ID   GILT_BOVIN              Reviewed;         244 AA.
AC   A6QPN6;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Gamma-interferon-inducible lysosomal thiol reductase;
DE            EC=1.8.-.- {ECO:0000250|UniProtKB:P13284};
DE   AltName: Full=IFI30 protein;
DE   Flags: Precursor;
GN   Name=IFI30;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal spinal cord;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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; BC149406; AAI49407.1; -; mRNA.
DR   RefSeq; NP_001094721.1; NM_001101251.2.
DR   AlphaFoldDB; A6QPN6; -.
DR   SMR; A6QPN6; -.
DR   STRING; 9913.ENSBTAP00000045061; -.
DR   PaxDb; A6QPN6; -.
DR   PRIDE; A6QPN6; -.
DR   Ensembl; ENSBTAT00000047907; ENSBTAP00000045061; ENSBTAG00000018349.
DR   GeneID; 615930; -.
DR   KEGG; bta:615930; -.
DR   CTD; 10437; -.
DR   VEuPathDB; HostDB:ENSBTAG00000018349; -.
DR   VGNC; VGNC:30043; IFI30.
DR   eggNOG; KOG3160; Eukaryota.
DR   GeneTree; ENSGT00390000010450; -.
DR   InParanoid; A6QPN6; -.
DR   OrthoDB; 803513at2759; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000018349; Expressed in uterine cervix and 105 other tissues.
DR   ExpressionAtlas; A6QPN6; baseline and differential.
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   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..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..51
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P13284"
FT                   /id="PRO_0000406218"
FT   CHAIN           52..244
FT                   /note="Gamma-interferon-inducible lysosomal thiol
FT                   reductase"
FT                   /id="PRO_0000406219"
FT   PROPEP          227..244
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P13284"
FT                   /id="PRO_0000406220"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        89
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        66..69
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:P13284"
SQ   SEQUENCE   244 AA;  27490 MW;  7E2CF7AC19E1FD07 CRC64;
     MASSPLLFVL LLLLPLEVPA ATRWSLLEAL PEGAAPCQVG ELCLQASPQK PDVPLVNVSL
     YYEALCPGCR EFLIRELFPT WLMVLEILNV TLVPYGNAQE RNVSGKWEFT CQHGERECLL
     NKVEACLLDQ LEQKIAFLTI VCLEEMDDME QNLKPCLQIY APKVSADSIM ECATGNRGMQ
     LLHINAQLTD ALRPPHKYVP WVVVNGEHMK DAEHLLHLVC RLYQGQKPDV CQLTAELSKE
     VHFK