SPS1_HUMAN
ID SPS1_HUMAN Reviewed; 392 AA.
AC P49903; B4DWK0; D3DRS9; D6PSQ9; Q5T5U8; Q5T5U9; Q9BVT4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Selenide, water dikinase 1;
DE EC=2.7.9.3 {ECO:0000269|PubMed:7665581};
DE AltName: Full=Selenium donor protein 1;
DE AltName: Full=Selenophosphate synthase 1;
GN Name=SEPHS1; Synonyms=SELD, SPS, SPS1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP ATP-BINDING, AND MUTAGENESIS OF GLY-268; GLY-270; GLY-273 AND HIS-274.
RC TISSUE=Liver;
RX PubMed=7665581; DOI=10.1074/jbc.270.37.21659;
RA Low S.C., Harney J.W., Berry M.J.;
RT "Cloning and functional characterization of human selenophosphate
RT synthetase, an essential component of selenoprotein synthesis.";
RL J. Biol. Chem. 270:21659-21664(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), SUBUNIT, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20471958; DOI=10.1016/j.bbrc.2010.05.055;
RA Kim J.Y., Lee K.H., Shim M.S., Shin H., Xu X.M., Carlson B.A.,
RA Hatfield D.L., Lee B.J.;
RT "Human selenophosphate synthetase 1 has five splice variants with unique
RT interactions, subcellular localizations and expression patterns.";
RL Biochem. Biophys. Res. Commun. 397:53-58(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Mammary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta, and PNS;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 5-16 AND 64-76, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ADP; MAGNESIUM IONS
RP AND PHOSPHATE, SUBUNIT, ACTIVITY REGULATION, AND MUTAGENESIS OF THR-85.
RX PubMed=19477186; DOI=10.1016/j.jmb.2009.05.032;
RA Wang K.T., Wang J., Li L.F., Su X.D.;
RT "Crystal structures of catalytic intermediates of human selenophosphate
RT synthetase 1.";
RL J. Mol. Biol. 390:747-759(2009).
CC -!- FUNCTION: Synthesizes selenophosphate from selenide and ATP.
CC {ECO:0000269|PubMed:7665581}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + hydrogenselenide = AMP + 2 H(+) + phosphate +
CC selenophosphate; Xref=Rhea:RHEA:18737, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16144, ChEBI:CHEBI:29317,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456215; EC=2.7.9.3;
CC Evidence={ECO:0000269|PubMed:7665581};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:19477186};
CC Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000269|PubMed:19477186};
CC -!- ACTIVITY REGULATION: Activated by phosphate ions and by potassium ions.
CC {ECO:0000269|PubMed:19477186}.
CC -!- SUBUNIT: [Isoform 1]: Homodimer (PubMed:20471958, PubMed:19477186).
CC Heterodimer with isoform 3 (PubMed:20471958).
CC {ECO:0000269|PubMed:19477186, ECO:0000269|PubMed:20471958}.
CC -!- SUBUNIT: [Isoform 2]: Homodimer (PubMed:20471958). Heterodimer with
CC isoform 4 (PubMed:20471958). {ECO:0000269|PubMed:20471958}.
CC -!- SUBUNIT: [Isoform 3]: Homodimer (PubMed:20471958). Heterodimer with
CC isoform 1 (PubMed:20471958). {ECO:0000269|PubMed:20471958}.
CC -!- SUBUNIT: [Isoform 4]: Homodimer (PubMed:20471958). Heterodimer with
CC isoform 2 (PubMed:20471958). {ECO:0000269|PubMed:20471958}.
