GILT_RAT
ID GILT_RAT Reviewed; 248 AA.
AC Q499T2; Q5I0J7;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Gamma-interferon-inducible lysosomal thiol reductase;
DE EC=1.8.-.- {ECO:0000250|UniProtKB:P13284};
DE AltName: Full=Interferon gamma inducible protein 30;
DE Flags: Precursor;
GN Name=Ifi30;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Lysosomal thiol reductase that can reduce protein disulfide
CC bonds. May facilitate the complete unfolding of proteins destined for
CC lysosomal degradation. Plays an important role in antigen processing.
CC Facilitates the generation of MHC class II-restricted epitodes from
CC disulfide bond-containing antigen by the endocytic reduction of
CC disulfide bonds. Facilitates also MHC class I-restricted recognition of
CC exogenous antigens containing disulfide bonds by CD8+ T-cells or
CC crosspresentation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Dimer; disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Lysosome {ECO:0000250}.
CC -!- PTM: N-glycosylated. Sugar chains contain mannose-6-phosphate (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Synthesized as a 35 kDa precursor which is then processed into the
CC mature 30 kDa form via cleavage of N-terminal and C-terminal
CC propeptides. Processing of the precursor is mediated by multiple
CC lysosomal proteases (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: Both precursor form and mature form have thiol reductase
CC activity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GILT family. {ECO:0000305}.
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DR EMBL; CH474031; EDL90735.1; -; Genomic_DNA.
DR EMBL; BC099774; AAH99774.1; -; mRNA.
DR EMBL; BC088256; AAH88256.1; -; mRNA.
DR RefSeq; NP_001025197.1; NM_001030026.1.
DR AlphaFoldDB; Q499T2; -.
DR SMR; Q499T2; -.
DR STRING; 10116.ENSRNOP00000026225; -.
DR GlyGen; Q499T2; 3 sites.
DR PhosphoSitePlus; Q499T2; -.
DR PaxDb; Q499T2; -.
DR Ensembl; ENSRNOT00000026225; ENSRNOP00000026225; ENSRNOG00000019387.
DR GeneID; 290644; -.
DR KEGG; rno:290644; -.
DR CTD; 10437; -.
DR RGD; 1310758; Ifi30.
DR eggNOG; KOG3160; Eukaryota.
DR GeneTree; ENSGT00390000010450; -.
DR HOGENOM; CLU_066886_0_0_1; -.
DR InParanoid; Q499T2; -.
DR OMA; EACVLDQ; -.
DR OrthoDB; 803513at2759; -.
DR PhylomeDB; Q499T2; -.
DR TreeFam; TF315141; -.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR PRO; PR:Q499T2; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Proteomes; UP000234681; Chromosome 16.
DR Bgee; ENSRNOG00000019387; Expressed in spleen and 19 other tissues.
DR Genevisible; Q499T2; RN.
DR GO; GO:0030054; C:cell junction; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016667; F:oxidoreductase activity, acting on a sulfur group of donors; ISS:UniProtKB.
DR GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IEA:InterPro.
DR GO; GO:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; ISS:UniProtKB.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; ISO:RGD.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISO:RGD.
DR GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR InterPro; IPR004911; Interferon-induced_GILT.
DR PANTHER; PTHR13234; PTHR13234; 1.
DR Pfam; PF03227; GILT; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Immunity; Lysosome; Oxidoreductase;
KW Redox-active center; Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..54
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P13284"
FT /id="PRO_0000406227"
FT CHAIN 55..230
FT /note="Gamma-interferon-inducible lysosomal thiol
FT reductase"
FT /id="PRO_0000406228"
FT PROPEP 231..248
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P13284"
FT /id="PRO_0000406229"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 69..72
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:P13284"
SQ SEQUENCE 248 AA; 27644 MW; 12A82B9AF6E2E3B4 CRC64;
MSCSPLVPFL SLLLLLFLPE VPRAATASLP QGSSEGAATC KAHDLCLFGP RRLLSAPPVN
VSLYYESLCG ACRYFLVRNL FPTWLMVMEI MNITLVPYGN AQERNVSGTW EFTCQHGELE
CKLNKVEACL LDKLEKEAAF LTIVCMEEME DMEKKLGPCL QLYVPEVSPE SIMECATGKR
GTELMHENAQ LTDALQPPHE YVPWVLVNEK PLTDPSQLLS SVCELYQGTE KPDICSSMAD
APREVCYK
