SPS1_DROME
ID SPS1_DROME Reviewed; 398 AA.
AC O18373; O18597; Q0E979; Q9V700;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Inactive selenide, water dikinase-like protein;
DE AltName: Full=Protein patufet;
DE AltName: Full=dSelD;
GN Name=SelD; Synonyms=PTF1, ptuf; ORFNames=CG8553;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Canton-S; TISSUE=Embryo;
RX PubMed=9398525; DOI=10.1006/jmbi.1997.1371;
RA Persson B.C., Boeck A., Jaeckle H., Vorbrueggen G.;
RT "SelD homolog from Drosophila lacking selenide-dependent
RT monoselenophosphate synthetase activity.";
RL J. Mol. Biol. 274:174-180(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=9491069; DOI=10.1007/s004380050630;
RA Alsina B., Serras F., Baguna J., Corominas M.;
RT "patufet, the gene encoding the Drosophila melanogaster homologue of
RT selenophosphate synthetase, is involved in imaginal disc morphogenesis.";
RL Mol. Gen. Genet. 257:113-123(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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]
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10444382; DOI=10.1242/jcs.112.17.2875;
RA Alsina B., Corominas M., Berry M.J., Baguna J., Serras F.;
RT "Disruption of selenoprotein biosynthesis affects cell proliferation in the
RT imaginal discs and brain of Drosophila melanogaster.";
RL J. Cell Sci. 112:2875-2884(1999).
CC -!- FUNCTION: Plays a role in apoptosis and consequently a role in imaginal
CC disk patterning and growth. {ECO:0000269|PubMed:10444382,
CC ECO:0000269|PubMed:9491069}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels throughout the embryo. At
CC later developmental stages, expressed in areas of high cell
CC proliferation. From embryo stage 13, expression is high in central
CC nervous system and midgut, especially in the gastric caeca. Expression
CC also seen in larval imaginal disks and brain.
CC {ECO:0000269|PubMed:10444382, ECO:0000269|PubMed:9398525,
CC ECO:0000269|PubMed:9491069}.
CC -!- DEVELOPMENTAL STAGE: Throughout development, from embryo to adult.
CC {ECO:0000269|PubMed:9491069}.
CC -!- SIMILARITY: Belongs to the selenophosphate synthase 1 family. Class II
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: The conserved active site Cys (or selenocysteine) residue in
CC position 49 is replaced by an Arg and therefore lacks selenide-
CC dependent monoselenophosphate synthetase activity.
CC {ECO:0000269|PubMed:9398525}.
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DR EMBL; AJ000672; CAA04229.1; -; mRNA.
DR EMBL; U91994; AAB88790.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF58266.1; -; Genomic_DNA.
DR EMBL; AY095058; AAM11386.1; -; mRNA.
DR RefSeq; NP_725374.1; NM_166045.2.
DR RefSeq; NP_725375.1; NM_166046.2.
DR AlphaFoldDB; O18373; -.
DR SMR; O18373; -.
DR BioGRID; 62337; 12.
DR DIP; DIP-21887N; -.
DR IntAct; O18373; 6.
DR STRING; 7227.FBpp0086691; -.
DR PaxDb; O18373; -.
DR PRIDE; O18373; -.
DR DNASU; 36587; -.
DR EnsemblMetazoa; FBtr0087564; FBpp0086690; FBgn0261270.
DR EnsemblMetazoa; FBtr0087565; FBpp0086691; FBgn0261270.
DR GeneID; 36587; -.
DR KEGG; dme:Dmel_CG8553; -.
DR CTD; 36587; -.
DR FlyBase; FBgn0261270; SelD.
DR VEuPathDB; VectorBase:FBgn0261270; -.
DR eggNOG; KOG3939; Eukaryota.
DR GeneTree; ENSGT00390000000950; -.
DR HOGENOM; CLU_032859_1_0_1; -.
DR InParanoid; O18373; -.
DR OMA; RWNKINM; -.
DR OrthoDB; 1166567at2759; -.
DR PhylomeDB; O18373; -.
DR BRENDA; 2.7.9.3; 1994.
DR Reactome; R-DME-2408557; Selenocysteine synthesis.
DR BioGRID-ORCS; 36587; 2 hits in 3 CRISPR screens.
DR GenomeRNAi; 36587; -.
DR PRO; PR:O18373; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0261270; Expressed in egg cell and 30 other tissues.
DR Genevisible; O18373; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0010637; P:negative regulation of mitochondrial fusion; IMP:FlyBase.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IMP:FlyBase.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd02195; SelD; 1.
DR Gene3D; 3.30.1330.10; -; 1.
DR Gene3D; 3.90.650.10; -; 1.
DR InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR016188; PurM-like_N.
DR InterPro; IPR036921; PurM-like_N_sf.
DR InterPro; IPR004536; SPS/SelD.
DR PANTHER; PTHR10256; PTHR10256; 1.
DR Pfam; PF00586; AIRS; 1.
DR Pfam; PF02769; AIRS_C; 1.
DR PIRSF; PIRSF036407; Selenphspht_syn; 1.
DR SUPFAM; SSF55326; SSF55326; 1.
DR SUPFAM; SSF56042; SSF56042; 1.
DR TIGRFAMs; TIGR00476; selD; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; Developmental protein; Kinase; Nucleotide-binding;
KW Reference proteome; Selenium; Transferase.
FT CHAIN 1..398
FT /note="Inactive selenide, water dikinase-like protein"
FT /id="PRO_0000127652"
FT CONFLICT 253..254
FT /note="ED -> KN (in Ref. 2; AAB88790)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 398 AA; 43446 MW; B265DAF4FDACC2D8 CRC64;
MSYAADVLNS AHLELHGGGD AELRRPFDPT AHDLDASFRL TRFADLKGRG CKVPQDVLSK
LVSALQQDYS AQDQEPQFLN VAIPRIGIGL DCSVIPLRHG GLCLVQTTDF FYPIVDDPYM
MGKIACANVL SDLYAMGVTD CDNMLMLLAV STKMTEKERD VVIPLIMRGF KDSALEAGTT
VTGGQSVVNP WCTIGGVAST ICQPNEYIVP DNAVVGDVLV LTKPLGTQVA VNAHQWIDQP
ERWNRIKLVV SEEDVRKAYH RAMNSMARLN RVAARLMHKY NAHGATDITG FGLLGHAQTL
AAHQKKDVSF VIHNLPVIAK MAAVAKACGN MFQLLQGHSA ETSGGLLICL PREQAAAYCK
DIEKQEGYQA WIIGIVEKGN KTARIIDKPR VIEVPAKD
