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GILT2_DROME
ID   GILT2_DROME             Reviewed;         207 AA.
AC   Q9VCK1;
DT   15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 171.
DE   RecName: Full=GILT-like protein 2 {ECO:0000305};
DE            EC=1.8.-.- {ECO:0000250|UniProtKB:P13284};
DE   Flags: Precursor;
GN   Name=GILT2 {ECO:0000312|FlyBase:FBgn0039099};
GN   ORFNames=CG10157 {ECO:0000312|FlyBase:FBgn0039099};
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:AAM12281.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley {ECO:0000312|EMBL:AAM12281.1};
RC   TISSUE=Embryo {ECO:0000312|EMBL:AAM12281.1};
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, 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).
CC   -!- FUNCTION: Probable lysosomal thiol reductase that can reduce protein
CC       disulfide bonds (By similarity). Involved in the immune response to
CC       bacterial infection (PubMed:24491521). {ECO:0000250|UniProtKB:P13284,
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   -!- 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}.
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DR   EMBL; AE014297; AAF56157.1; -; Genomic_DNA.
DR   EMBL; AY095188; AAM12281.1; -; mRNA.
DR   RefSeq; NP_651166.1; NM_142909.4.
DR   AlphaFoldDB; Q9VCK1; -.
DR   SMR; Q9VCK1; -.
DR   IntAct; Q9VCK1; 3.
DR   STRING; 7227.FBpp0083827; -.
DR   GlyGen; Q9VCK1; 1 site.
DR   PaxDb; Q9VCK1; -.
DR   PRIDE; Q9VCK1; -.
DR   DNASU; 42788; -.
DR   EnsemblMetazoa; FBtr0084435; FBpp0083827; FBgn0039099.
DR   GeneID; 42788; -.
DR   KEGG; dme:Dmel_CG10157; -.
DR   UCSC; CG10157-RA; d. melanogaster.
DR   CTD; 42788; -.
DR   FlyBase; FBgn0039099; GILT2.
DR   VEuPathDB; VectorBase:FBgn0039099; -.
DR   eggNOG; KOG3160; Eukaryota.
DR   GeneTree; ENSGT00940000173058; -.
DR   HOGENOM; CLU_066886_2_2_1; -.
DR   InParanoid; Q9VCK1; -.
DR   OMA; FCAKYKE; -.
DR   OrthoDB; 803513at2759; -.
DR   PhylomeDB; Q9VCK1; -.
DR   Reactome; R-DME-2132295; MHC class II antigen presentation.
DR   SignaLink; Q9VCK1; -.
DR   BioGRID-ORCS; 42788; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 42788; -.
DR   PRO; PR:Q9VCK1; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0039099; Expressed in seminal fluid secreting gland and 24 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   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   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR13234; PTHR13234; 1.
DR   Pfam; PF03227; GILT; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Immunity; Oxidoreductase;
KW   Redox-active center; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..207
FT                   /note="GILT-like protein 2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5008180644"
FT   CARBOHYD        182
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        40..43
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:P13284"
SQ   SEQUENCE   207 AA;  23506 MW;  D87B6A3BCBC2040B CRC64;
     MRAAVFVCLL LGWVGVATPR RLRGPQADRL AITLYYEALC PYCMEFVTTQ LNPSMVRQDR
     LPFTDLTLVP YGNARTNDDG NVECQHGVME CELNAWHACI LEHHDIAQSL KLIACMMRGK
     KNRLEKCADH YQIDVGDVKN CKKTRQVNDI LRKYGKETAK VSFQGVPAVA LDNVYNADLS
     ANLTDHFDAI FCAKYKEKFN KQLNNCQ
 
 
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