GILT3_DROME
ID GILT3_DROME Reviewed; 216 AA.
AC Q9VCK2;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=GILT-like protein 3 {ECO:0000305};
DE Flags: Precursor;
GN Name=GILT3 {ECO:0000312|FlyBase:FBgn0039098};
GN ORFNames=CG13822 {ECO:0000312|FlyBase:FBgn0039098};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAL48654.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL48654.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAL48654.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000305}
RP FUNCTION, AND INDUCTION.
RX PubMed=24491521; DOI=10.1016/j.dci.2014.01.007;
RA Kongton K., McCall K., Phongdara A.;
RT "Identification of gamma-interferon-inducible lysosomal thiol reductase
RT (GILT) homologues in the fruit fly Drosophila melanogaster.";
RL Dev. Comp. Immunol. 44:389-396(2014).
CC -!- FUNCTION: Involved in the immune response to bacterial infection.
CC {ECO:0000269|PubMed:24491521}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- INDUCTION: Up-regulated following injection with the Gram-negative
CC bacterium E.coli. Up-regulation increases between 1 and 12 hours after
CC the injection, then decreases between 12 and 48 hours, and then
CC increases again at 72 hours. {ECO:0000269|PubMed:24491521}.
CC -!- SIMILARITY: Belongs to the GILT family. {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved active site CXXC motif that is essential
CC for thiol reductase activity. Its enzyme activity is therefore unsure.
CC {ECO:0000305|PubMed:24491521}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014297; AAF56156.1; -; Genomic_DNA.
DR EMBL; AY071032; AAL48654.1; -; mRNA.
DR RefSeq; NP_651165.1; NM_142908.3.
DR AlphaFoldDB; Q9VCK2; -.
DR SMR; Q9VCK2; -.
DR IntAct; Q9VCK2; 1.
DR STRING; 7227.FBpp0083826; -.
DR GlyGen; Q9VCK2; 1 site.
DR PaxDb; Q9VCK2; -.
DR PRIDE; Q9VCK2; -.
DR DNASU; 42787; -.
DR EnsemblMetazoa; FBtr0084434; FBpp0083826; FBgn0039098.
DR GeneID; 42787; -.
DR KEGG; dme:Dmel_CG13822; -.
DR UCSC; CG13822-RA; d. melanogaster.
DR CTD; 42787; -.
DR FlyBase; FBgn0039098; GILT3.
DR VEuPathDB; VectorBase:FBgn0039098; -.
DR eggNOG; KOG3160; Eukaryota.
DR GeneTree; ENSGT00940000173058; -.
DR HOGENOM; CLU_066886_2_2_1; -.
DR InParanoid; Q9VCK2; -.
DR OMA; FDLIYCM; -.
DR OrthoDB; 803513at2759; -.
DR PhylomeDB; Q9VCK2; -.
DR Reactome; R-DME-2132295; MHC class II antigen presentation.
DR SignaLink; Q9VCK2; -.
DR BioGRID-ORCS; 42787; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 42787; -.
DR PRO; PR:Q9VCK2; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0039098; Expressed in seminal fluid secreting gland and 23 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:FlyBase.
DR GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IEA:InterPro.
DR InterPro; IPR004911; Interferon-induced_GILT.
DR PANTHER; PTHR13234; PTHR13234; 1.
DR Pfam; PF03227; GILT; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..216
FT /note="GILT-like protein 3"
FT /evidence="ECO:0000255"
FT /id="PRO_5008180666"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 216 AA; 24721 MW; A8A2D1506C92313A CRC64;
MNKIFGLLFT LCLLLVWPTP GNGQSPDESR LLVAIHYEAL CPDSMSFIRR RLYDALQDND
WWSVTDLKLY PFGKAGFYNN TSTGESQVFC QHGVDECELN ALHACIIETL DIRKAFNLIY
CMLRSYSNEL GPCSRSMGVD VSKARECKAS RTTAEILAPY GKETLKLGIS FVPTIVFEND
FDPYDQRSIR NNFERHFCRQ YLKKFNIKLP TCSAIL