ID   SPS2_MOUSE              Reviewed;         452 AA.
AC   P97364; Q3TGI4; Q80ZY9;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 3.
DT   02-SEP-2026, entry version 170.
DE   RecName: Full=Selenide, water dikinase 2;
DE            EC=2.7.9.3 {ECO:0000269|PubMed:17346238, ECO:0000305|PubMed:17194211};
DE   AltName: Full=Selenium donor protein 2;
DE   AltName: Full=Selenophosphate synthase 2 {ECO:0000303|PubMed:17346238};
GN   Name=Sephs2; Synonyms=Sps2 {ECO:0000303|PubMed:17346238};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7588067; DOI=10.1242/dev.121.10.3335;
RA   Guimaraes M.J., Bazan J.F., Zlotnik A., Wiles M.V., Grimaldi J.C., Lee F.,
RA   McClanahan T.;
RT   "A new approach to the study of haematopoietic development in the yolk sac
RT   and embryoid bodies.";
RL   Development 121:3335-3346(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8986768; DOI=10.1073/pnas.93.26.15086;
RA   Guimaraes M.J., Peterson D., Vicari A., Cocks B.G., Copeland N.G.,
RA   Gilbert D.J., Jenkins N.A., Ferrick D.A., Kastelein R., Bazan J.F.,
RA   Zlotnik A.;
RT   "Identification of a novel selD homolog from eukaryotes, bacteria, and
RT   archaea: is there an autoregulatory mechanism in selenocysteine
RT   metabolism?";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:15086-15091(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Amnion, Kidney, and Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver, and Salivary gland;
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   [5]
RP   PROTEIN SEQUENCE OF 353-362, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [6]
RP   FUNCTION, AND COFACTOR.
RX   PubMed=10515607; DOI=10.1016/s1016-8478(23)13563-1;
RA   Kim T.S., Yu M.H., Chung Y.W., Kim J., Choi E.J., Ahn K., Kim I.Y.;
RT   "Fetal mouse selenophosphate synthetase 2 (SPS2): biological activities of
RT   mutant forms in Escherichia coli.";
RL   Mol. Cells 9:422-428(1999).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [8]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=17194211; DOI=10.1371/journal.pbio.0050004;
RA   Xu X.M., Carlson B.A., Mix H., Zhang Y., Saira K., Glass R.S., Berry M.J.,
RA   Gladyshev V.N., Hatfield D.L.;
RT   "Biosynthesis of selenocysteine on its tRNA in eukaryotes.";
RL   PLoS Biol. 5:e4-e4(2007).
RN   [9]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=17346238; DOI=10.1042/bj20070165;
RA   Xu X.M., Carlson B.A., Irons R., Mix H., Zhong N., Gladyshev V.N.,
RA   Hatfield D.L.;
RT   "Selenophosphate synthetase 2 is essential for selenoprotein
RT   biosynthesis.";
RL   Biochem. J. 404:115-120(2007).
CC   -!- FUNCTION: Selenophosphate synthase that generates the selenium donor
CC       for selenocysteine biosynthesis by catalyzing formation of
CC       selenophosphate from selenide and ATP. {ECO:0000269|PubMed:10515607,
CC       ECO:0000269|PubMed:17194211, ECO:0000269|PubMed:17346238}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hydrogenselenide + ATP + H2O = selenophosphate + AMP +
CC         phosphate + 2 H(+); 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:17346238, ECO:0000305|PubMed:17194211};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18738;
CC         Evidence={ECO:0000269|PubMed:17346238, ECO:0000305|PubMed:17194211};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:10515607};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P49903};
CC   -!- SUBUNIT: Homodimer (By similarity). Component of a complex composed of
CC       SEPHS1, SEPHS2, SEPSECS and TRNAU1AP (By similarity).
CC       {ECO:0000250|UniProtKB:P49903, ECO:0000250|UniProtKB:Q99611}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99611}.
CC   -!- PTM: Truncated SEPHS2 proteins produced by failed UGA/Sec decoding are
CC       ubiquitinated by the CRL2(KLHDC3) complex, which recognizes the glycine
CC       (Gly) at the C-terminus of truncated SEPHS2 proteins.
CC       {ECO:0000250|UniProtKB:Q99611}.
CC   -!- SIMILARITY: Belongs to the selenophosphate synthase 1 family. Class I
CC       subfamily. {ECO:0000305}.
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DR   EMBL; U43285; AAC53024.2; -; mRNA.
DR   EMBL; AK149516; BAE28931.1; -; mRNA.
DR   EMBL; AK168722; BAE40564.1; -; mRNA.
DR   EMBL; AK168965; BAE40770.1; -; mRNA.
DR   EMBL; BC016508; AAH16508.1; -; mRNA.
DR   EMBL; BC028966; AAH28966.1; -; mRNA.
DR   EMBL; BC043334; AAH43334.2; -; mRNA.
DR   CCDS; CCDS21863.1; -.
DR   RefSeq; NP_033292.2; NM_009266.3.
DR   BioGRID; 203484; 2.
