GILT_DANRE
ID GILT_DANRE Reviewed; 255 AA.
AC Q5XJN2;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Gamma-interferon-inducible lysosomal thiol reductase {ECO:0000303|PubMed:22982335};
DE EC=1.8.-.- {ECO:0000269|PubMed:22982335};
DE AltName: Full=Gamma-interferon-inducible protein IP-30 {ECO:0000250|UniProtKB:P13284};
DE Flags: Precursor;
GN Name=ifi30 {ECO:0000312|ZFIN:ZDB-GENE-030131-8447};
GN Synonyms=GILT {ECO:0000303|PubMed:22982335};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|EMBL:AAH83267.1};
RN [1] {ECO:0000312|EMBL:AFV57380.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=22982335; DOI=10.1016/j.fsi.2012.08.021;
RA Cui X.W., Ji C.B., Cao X.G., Fu Z.Y., Zhang S.Q., Guo X.R.;
RT "Molecular and biological characterization of interferon-gamma-inducible-
RT lysosomal thiol reductase gene in zebrafish (Danio rerio).";
RL Fish Shellfish Immunol. 33:1133-1138(2012).
RN [2] {ECO:0000312|EMBL:CR769774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3] {ECO:0000312|EMBL:AAH83267.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2008) 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 {ECO:0000269|PubMed:22982335}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4-5. {ECO:0000269|PubMed:22982335};
CC -!- SUBUNIT: Dimer; disulfide-linked. {ECO:0000250|UniProtKB:P13284}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P13284}. Lysosome
CC {ECO:0000250|UniProtKB:P13284}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in spleen and kidney. Also
CC detected at lower levels in heart, liver, intestine and muscle.
CC {ECO:0000269|PubMed:22982335}.
CC -!- INDUCTION: Up-regulated in spleen and kidney in response to bacterial
CC lipopolysaccharide (LPS). {ECO:0000269|PubMed:22982335}.
CC -!- SIMILARITY: Belongs to the GILT family. {ECO:0000305}.
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DR EMBL; JX018169; AFV57380.1; -; mRNA.
DR EMBL; CR769774; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC083267; AAH83267.1; -; mRNA.
DR EMBL; BC165122; AAI65122.1; -; mRNA.
DR RefSeq; NP_001006057.1; NM_001006057.1.
DR AlphaFoldDB; Q5XJN2; -.
DR SMR; Q5XJN2; -.
DR STRING; 7955.ENSDARP00000073325; -.
DR PaxDb; Q5XJN2; -.
DR Ensembl; ENSDART00000078866; ENSDARP00000073325; ENSDARG00000056378.
DR Ensembl; ENSDART00000191692; ENSDARP00000153401; ENSDARG00000112359.
DR GeneID; 336503; -.
DR KEGG; dre:336503; -.
DR CTD; 10437; -.
DR ZFIN; ZDB-GENE-030131-8447; ifi30.
DR eggNOG; KOG3160; Eukaryota.
DR GeneTree; ENSGT00940000164804; -.
DR HOGENOM; CLU_066886_0_0_1; -.
DR InParanoid; Q5XJN2; -.
DR OMA; ITEQVYP; -.
DR OrthoDB; 803513at2759; -.
DR PhylomeDB; Q5XJN2; -.
DR TreeFam; TF315141; -.
DR Reactome; R-DRE-2132295; MHC class II antigen presentation.
DR PRO; PR:Q5XJN2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 2.
DR Bgee; ENSDARG00000056378; Expressed in intestine and 21 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016667; F:oxidoreductase activity, acting on a sulfur group of donors; IBA:GO_Central.
DR GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IDA:ZFIN.
DR GO; GO:0047134; F:protein-disulfide reductase (NAD(P)) activity; IDA:CACAO.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
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.
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..255
FT /note="Gamma-interferon-inducible lysosomal thiol
FT reductase"
FT /evidence="ECO:0000255"
FT /id="PRO_5010844840"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 72..75
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:P13284"
SQ SEQUENCE 255 AA; 28327 MW; 122084F58FFC379A CRC64;
MFGFNLCVVL VAVFSLSKCS ARFVYSCKYP PSQWCSSEDI AAECGVLEQC MKYNSTKAAD
KVKVSLYYES LCPGCRMFLT SQLVPTLIML QDIMEIDLVP YGNAQETQAQ GKYIFTCQHG
EDECLGNMIE TCMLNKLGLD AVMVIFCMES GNDVLKSAQP CLGVYRPDVT WDSIMQCVKG
DQGNKLMHEN AVKTDALNPP HQYVPWITVN GEHTDDLQDK AMGSLFSLVC SLYKGQKPAA
CTLGLKKNTN NYCMN
