni

Subunit structurei

Dimer; disulfide-linked.2 Publications

Protein-protein interaction databases

BioGridi115704. 27 interactions.
IntActiP13284. 1 interaction.
STRINGi9606.ENSP00000384886.

Structurei

3D structure databases

ProteinModelPortaliP13284.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GILT family.Curated

Keywords - Domaini

Redox-active center, Signal

Phylogenomic databases

eggNOGiNOG315223.
GeneTreeiENSGT00390000010450.
HOGENOMiHOG000238423.
HOVERGENiHBG005837.
InParanoidiP13284.
KOiK08059.
OMAiHGEQECK.
PhylomeDBiP13284.
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.

P13284-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTLSPLLLFL PPLLLLLDVP TAAVQASPLQ ALDFFGNGPP VNYKTGNLYL
60 70 80 90 100
RGPLKKSNAP LVNVTLYYEA LCGGCRAFLI RELFPTWLLV MEILNVTLVP
110 120 130 140 150
YGNAQEQNVS GRWEFKCQHG EEECKFNKVE ACVLDELDME LAFLTIVCME
160 170 180 190 200
EFEDMERSLP LCLQLYAPGL SPDTIMECAM GDRGMQLMHA NAQRTDALQP
210 220 230 240 250
PHEYVPWVTV NGKPLEDQTQ LLTLVCQLYQ GKKPDVCPSS TSSLRSVCFK
Length:250
Mass (Da):27,964
Last modified:April 5, 2011 - v3
Checksum:i54B4950E3788CD5A
GO

Sequence cautioni

The sequence AAA36105.1 differs from that shown. Reason: Chimeric cDNA. N-terminal sequence identical to a region of chromosome 11.Curated
The sequence AAA36105.1 differs from that shown. Reason: Frameshift at positions 146 and 174. Curated
The sequence AAA36105.1 differs from that shown. Reason: Erroneous termination at position 251. Translated as stop.Curated
The sequence AAF04618.1 differs from that shown. Reason: Chimeric cDNA. N-terminal sequence identical to a region of chromosome 11.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti76 – 761R → Q in AAH31020. (PubMed:15489334)Curated
Sequence conflicti98 – 981L → S in AAA36105. (PubMed:3136170)Curated
Sequence conflicti119 – 1191H → L in AAA36105. (PubMed:3136170)Curated
Sequence conflicti148 – 1481C → WHG in AAA36105. (PubMed:3136170)Curated
Sequence conflicti223 – 2231T → A in BAC98466. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS46015.1.
PIRiA43708.
RefSeqiNP_006323.2. NM_006332.4.
UniGeneiHs.14623.

Genome annotation databases

EnsembliENST00000407280; ENSP00000384886; ENSG00000216490.
GeneIDi10437.
KEGGihsa:10437.
UCSCiuc002nic.1. human.

Polymorphism databases

DMDMi327478582.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS46015.1.
PIRi A43708.
RefSeqi NP_006323.2. NM_006332.4.
UniGenei Hs.14623.

3D structure databases

ProteinModelPortali P13284.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115704. 27 interactions.
IntActi P13284. 1 interaction.
STRINGi 9606.ENSP00000384886.

PTM databases

PhosphoSitei P13284.

Polymorphism databases

DMDMi 327478582.

Proteomic databases

MaxQBi P13284.
PaxDbi P13284.
PRIDEi P13284.

Protocols and materials databases

DNASUi 10437.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000407280 ; ENSP00000384886 ; ENSG00000216490 .
GeneIDi 10437.
KEGGi hsa:10437.
UCSCi uc002nic.1. human.

Organism-specific databases

CTDi 10437.
GeneCardsi GC19P018401.
HGNCi HGNC:5398. IFI30.
HPAi HPA026650.
MIMi 604664. gene.
neXtProti NX_P13284.
PharmGKBi PA29644.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG315223.
GeneTreei ENSGT00390000010450.
HOGENOMi HOG000238423.
HOVERGENi HBG005837.
InParanoidi P13284.
KOi K08059.
OMAi HGEQECK.
PhylomeDBi P13284.
TreeFami TF315141.

Enzyme and pathway databases

Reactomei REACT_121399. MHC class II antigen presentation.
REACT_25078. Interferon gamma signaling.

Miscellaneous databases

GeneWikii IFI30.
GenomeRNAii 10437.
NextBioi 39558.
PROi P13284.
SOURCEi Search...

Gene expression databases

Bgeei P13284.
CleanExi HS_IFI30.
ExpressionAtlasi P13284. baseline.
Genevestigatori P13284.

Family and domain databases

InterProi IPR004911. Interferon-induced_GILT.
[Graphical view ]
PANTHERi PTHR13234. PTHR13234. 1 hit.
Pfami PF03227. GILT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGILT_HUMAN
AccessioniPrimary (citable) accession number: P13284
Secondary accession number(s): Q76MF9
, Q8NEI4, Q8WU77, Q9UL08
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: April 5, 2011
Last modified: October 29, 2014
This is version 109 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

Both precursor form and mature form have thiol reductase activity.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3