DR   FunCoup; P97364; 234.
DR   STRING; 10090.ENSMUSP00000081009; -.
DR   iPTMnet; P97364; -.
DR   PhosphoSitePlus; P97364; -.
DR   SwissPalm; P97364; -.
DR   REPRODUCTION-2DPAGE; IPI00124181; -.
DR   jPOST; P97364; -.
DR   PaxDb; 10090-ENSMUSP00000081009; -.
DR   PeptideAtlas; P97364; -.
DR   ProteomicsDB; 261633; -.
DR   Pumba; P97364; -.
DR   Antibodypedia; 43619; 114 antibodies from 22 providers.
DR   DNASU; 20768; -.
DR   GeneID; 20768; -.
DR   KEGG; mmu:20768; -.
DR   UCSC; uc009jux.2; mouse.
DR   AGR; MGI:108388; -.
DR   CTD; 22928; -.
DR   MGI; MGI:108388; Sephs2.
DR   VEuPathDB; HostDB:ENSMUSG00000049091; -.
DR   eggNOG; KOG3939; Eukaryota.
DR   HOGENOM; CLU_032859_1_0_1; -.
DR   InParanoid; P97364; -.
DR   OMA; RWNKINM; -.
DR   OrthoDB; 409395at2759; -.
DR   PhylomeDB; P97364; -.
DR   BioCyc; MetaCyc:MONOMER-14949; -.
DR   BRENDA; 2.7.9.3; 3474.
DR   Reactome; R-MMU-2408557; Selenocysteine synthesis.
DR   BioGRID-ORCS; 20768; 23 hits in 78 CRISPR screens.
DR   PRO; PR:P97364; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; P97364; protein.
DR   Bgee; ENSMUSG00000049091; Expressed in left lobe of liver and 269 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004756; F:selenide, water dikinase activity; IDA:UniProtKB.
DR   GO; GO:0016260; P:L-selenocysteine biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0001887; P:selenium compound metabolic process; IDA:MGI.
DR   CDD; cd02195; SelD; 1.
DR   FunFam; 3.90.650.10:FF:000003; Selenide, water dikinase 1; 1.
DR   FunFam; 3.30.1330.10:FF:000018; selenide, water dikinase 2; 1.
DR   Gene3D; 3.90.650.10; PurM-like C-terminal domain; 1.
DR   Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 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   NCBIfam; TIGR00476; selD; 1.
DR   PANTHER; PTHR10256; SELENIDE, WATER DIKINASE; 1.
DR   PANTHER; PTHR10256:SF1; SELENIDE, WATER DIKINASE 2; 1.
DR   Pfam; PF00586; AIRS; 1.
DR   Pfam; PF02769; AIRS_C; 1.
DR   SUPFAM; SSF56042; PurM C-terminal domain-like; 1.
DR   SUPFAM; SSF55326; PurM N-terminal domain-like; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cytoplasm; Direct protein sequencing; Kinase;
KW   Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Selenium; Selenocysteine; Transferase; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q99611"
FT   CHAIN           2..452
FT                   /note="Selenide, water dikinase 2"
FT                   /id="PRO_0000127651"
FT   REGION          86..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..105
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        63
FT                   /evidence="ECO:0000255"
FT   BINDING         66
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:0000250|UniProtKB:P49903"
FT   BINDING         121..123
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:0000250|UniProtKB:P49903"
FT   BINDING         123
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P49903"
FT   BINDING         141
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:0000250|UniProtKB:P49903"
FT   BINDING         164
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:0000250|UniProtKB:P49903"
FT   BINDING         164
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P49903"
FT   BINDING         215..218
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P49903"
FT   BINDING         319
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P49903"
FT   SITE            66
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:P16456"
FT   NON_STD         63
FT                   /note="Selenocysteine"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99611"
FT   MOD_RES         49
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   452 AA;  47834 MW;  CF82585D01ABE3BF CRC64;
     MAEAAAAGAS GETMAALVAA EGSLGPAGWS AGRSFSNYRP FEPQTLGFSP SWRLTSFSGM
     KGUGCKVPQE TLLKLLEGLT RPALQPPLTS GLVGGQEETV QEGGLSTRPG PGSAFPSLSI
     GMDSCVIPLR HGGLSLVQTT DFFYPLVEDP YMMGRIACAN VLSDLYAMGI TECDNMLMLL
     SVSQSMSEKE REKVTPLMIK GFRDAAEEGG TAVTGGQTVV NPWIIIGGVA TVVCQQNEFI
     MPDSAVVGDV LVLTKPLGTQ VAANAHQWLD NPEKWNKIKM VVSREEVELA YQEAMFNMAT
     LNRTAAGLMH TFNAHAATDI TGFGILGHSQ NLAKQQKNEV SFVIHNLPII AKMAAISKAS
     GRFGLLQGTS AETSGGLLIC LPREQAARFC SEIKSSKYGE GHQAWIVGIV EKGNRTARII
     DKPRVIEVLP RGASAAAAAA PDNSNAASEP SS
//