SELG_DROME
ID SELG_DROME Reviewed; 110 AA.
AC Q7Z2C4; Q2V8Y4; Q962X6; Q9VYS7;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Glycine-rich selenoprotein;
DE Short=G-rich selenoprotein;
DE AltName: Full=dSelG;
GN Name=SelG; Synonyms=G-rich; ORFNames=CG1844;
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|EMBL:AAF48111.2};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S {ECO:0000269|PubMed:11389138};
RC TISSUE=Embryo {ECO:0000269|PubMed:11389138}, and
RC Larva {ECO:0000269|PubMed:11389138};
RX PubMed=11389138; DOI=10.1074/jbc.m100422200;
RA Martin-Romero F.J., Kryukov G.V., Lobanov A.V., Carlson B.A., Lee B.J.,
RA Gladyshev V.N., Hatfield D.L.;
RT "Selenium metabolism in Drosophila: selenoproteins, selenoprotein mRNA
RT expression, fertility, and mortality.";
RL J. Biol. Chem. 276:29798-29804(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=16920070; DOI=10.1016/j.bbrc.2006.07.203;
RA Chen C.L., Shim M.S., Chung J., Yoo H.-S., Ha J.M., Kim J.Y., Choi J.,
RA Zang S.L., Hou X., Carlson B.A., Hatfield D.L., Lee B.J.;
RT "G-rich, a Drosophila selenoprotein, is a Golgi-resident type III membrane
RT protein.";
RL Biochem. Biophys. Res. Commun. 348:1296-1301(2006).
RN [3] {ECO:0000312|EMBL:AAF48111.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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 [4] {ECO:0000305}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
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 [5] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
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 [6] {ECO:0000305}
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=11493597; DOI=10.1093/embo-reports/kve151;
RA Castellano S., Morozova N., Morey M., Berry M.J., Serras F., Corominas M.,
RA Guigo R.;
RT "In silico identification of novel selenoproteins in the Drosophila
RT melanogaster genome.";
RL EMBO Rep. 2:697-702(2001).
CC -!- FUNCTION: Plays a role in the life span. May be involved in regulating
CC the redox state of the cell and possesses anticarcinogenic properties.
CC {ECO:0000269|PubMed:11389138, ECO:0000303|PubMed:11493597}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:16920070}; Single-pass type III membrane protein
CC {ECO:0000269|PubMed:16920070}.
CC -!- DEVELOPMENTAL STAGE: Expressed in larvae and adults but strongest
CC expression is found in embryos, within syncytial blastoderm, cellular
CC blastoderm and gastrulation stages. {ECO:0000269|PubMed:11389138,
CC ECO:0000269|PubMed:11493597}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL28159.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF396454; AAK72981.1; -; mRNA.
DR EMBL; DQ285021; ABB90104.1; -; mRNA.
DR EMBL; AE014298; AAF48111.2; -; Genomic_DNA.
DR EMBL; AY060611; AAL28159.1; ALT_SEQ; mRNA.
DR RefSeq; NP_572763.3; NM_132535.3.
DR BioGRID; 58554; 1.
DR STRING; 7227.FBpp0073414; -.
DR PaxDb; Q7Z2C4; -.
DR DNASU; 32149; -.
DR EnsemblMetazoa; FBtr0073570; FBpp0073414; FBgn0030350.
DR GeneID; 32149; -.
DR KEGG; dme:Dmel_CG1844; -.
DR CTD; 32149; -.
DR FlyBase; FBgn0030350; SelG.
DR VEuPathDB; VectorBase:FBgn0030350; -.
DR eggNOG; ENOG502S803; Eukaryota.
DR GeneTree; ENSGT00940000176559; -.
DR HOGENOM; CLU_179538_0_0_1; -.
DR InParanoid; Q7Z2C4; -.
DR OMA; SCNMPAG; -.
DR OrthoDB; 1583096at2759; -.
DR PhylomeDB; Q7Z2C4; -.
DR BioGRID-ORCS; 32149; 0 hits in 1 CRISPR screen.
DR ChiTaRS; SelG; fly.
DR GenomeRNAi; 32149; -.
DR PRO; PR:Q7Z2C4; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0030350; Expressed in spermathecum and 25 other tissues.
DR ExpressionAtlas; Q7Z2C4; baseline and differential.
DR Genevisible; Q7Z2C4; DM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:FlyBase.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:FlyBase.
DR GO; GO:0007350; P:blastoderm segmentation; IDA:FlyBase.
DR GO; GO:0006816; P:calcium ion transport; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; TAS:UniProtKB.
DR GO; GO:0008340; P:determination of adult lifespan; IDA:UniProtKB.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IDA:UniProtKB.
DR GO; GO:0001700; P:embryonic development via the syncytial blastoderm; IDA:FlyBase.
DR GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; IMP:FlyBase.
DR GO; GO:0010470; P:regulation of gastrulation; IDA:FlyBase.
DR InterPro; IPR024491; Se_SelK/SelG.
DR PANTHER; PTHR16875; PTHR16875; 1.
DR Pfam; PF10961; SelK_SelG; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Golgi apparatus; Membrane; Reference proteome;
KW Selenocysteine; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..110
FT /note="Glycine-rich selenoprotein"
FT /id="PRO_0000097666"
FT TOPO_DOM 1..20
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..41
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..110
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 48..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_STD 109
FT /note="Selenocysteine"
FT /evidence="ECO:0000269|PubMed:11389138"
SQ SEQUENCE 110 AA; 11574 MW; 7C08E5AF12D30662 CRC64;
MVYIDHNGRV WEKRPWDWRR IVELFVGIWF AIKQLFLTFL APFTGNNNQA NPRRGNGWGG
GGGWGGGGGG GGGGGGGRPG SGSGGLRPNR RIGRIQPTMS CNMPAGGGUG
