ID SPS1_HUMAN Reviewed; 392 AA. AC P49903; Q5T5U8; Q9BVT4; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 13-DEC-2002, sequence version 2. DT 06-MAR-2013, entry version 110. DE RecName: Full=Selenide, water dikinase 1; DE EC=2.7.9.3; 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ATP-BINDING, AND MUTAGENESIS OF RP GLY-268; GLY-270; GLY-273 AND HIS-274. RC TISSUE=Liver; RX MEDLINE=95394923; 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 [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., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., RA 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP PROTEIN SEQUENCE OF 5-16 AND 64-76, AND MASS SPECTROMETRY. RC TISSUE=Fetal brain cortex; RA Lubec G., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [6] 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., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [7] 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., RA Buerckstuemmer T., 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 [8] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ADP; MAGNESIUM RP IONS AND PHOSPHATE, SUBUNIT, ENZYME REGULATION, AND MUTAGENESIS OF RP 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 RT selenophosphate synthetase 1."; RL J. Mol. Biol. 390:747-759(2009). CC -!- FUNCTION: Synthesizes selenophosphate from selenide and ATP. CC -!- CATALYTIC ACTIVITY: ATP + selenide + H(2)O = AMP + selenophosphate CC + phosphate. CC -!- ENZYME REGULATION: Activated by phosphate ions and by potassium CC ions. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the selenophosphate synthase 1 family. CC Class II subfamily. CC -!- CAUTION: The conserved active site Cys (or selenocysteine) residue CC in position 29 is replaced by a Thr. However, as function in CC selenoprotein synthesis is proven, it is possible Cys-31 is the CC active site. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U34044; AAA87567.1; -; mRNA. DR EMBL; AL138764; CAI12907.1; -; Genomic_DNA. DR EMBL; AL355870; CAI12907.1; JOINED; Genomic_DNA. DR EMBL; AL355870; CAI14198.1; -; Genomic_DNA. DR EMBL; AL138764; CAI14198.1; JOINED; Genomic_DNA. DR EMBL; CH471072; EAW86290.1; -; Genomic_DNA. DR EMBL; BC000941; AAH00941.1; -; mRNA. DR EMBL; BC063816; AAH63816.1; -; mRNA. DR IPI; IPI00029056; -. DR RefSeq; NP_036379.2; NM_012247.4. DR UniGene; Hs.124027; -. 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 ProteinModelPortal; P49903; -. DR SMR; P49903; 6-377. DR IntAct; P49903; 8. DR STRING; P49903; -. DR PhosphoSite; P49903; -. DR DMDM; 27151792; -. DR PaxDb; P49903; -. DR PeptideAtlas; P49903; -. DR PRIDE; P49903; -. DR DNASU; 22929; -. DR Ensembl; ENST00000327347; ENSP00000367893; ENSG00000086475. DR GeneID; 22929; -. DR KEGG; hsa:22929; -. DR UCSC; uc001imh.3; human. DR CTD; 22929; -. DR GeneCards; GC10M013360; -. DR HGNC; HGNC:19685; SEPHS1. DR HPA; HPA037645; -. DR MIM; 600902; gene. DR neXtProt; NX_P49903; -. DR PharmGKB; PA134905215; -. DR eggNOG; COG0709; -. DR HOGENOM; HOG000219301; -. DR HOVERGEN; HBG001207; -. DR InParanoid; P49903; -. DR KO; K01008; -. DR OMA; PIRLTQY; -. DR OrthoDB; EOG4ZW5B4; -. DR BRENDA; 2.7.9.3; 2681. DR EvolutionaryTrace; P49903; -. DR GenomeRNAi; 22929; -. DR NextBio; 43651; -. DR ArrayExpress; P49903; -. DR Bgee; P49903; -. DR CleanEx; HS_SEPHS1; -. DR Genevestigator; P49903; -. DR GermOnline; ENSG00000086475; Homo sapiens. DR GO; GO:0005524; F:ATP binding; TAS:ProtInc. DR GO; GO:0005525; F:GTP binding; TAS:ProtInc. DR GO; GO:0004756; F:selenide, water dikinase activity; IEA:EC. DR GO; GO:0006464; P:cellular protein modification process; TAS:ProtInc. DR InterPro; IPR010918; AIR_synth_C_dom. DR InterPro; IPR000728; AIR_synth_N_dom. DR InterPro; IPR016188; PurM_N-like. DR InterPro; IPR004536; SelD. DR Pfam; PF00586; AIRS; 1. DR Pfam; PF02769; AIRS_C; 1. DR PIRSF; PIRSF036407; Selenphspht_syn; 1. DR SUPFAM; SSF56042; AIR_synth_C; 1. DR SUPFAM; SSF55326; PurM_N-like; 1. DR TIGRFAMs; TIGR00476; selD; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; KW Direct protein sequencing; Kinase; Nucleotide-binding; KW Reference proteome; Selenium; Transferase. FT CHAIN 1 392 Selenide, water dikinase 1. FT /FTId=PRO_0000127648. FT NP_BIND 67 69 ATP. FT NP_BIND 162 164 ATP; shared with dimeric partner. FT NP_BIND 267 273 ATP. FT ACT_SITE 31 31 Potential. FT BINDING 32 32 ATP. FT BINDING 87 87 ATP. FT BINDING 110 110 ATP. FT SITE 32 32 Important for catalytic activity (By FT similarity). FT MUTAGEN 85 85 T->A: Strongly reduced ADP hydrolysis. FT MUTAGEN 268 268 G->C: No change in ATP-binding. FT MUTAGEN 270 270 G->R: No change in ATP-binding. FT MUTAGEN 273 273 G->A,D,V: Loss of ATP-binding. FT MUTAGEN 274 274 H->N: Reduced ATP-binding. FT MUTAGEN 274 274 H->Y: Increased ATP-binding. FT CONFLICT 260 260 A -> T (in Ref. 1; AAA87567). FT CONFLICT 377 392 PQVATQNVNPTPGATS -> HKWPLKT (in Ref. 1; FT AAA87567). FT HELIX 10 12 FT HELIX 20 23 FT HELIX 35 42 FT STRAND 68 74 FT STRAND 81 89 FT HELIX 96 113 FT STRAND 120 129 FT HELIX 134 154 FT STRAND 159 169 FT STRAND 171 180 FT HELIX 182 184 FT STRAND 196 201 FT HELIX 205 213 FT HELIX 230 245 FT HELIX 249 257 FT STRAND 262 265 FT HELIX 270 279 FT STRAND 283 296 FT HELIX 299 305 FT TURN 306 308 FT HELIX 312 314 FT STRAND 324 328 FT HELIX 330 341 FT STRAND 352 362 FT STRAND 364 375 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 //