ID   GILT_PIG                Reviewed;         246 AA.
AC   B3SP85;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Gamma-interferon-inducible-lysosomal thiol reductase;
DE            EC=1.8.-.- {ECO:0000250|UniProtKB:P13284};
DE   Flags: Precursor;
GN   Name=IFI30; Synonyms=GILT;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], INDUCTION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=18722674; DOI=10.1016/j.vetimm.2008.06.009;
RA   Dan W.B., Wang S.L., Liang J.Q., Zhang S.Q.;
RT   "Molecular cloning and expression analysis of porcine gamma-interferon-
RT   inducible lysosomal thiol reductase (GILT).";
RL   Vet. Immunol. Immunopathol. 126:163-167(2008).
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   -!- TISSUE SPECIFICITY: Expressed in many tissues, including spleen, liver,
CC       lung, heart, intestine, blood and kidney.
CC       {ECO:0000269|PubMed:18722674}.
CC   -!- INDUCTION: By LPS in spleen and blood. {ECO:0000269|PubMed:18722674}.
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; EF644197; ABV21385.1; -; mRNA.
DR   EMBL; EU154970; ABX79390.1; -; Genomic_DNA.
DR   RefSeq; NP_001124518.1; NM_001131046.1.
DR   AlphaFoldDB; B3SP85; -.
DR   SMR; B3SP85; -.
DR   STRING; 9823.ENSSSCP00000014781; -.
DR   PaxDb; B3SP85; -.
DR   PeptideAtlas; B3SP85; -.
DR   PRIDE; B3SP85; -.
DR   GeneID; 100174943; -.
DR   KEGG; ssc:100174943; -.
DR   CTD; 10437; -.
DR   eggNOG; KOG3160; Eukaryota.
DR   HOGENOM; CLU_066886_0_0_1; -.
DR   InParanoid; B3SP85; -.
DR   OMA; EACVLDQ; -.
DR   OrthoDB; 803513at2759; -.
DR   TreeFam; TF315141; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Genevisible; B3SP85; SS.
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; IEA:Ensembl.
DR   GO; GO:0048147; P:negative regulation of fibroblast proliferation; IEA:Ensembl.
DR   GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
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..26
FT                   /evidence="ECO:0000255"
FT   PROPEP          27..53
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P13284"
FT                   /id="PRO_0000406224"
FT   CHAIN           54..228
FT                   /note="Gamma-interferon-inducible-lysosomal thiol
FT                   reductase"
FT                   /id="PRO_0000406225"
FT   PROPEP          229..246
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P13284"
FT                   /id="PRO_0000406226"
FT   CARBOHYD        91
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        68..71
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:P13284"
SQ   SEQUENCE   246 AA;  27614 MW;  1011A84364F879A9 CRC64;
     MASSPLLPFL PLLLLLLLEV PAAAPASPLQ SLLQGAAPCK AGEPCLQRPV GKSDPPPVNV
     NLYYESLCNG CRYFLVRELF PTWLMVWEIL NVTLVPYGNA QERNVSGRWE FTCQHGEQEC
     KMNKVEACLL DKLEKNMAFL TIVCIEELDD MEKNLEPCLQ IYAPKVSPDS IMECAMGDRG
     MQLLHINAQL TDALKPPHEY VPWVVVNGKP MTEKDQLLRL VCQLYEGEKP DVCQILASSH
     KEVCFK