P13284 (GILT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	250 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Immunity
Cellular component	Lysosome Secreted
Domain	Redox-active center Signal
Molecular function	Oxidoreductase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	antigen processing and presentation of exogenous peptide antigen via MHC class I Inferred from sequence or structural similarity. Source: UniProtKB interferon-gamma-mediated signaling pathway Traceable author statement. Source: Reactome
Cellular component	cell junction Inferred from direct assay. Source: HPA extracellular region Traceable author statement. Source: ProtInc lysosomal lumen Traceable author statement. Source: Reactome plasma membrane Inferred from direct assay. Source: HPA
Molecular function	oxidoreductase activity, acting on a sulfur group of donors Inferred from mutant phenotype Ref.2. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 26	26	Potential
	Propeptide	27 – 57	31	Removed in mature form		PRO_0000021328
	Chain	58 – 232	175	Gamma-interferon-inducible lysosomal thiol reductase		PRO_0000021329
	Propeptide	233 – 250	18	Removed in mature form		PRO_0000021330
Amino acid modifications
	Modified residue	45	1	Phosphothreonine Ref.9
	Glycosylation	63	1	N-linked (GlcNAc...) Potential
	Glycosylation	95	1	N-linked (GlcNAc...) Potential
	Glycosylation	108	1	N-linked (GlcNAc...) Potential
	Disulfide bond	72 ↔ 75		Redox-active
Experimental info
	Mutagenesis	72	1	C → S: Abolishes reducing activity, does not affect dimerization. Abolishes reducing activity; when associated with S-75. Ref.2 Ref.8
	Mutagenesis	75	1	C → S: Abolishes reducing activity, does not affect dimerization. Abolishes reducing activity; when associated with S-72. Ref.2 Ref.8
	Sequence conflict	76	1	R → Q in AAH31020. Ref.7
	Sequence conflict	98	1	L → S in AAA36105. Ref.1
	Sequence conflict	119	1	H → L in AAA36105. Ref.1
	Sequence conflict	148	1	C → WHG in AAA36105. Ref.1
	Sequence conflict	223	1	T → A in BAC98466. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P13284 [UniParc]. Last modified April 5, 2011. Version 3. Checksum: 54B4950E3788CD5A	FASTA	250	27,964
	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

References

	« Hide 'large scale' referencesShow '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: 3136170] [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: 10639150] [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: 14702039] [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: 15057824] [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. , 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: 15489334] [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: 10852914] [Abstract] Cited for: SUBUNIT, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-72 AND CYS-75, GLYCOSYLATION.
[9]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-45, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
+	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.
IPI	IPI00007853.
PIR	A43708.
RefSeq	NP_006323.2. NM_006332.3.
UniGene	Hs.14623.
3D structure databases
ProteinModelPortal	P13284.
ModBase	Search...
Protein-protein interaction databases
IntAct	P13284. 1 interaction.
STRING	P13284.
PTM databases
PhosphoSite	P13284.
Polymorphism databases
DMDM	12643406.
Proteomic databases
PRIDE	P13284.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000407280; ENSP00000384886; ENSG00000216490.
GeneID	10437.
KEGG	hsa:10437.
Organism-specific databases
CTD	10437.
GeneCards	GC19P018284.
HGNC	HGNC:5398. IFI30.
HPA	HPA026650.
MIM	604664. gene.
neXtProt	NX_P13284.
PharmGKB	PA29644.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG13287.
HOGENOM	HBG594001.
HOVERGEN	HBG005837.
InParanoid	P13284.
OMA	QPPHEYV.
OrthoDB	EOG4HHP3H.
PhylomeDB	P13284.
Enzyme and pathway databases
Reactome	REACT_6900. Immune System.
Gene expression databases
ArrayExpress	P13284.
Bgee	P13284.
CleanEx	HS_IFI30.
Genevestigator	P13284.
Family and domain databases
InterPro	IPR004911. Interferon-induced_GILT. [Graphical view]
KO	K08059.
PANTHER	PTHR13234. GILT. 1 hit.
Pfam	PF03227. GILT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

GILT_HUMAN

Accession

Primary (citable) accession number: P13284
Secondary accession number(s): Q76MF9 , Q8NEI4, Q8WU77, Q9UL08

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	April 5, 2011
Last modified:	January 25, 2012
This is version 85 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.