GILT1_DROME
ID GILT1_DROME Reviewed; 250 AA.
AC Q95RA9; Q9VFV4;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=GILT-like protein 1 {ECO:0000305};
DE Flags: Precursor;
GN Name=GILT1 {ECO:0000312|FlyBase:FBgn0038149};
GN ORFNames=CG9796 {ECO:0000312|FlyBase:FBgn0038149};
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:AAL29067.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL29067.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAL29067.1};
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
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).
RN [5]
RP URMYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=28953965; DOI=10.1371/journal.pone.0185611;
RA Khoshnood B., Dacklin I., Grabbe C.;
RT "A proteomics approach to identify targets of the ubiquitin-like molecule
RT Urm1 in Drosophila melanogaster.";
RL PLoS ONE 12:E0185611-E0185611(2017).
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 6 hours after
CC the injection, then expression remains at a relatively steady level
CC until 72 hours when it is strongly up-regulated.
CC {ECO:0000269|PubMed:24491521}.
CC -!- PTM: Conjugated to URM1, a ubiquitin-like protein.
CC {ECO:0000269|PubMed:28953965}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in the fat body or
CC hemocyte of flies infected with the Gram-negative bacterium E.coli
CC results in an increase in bacterial load 24 hours after infection.
CC {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}.
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DR EMBL; AE014297; AAF54945.2; -; Genomic_DNA.
DR EMBL; AY061519; AAL29067.1; -; mRNA.
DR RefSeq; NP_650287.3; NM_142030.4.
DR AlphaFoldDB; Q95RA9; -.
DR SMR; Q95RA9; -.
DR IntAct; Q95RA9; 15.
DR STRING; 7227.FBpp0082228; -.
DR GlyGen; Q95RA9; 1 site.
DR PaxDb; Q95RA9; -.
DR PRIDE; Q95RA9; -.
DR DNASU; 41650; -.
DR EnsemblMetazoa; FBtr0082760; FBpp0082228; FBgn0038149.
DR GeneID; 41650; -.
DR KEGG; dme:Dmel_CG9796; -.
DR UCSC; CG9796-RA; d. melanogaster.
DR CTD; 41650; -.
DR FlyBase; FBgn0038149; GILT1.
DR VEuPathDB; VectorBase:FBgn0038149; -.
DR eggNOG; KOG3160; Eukaryota.
DR HOGENOM; CLU_066886_2_1_1; -.
DR InParanoid; Q95RA9; -.
DR OMA; ITEQVYP; -.
DR OrthoDB; 803513at2759; -.
DR PhylomeDB; Q95RA9; -.
DR Reactome; R-DME-2132295; MHC class II antigen presentation.
DR BioGRID-ORCS; 41650; 0 hits in 1 CRISPR screen.
DR ChiTaRS; GILT1; fly.
DR GenomeRNAi; 41650; -.
DR PRO; PR:Q95RA9; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0038149; Expressed in eye disc (Drosophila) and 34 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
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 GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:1900426; P:positive regulation of defense response to bacterium; IMP:FlyBase.
DR InterPro; IPR004911; Interferon-induced_GILT.
DR PANTHER; PTHR13234; PTHR13234; 1.
DR Pfam; PF03227; GILT; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Immunity; Reference proteome; Secreted; Signal;
KW Ubl conjugation.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..250
FT /note="GILT-like protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_5008179656"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 250 AA; 27692 MW; 3F55649BFED5D547 CRC64;
MSHKIAAVCL LMSCLIATAY SAAKVPISIY YESLCPDSAK FITEQVYPAV KGELRDVVEL
TFVPFGKSQF VTQGSEVTFT CHHGPNECYG NKVHACAIEH IQANSYQVEY TRESLTMDFI
NCLMKAGKNF PDNVYPGQRC ASENHINNWE NIKTCANSTE GSVLLRKAGE STMRLKEPLT
SVPTILFNEQ FDKKVNDRAQ VNLVGTICQY VSAPQPRICN QHNGASTPSL ASVSAILSSL
LGLWFIRSFY