CC -!- INTERACTION:
CC P49903; Q9UPG8: PLAGL2; NbExp=3; IntAct=EBI-714091, EBI-2876622;
CC P49903; Q2TAL8: QRICH1; NbExp=8; IntAct=EBI-714091, EBI-2798044;
CC P49903; P49903: SEPHS1; NbExp=6; IntAct=EBI-714091, EBI-714091;
CC P49903; Q6GPH4: XAF1; NbExp=3; IntAct=EBI-714091, EBI-2815120;
CC P49903; P24278: ZBTB25; NbExp=7; IntAct=EBI-714091, EBI-739899;
CC P49903; O95125: ZNF202; NbExp=5; IntAct=EBI-714091, EBI-751960;
CC P49903; Q8N554: ZNF276; NbExp=3; IntAct=EBI-714091, EBI-750821;
CC P49903; Q6S9Z5: ZNF474; NbExp=3; IntAct=EBI-714091, EBI-17269964;
CC P49903; Q8TF50: ZNF526; NbExp=3; IntAct=EBI-714091, EBI-11035148;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:20471958}; Peripheral membrane protein
CC {ECO:0000305}. Nucleus membrane {ECO:0000269|PubMed:20471958};
CC Peripheral membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:20471958}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm
CC {ECO:0000269|PubMed:20471958}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm
CC {ECO:0000269|PubMed:20471958}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Major type, MT;
CC IsoId=P49903-1; Sequence=Displayed;
CC Name=2; Synonyms=Delta E8;
CC IsoId=P49903-2; Sequence=VSP_046702;
CC Name=3; Synonyms=Delta E2;
CC IsoId=P49903-3; Sequence=VSP_046701;
CC Name=4; Synonyms=E9, E9a;
CC IsoId=P49903-4; Sequence=VSP_047451;
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Gradually expressed during the cell
CC cycle until G2/M phase and then decreases.
CC {ECO:0000269|PubMed:20471958}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Gradually expressed during the cell
CC cycle until G2/M phase and then decreases.
CC {ECO:0000269|PubMed:20471958}.
CC -!- TISSUE SPECIFICITY: [Isoform 3]: Gradually expressed during the cell
CC cycle until S phase and then decreases. {ECO:0000269|PubMed:20471958}.
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 29 is replaced by a Thr. However, as function in selenoprotein
CC synthesis is proven, it is possible Cys-31 is the active site.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA87567.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U34044; AAA87567.1; ALT_FRAME; mRNA.
DR EMBL; GU954545; ADF78120.1; -; mRNA.
DR EMBL; GU954546; ADF78121.1; -; mRNA.
DR EMBL; GU954547; ADF78122.1; -; mRNA.
DR EMBL; GU954548; ADF78123.1; -; mRNA.
DR EMBL; GU954549; ADF78124.1; -; mRNA.
DR EMBL; AK301568; BAG63062.1; -; mRNA.
DR EMBL; AL138764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355870; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471072; EAW86289.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW86290.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW86291.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW86292.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW86293.1; -; Genomic_DNA.
DR EMBL; BC000941; AAH00941.1; -; mRNA.
DR EMBL; BC063816; AAH63816.1; -; mRNA.
DR CCDS; CCDS55702.1; -. [P49903-3]
DR CCDS; CCDS55703.1; -. [P49903-2]
DR CCDS; CCDS7098.1; -. [P49903-1]
DR RefSeq; NP_001182531.1; NM_001195602.1. [P49903-3]
DR RefSeq; NP_001182533.1; NM_001195604.1. [P49903-2]
DR RefSeq; NP_036379.2; NM_012247.4. [P49903-1]
DR RefSeq; XP_016871431.1; XM_017015942.1.
DR RefSeq; XP_016871432.1; XM_017015943.1. [P49903-1]
DR RefSeq; XP_016871434.1; XM_017015945.1.
DR PDB; 3FD5; X-ray; 1.90 A; A/B=1-392.
DR PDB; 3FD6; X-ray; 1.95 A; A/B=1-392.
DR PDBsum; 3FD5; -.
DR PDBsum; 3FD6; -.
DR AlphaFoldDB; P49903; -.
DR SMR; P49903; -.
DR BioGRID; 116589; 63.
DR CORUM; P49903; -.
DR IntAct; P49903; 23.
DR MINT; P49903; -.
DR STRING; 9606.ENSP00000367893; -.
DR GlyGen; P49903; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P49903; -.
DR MetOSite; P49903; -.
DR PhosphoSitePlus; P49903; -.
DR SwissPalm; P49903; -.
DR BioMuta; SEPHS1; -.
DR DMDM; 27151792; -.
DR EPD; P49903; -.
DR jPOST; P49903; -.
DR MassIVE; P49903; -.
DR MaxQB; P49903; -.
DR PaxDb; P49903; -.
DR PeptideAtlas; P49903; -.
DR PRIDE; P49903; -.
