SPS2_MOUSE
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 03-AUG-2022, entry version 152.
DE RecName: Full=Selenide, water dikinase 2;
DE EC=2.7.9.3 {ECO:0000250|UniProtKB:P49903};
DE AltName: Full=Selenium donor protein 2;
DE AltName: Full=Selenophosphate synthase 2;
GN Name=Sephs2; Synonyms=Sps2;
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 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, Spleen,
RC 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).
CC -!- FUNCTION: Synthesizes selenophosphate from selenide and ATP.
CC {ECO:0000250|UniProtKB:P49903}.
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:0000250|UniProtKB:P49903};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P49903};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P49903};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P49903}.
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; 1.
DR STRING; 10090.ENSMUSP00000081009; -.
DR iPTMnet; P97364; -.
DR PhosphoSitePlus; P97364; -.
DR REPRODUCTION-2DPAGE; IPI00124181; -.
DR EPD; P97364; -.
DR jPOST; P97364; -.
DR MaxQB; P97364; -.
DR PaxDb; P97364; -.
DR PeptideAtlas; P97364; -.
DR PRIDE; P97364; -.
DR ProteomicsDB; 261633; -.
DR Antibodypedia; 43619; 112 antibodies from 22 providers.
DR DNASU; 20768; -.
DR Ensembl; ENSMUST00000082428; ENSMUSP00000081009; ENSMUSG00000049091.
DR GeneID; 20768; -.
DR KEGG; mmu:20768; -.
DR UCSC; uc009jux.2; mouse.
DR CTD; 22928; -.
DR MGI; MGI:108388; Sephs2.
DR VEuPathDB; HostDB:ENSMUSG00000049091; -.
DR eggNOG; KOG3939; Eukaryota.
DR GeneTree; ENSGT00390000000950; -.
DR HOGENOM; CLU_032859_1_0_1; -.
DR InParanoid; P97364; -.
DR OMA; RWNKINM; -.
DR OrthoDB; 1166567at2759; -.
DR PhylomeDB; P97364; -.
DR TreeFam; TF313811; -.
DR BioCyc; MetaCyc:MON-14949; -.
DR BRENDA; 2.7.9.3; 3474.
DR Reactome; R-MMU-2408557; Selenocysteine synthesis.
DR BioGRID-ORCS; 20768; 23 hits in 73 CRISPR screens.
DR ChiTaRS; Sephs2; mouse.
DR PRO; PR:P97364; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P97364; protein.
DR Bgee; ENSMUSG00000049091; Expressed in left lobe of liver and 266 other tissues.
DR Genevisible; P97364; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004756; F:selenide, water dikinase activity; IDA:MGI.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0001887; P:selenium compound metabolic process; IDA:MGI.
DR GO; GO:0016260; P:selenocysteine biosynthetic process; IMP:MGI.
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 SUPFAM; SSF55326; SSF55326; 1.
DR SUPFAM; SSF56042; SSF56042; 1.
DR TIGRFAMs; TIGR00476; selD; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Direct protein sequencing; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW 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..113
FT /note="Disordered"
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
