ID   GILT_CARAU              Reviewed;         251 AA.
AC   E7E2N8;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   25-MAY-2022, entry version 19.
DE   RecName: Full=Gamma-interferon-inducible lysosomal thiol reductase {ECO:0000303|PubMed:25447639};
DE            EC=1.8.-.- {ECO:0000269|PubMed:25447639};
DE   Flags: Precursor;
GN   Name=ifi30 {ECO:0000250|UniProtKB:Q5XJN2};
GN   Synonyms=GILT {ECO:0000303|PubMed:25447639};
OS   Carassius auratus (Goldfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Carassius.
OX   NCBI_TaxID=7957 {ECO:0000312|EMBL:ADU02196.1};
RN   [1] {ECO:0000312|EMBL:ADU02196.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY LPS.
RX   PubMed=25447639; DOI=10.1016/j.fsi.2014.11.032;
RA   Li J.F., Li J., Wang Z.G., Liu H.Z., Zhao Y.L., Zhang J.X., Zhang S.Q.,
RA   Liu J.P.;
RT   "Identification of interferon-gamma-inducible-lysosomal thiol reductase
RT   (GILT) gene in goldfish (Carassius auratus) and its immune response to LPS
RT   challenge.";
RL   Fish Shellfish Immunol. 42:465-472(2015).
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       {ECO:0000269|PubMed:25447639}.
CC   -!- SUBUNIT: Dimer; disulfide-linked. {ECO:0000250|UniProtKB:P13284}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:25447639}. Lysosome
CC       {ECO:0000269|PubMed:25447639}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in spleen and kidney. Also
CC       detected at lower levels in liver, heart, brain, intestine and gill.
CC       {ECO:0000269|PubMed:25447639}.
CC   -!- INDUCTION: Strongly up-regulated in spleen and kidney in response to
CC       bacterial lipopolysaccharide (LPS). {ECO:0000269|PubMed:25447639}.
CC   -!- SIMILARITY: Belongs to the GILT family. {ECO:0000305}.
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DR   EMBL; HQ610621; ADU02196.1; -; mRNA.
DR   AlphaFoldDB; E7E2N8; -.
DR   SMR; E7E2N8; -.
DR   Proteomes; UP000515129; Genome assembly.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR   GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IEA:InterPro.
DR   GO; GO:0047134; F:protein-disulfide reductase (NAD(P)) activity; IDA:UniProtKB.
DR   GO; GO:0019882; P:antigen processing and presentation; IDA:UniProtKB.
DR   InterPro; IPR004911; Interferon-induced_GILT.
DR   InterPro; IPR003119; SAP_A.
DR   PANTHER; PTHR13234; PTHR13234; 1.
DR   Pfam; PF03227; GILT; 1.
DR   Pfam; PF02199; SapA; 1.
DR   PROSITE; PS51110; SAP_A; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Immunity; Lysosome; Oxidoreductase;
KW   Redox-active center; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..251
FT                   /note="Gamma-interferon-inducible lysosomal thiol
FT                   reductase"
FT                   /id="PRO_5003217147"
FT   DOMAIN          22..60
FT                   /note="Saposin A-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00414"
FT   CARBOHYD        108
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        68..71
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:P13284"
SQ   SEQUENCE   251 AA;  27803 MW;  EEBECE6BCC4348DD CRC64;
     MFGFRLSVLL FAVCSLSACS CMFVNSCKYP PSQWCDSRDI AAQCGVLEQC MKFNASPVTV
     SLYYESLCPG CREFLVSQLV PTFIMLSDIM NIELVPYGNA QEKDDQGNYT FICQHGEDEC
     RGNMIETCLL KALGPKAIPV IFCMESGADV LKAAQPCLGV YFPDTTWDSV MKCVTGDEGN
     KLMHQNALKT NALKPPHEYV PWITINGEHT DDLQDKATNS LFNLVCSLYK GEKPAACGQG
     LKKRTNSYCM N