DR ProteomicsDB; 12836; -.
DR ProteomicsDB; 5348; -.
DR ProteomicsDB; 56175; -. [P49903-1]
DR ProteomicsDB; 64555; -.
DR Antibodypedia; 24810; 195 antibodies from 30 providers.
DR DNASU; 22929; -.
DR Ensembl; ENST00000327347.10; ENSP00000367893.3; ENSG00000086475.15. [P49903-1]
DR Ensembl; ENST00000378614.8; ENSP00000367877.3; ENSG00000086475.15. [P49903-2]
DR Ensembl; ENST00000545675.5; ENSP00000441119.2; ENSG00000086475.15. [P49903-3]
DR GeneID; 22929; -.
DR KEGG; hsa:22929; -.
DR MANE-Select; ENST00000327347.10; ENSP00000367893.3; NM_012247.5; NP_036379.2.
DR UCSC; uc001imk.4; human. [P49903-1]
DR CTD; 22929; -.
DR DisGeNET; 22929; -.
DR GeneCards; SEPHS1; -.
DR HGNC; HGNC:19685; SEPHS1.
DR HPA; ENSG00000086475; Low tissue specificity.
DR MIM; 600902; gene.
DR neXtProt; NX_P49903; -.
DR OpenTargets; ENSG00000086475; -.
DR PharmGKB; PA134905215; -.
DR VEuPathDB; HostDB:ENSG00000086475; -.
DR eggNOG; KOG3939; Eukaryota.
DR GeneTree; ENSGT00390000000950; -.
DR HOGENOM; CLU_032859_1_0_1; -.
DR InParanoid; P49903; -.
DR OMA; DNEPKYG; -.
DR OrthoDB; 1166567at2759; -.
DR PhylomeDB; P49903; -.
DR TreeFam; TF313811; -.
DR BRENDA; 2.7.9.3; 2681.
DR PathwayCommons; P49903; -.
DR SignaLink; P49903; -.
DR BioGRID-ORCS; 22929; 131 hits in 1079 CRISPR screens.
DR ChiTaRS; SEPHS1; human.
DR EvolutionaryTrace; P49903; -.
DR GeneWiki; Selenophosphate_synthetase_1; -.
DR GenomeRNAi; 22929; -.
DR Pharos; P49903; Tbio.
DR PRO; PR:P49903; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P49903; protein.
DR Bgee; ENSG00000086475; Expressed in ventricular zone and 200 other tissues.
DR ExpressionAtlas; P49903; baseline and differential.
DR Genevisible; P49903; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; TAS:ProtInc.
DR GO; GO:0005525; F:GTP binding; TAS:ProtInc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0004756; F:selenide, water dikinase activity; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0036211; P:protein modification process; TAS:ProtInc.
DR GO; GO:0016260; P:selenocysteine biosynthetic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Cell membrane; Cytoplasm; Direct protein sequencing; Kinase; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Nucleus; Reference proteome;
KW Selenium; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..392
FT /note="Selenide, water dikinase 1"
FT /id="PRO_0000127648"
FT ACT_SITE 31
FT /evidence="ECO:0000255"
FT BINDING 32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:19477186,
FT ECO:0007744|PDB:3FD5, ECO:0007744|PDB:3FD6"
FT BINDING 67..69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:19477186,
FT ECO:0007744|PDB:3FD5, ECO:0007744|PDB:3FD6"
FT BINDING 69
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:19477186,
FT ECO:0007744|PDB:3FD6"
FT BINDING 87
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:19477186,
FT ECO:0007744|PDB:3FD5"
FT BINDING 110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:19477186,
FT ECO:0007744|PDB:3FD5, ECO:0007744|PDB:3FD6"
FT BINDING 110
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:19477186,
FT ECO:0007744|PDB:3FD6"
FT BINDING 161..164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:19477186,
FT ECO:0007744|PDB:3FD5, ECO:0007744|PDB:3FD6"
FT BINDING 265
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:19477186,
FT ECO:0007744|PDB:3FD6"
FT SITE 32
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P16456"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT VAR_SEQ 1..67
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:20471958"
FT /id="VSP_046701"
FT VAR_SEQ 251..321
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:20471958"
FT /id="VSP_046702"
FT VAR_SEQ 322..392
FT /note="GGLLICLPREQAARFCAEIKSPKYGEGHQAWIIGIVEKGNRTARIIDKPRII
FT EVAPQVATQNVNPTPGATS -> DVQ (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:20471958"
FT /id="VSP_047451"
FT MUTAGEN 85
FT /note="T->A: Strongly reduced ADP hydrolysis."
