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 14-APR-2009, entry version 72. DE RecName: Full=Selenide, water dikinase 1; DE EC=2.7.9.3; DE AltName: Full=Selenophosphate synthetase 1; DE AltName: Full=Selenium donor protein 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 [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. CC -!- FUNCTION: Synthesizes selenophosphate from selenide and ATP. CC -!- CATALYTIC ACTIVITY: ATP + selenide + H(2)O = AMP + selenophosphate CC + phosphate. CC -!- SIMILARITY: Belongs to the selenophosphate synthetase 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; -. DR UniGene; Hs.124027; -. DR IntAct; P49903; 11. DR PeptideAtlas; P49903; -. DR PRIDE; P49903; -. DR Ensembl; ENSG00000086475; Homo sapiens. DR GeneID; 22929; -. DR KEGG; hsa:22929; -. DR GeneCards; GC10M013400; -. DR H-InvDB; HIX0008655; -. DR HGNC; HGNC:19685; SEPHS1. DR MIM; 600902; gene. DR PharmGKB; PA134905215; -. DR HOGENOM; P49903; -. DR HOVERGEN; P49903; -. DR BRENDA; 2.7.9.3; 247. DR LinkHub; P49903; -. DR NextBio; 43651; -. DR ArrayExpress; P49903; -. DR Bgee; P49903; -. DR CleanEx; HS_SEPHS1; -. 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:InterPro. DR GO; GO:0008430; F:selenium binding; IEA:UniProtKB-KW. DR GO; GO:0006464; P:protein modification process; TAS:ProtInc. DR InterPro; IPR000728; AIR_synth. DR InterPro; IPR010918; AIR_synth_C. DR InterPro; IPR004536; SelD. DR Pfam; PF00586; AIRS; 1. DR Pfam; PF02769; AIRS_C; 1. DR PIRSF; PIRSF036407; Selenphspht_syn; 1. DR TIGRFAMs; TIGR00476; selD; 1. PE 1: Evidence at protein level; KW ATP-binding; Direct protein sequencing; Kinase; Nucleotide-binding; KW Selenium; Transferase. FT CHAIN 1 392 Selenide, water dikinase 1. FT /FTId=PRO_0000127648. FT NP_BIND 268 274 ATP (Potential). FT ACT_SITE 31 31 Potential. FT SITE 32 32 Important for catalytic activity (By FT similarity). 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). 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 //