FT /evidence="ECO:0000269|PubMed:19477186"
FT MUTAGEN 268
FT /note="G->C: No change in ATP-binding."
FT /evidence="ECO:0000269|PubMed:7665581"
FT MUTAGEN 270
FT /note="G->R: No change in ATP-binding."
FT /evidence="ECO:0000269|PubMed:7665581"
FT MUTAGEN 273
FT /note="G->A,D,V: Loss of ATP-binding."
FT /evidence="ECO:0000269|PubMed:7665581"
FT MUTAGEN 274
FT /note="H->N: Reduced ATP-binding."
FT /evidence="ECO:0000269|PubMed:7665581"
FT MUTAGEN 274
FT /note="H->Y: Increased ATP-binding."
FT /evidence="ECO:0000269|PubMed:7665581"
FT CONFLICT 260
FT /note="A -> T (in Ref. 1; AAA87567)"
FT /evidence="ECO:0000305"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:3FD5"
FT HELIX 20..23
FT /evidence="ECO:0007829|PDB:3FD5"
FT HELIX 35..42
FT /evidence="ECO:0007829|PDB:3FD5"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:3FD5"
FT STRAND 81..89
FT /evidence="ECO:0007829|PDB:3FD5"
FT HELIX 96..113
FT /evidence="ECO:0007829|PDB:3FD5"
FT STRAND 120..129
FT /evidence="ECO:0007829|PDB:3FD5"
FT HELIX 134..154
FT /evidence="ECO:0007829|PDB:3FD5"
FT STRAND 159..169
FT /evidence="ECO:0007829|PDB:3FD5"
FT STRAND 171..180
FT /evidence="ECO:0007829|PDB:3FD5"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:3FD5"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:3FD5"
FT HELIX 205..213
FT /evidence="ECO:0007829|PDB:3FD5"
FT HELIX 218..224
FT /evidence="ECO:0007829|PDB:3FD5"
FT HELIX 230..245
FT /evidence="ECO:0007829|PDB:3FD5"
FT HELIX 249..257
FT /evidence="ECO:0007829|PDB:3FD5"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:3FD5"
FT HELIX 270..279
FT /evidence="ECO:0007829|PDB:3FD5"
FT STRAND 283..296
FT /evidence="ECO:0007829|PDB:3FD5"
FT HELIX 299..305
FT /evidence="ECO:0007829|PDB:3FD5"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:3FD5"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:3FD5"
FT STRAND 324..328
FT /evidence="ECO:0007829|PDB:3FD5"
FT HELIX 330..341
FT /evidence="ECO:0007829|PDB:3FD5"
FT STRAND 352..362
FT /evidence="ECO:0007829|PDB:3FD5"
FT STRAND 364..375
FT /evidence="ECO:0007829|PDB:3FD5"
SQ SEQUENCE 392 AA; 42911 MW; E9636E38146D926D CRC64;
MSTRESFNPE SYELDKSFRL TRFTELKGTG CKVPQDVLQK LLESLQENHF QEDEQFLGAV
MPRLGIGMDT CVIPLRHGGL SLVQTTDYIY PIVDDPYMMG RIACANVLSD LYAMGVTECD
NMLMLLGVSN KMTDRERDKV MPLIIQGFKD AAEEAGTSVT GGQTVLNPWI VLGGVATTVC
QPNEFIMPDN AVPGDVLVLT KPLGTQVAVA VHQWLDIPEK WNKIKLVVTQ EDVELAYQEA
MMNMARLNRT AAGLMHTFNA HAATDITGFG ILGHAQNLAK QQRNEVSFVI HNLPVLAKMA
AVSKACGNMF GLMHGTCPET SGGLLICLPR EQAARFCAEI KSPKYGEGHQ AWIIGIVEKG
NRTARIIDKP RIIEVAPQVA TQNVNPTPGA TS
