SPS1_MOUSE
ID SPS1_MOUSE Reviewed; 392 AA.
AC Q8BH69;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Selenide, water dikinase 1;
DE EC=2.7.9.3 {ECO:0000250|UniProtKB:P49903};
DE AltName: Full=Selenium donor protein 1;
DE AltName: Full=Selenophosphate synthase 1;
GN Name=Sephs1; Synonyms=Sps1;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, 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).
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 monomer. {ECO:0000250|UniProtKB:P49903};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P49903}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P49903};
CC Peripheral membrane protein {ECO:0000305}. Nucleus membrane
CC {ECO:0000250|UniProtKB:P49903}; Peripheral membrane protein
CC {ECO:0000305}.
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 probable, it is possible Cys-31 is the active site.
CC {ECO:0000305}.
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DR EMBL; AK044971; BAC32163.1; -; mRNA.
DR EMBL; AK053638; BAC35456.1; -; mRNA.
DR CCDS; CCDS15659.1; -.
DR RefSeq; NP_780609.4; NM_175400.6.
DR RefSeq; XP_006497372.1; XM_006497309.2.
DR RefSeq; XP_017170393.1; XM_017314904.1.
DR AlphaFoldDB; Q8BH69; -.
DR SMR; Q8BH69; -.
DR BioGRID; 224546; 6.
DR IntAct; Q8BH69; 1.
DR STRING; 10090.ENSMUSP00000027973; -.
DR iPTMnet; Q8BH69; -.
DR PhosphoSitePlus; Q8BH69; -.
DR EPD; Q8BH69; -.
DR jPOST; Q8BH69; -.
DR MaxQB; Q8BH69; -.
DR PaxDb; Q8BH69; -.
DR PeptideAtlas; Q8BH69; -.
DR PRIDE; Q8BH69; -.
DR ProteomicsDB; 258731; -.
DR Antibodypedia; 24810; 195 antibodies from 30 providers.
DR DNASU; 109079; -.
DR Ensembl; ENSMUST00000027973; ENSMUSP00000027973; ENSMUSG00000026662.
DR Ensembl; ENSMUST00000115019; ENSMUSP00000110671; ENSMUSG00000026662.
DR GeneID; 109079; -.
DR KEGG; mmu:109079; -.
DR UCSC; uc008ifb.1; mouse.
DR CTD; 22929; -.
DR MGI; MGI:1923580; Sephs1.
DR VEuPathDB; HostDB:ENSMUSG00000026662; -.
DR eggNOG; KOG3939; Eukaryota.
DR GeneTree; ENSGT00390000000950; -.
DR HOGENOM; CLU_032859_1_0_1; -.
DR InParanoid; Q8BH69; -.
DR OMA; DNEPKYG; -.
DR OrthoDB; 1166567at2759; -.
DR PhylomeDB; Q8BH69; -.
DR TreeFam; TF313811; -.
DR BRENDA; 2.7.9.3; 3474.
DR BioGRID-ORCS; 109079; 17 hits in 74 CRISPR screens.
DR ChiTaRS; Sephs1; mouse.
DR PRO; PR:Q8BH69; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8BH69; protein.
DR Bgee; ENSMUSG00000026662; Expressed in floor plate of midbrain and 225 other tissues.
DR Genevisible; Q8BH69; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS: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: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 Acetylation; ATP-binding; Cell membrane; Kinase; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Nucleus; Reference proteome; Selenium;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P49903"
FT CHAIN 2..392
FT /note="Selenide, water dikinase 1"
FT /id="PRO_0000127649"
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:0000250|UniProtKB:P49903"
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:0000250|UniProtKB:P49903"
FT BINDING 69
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P49903"
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:0000250|UniProtKB:P49903"
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:0000250|UniProtKB:P49903"
FT BINDING 110
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P49903"
FT BINDING 161..164
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 265
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P49903"
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:0000250|UniProtKB:P49903"
SQ SEQUENCE 392 AA; 42907 MW; 46627E6ADB3D593C CRC64;
MSTRESFNPE TYELDKSFRL TRFTELKGTG CKVPQDVLQK LLESLQENHF QEDEQFLGAV
MPRLGIGMDT CVIPLRHGGL SLVQTTDYIY PIVDDPYMMG RIACANVLSD LYAMGVTECD
NMLMLLGVSN KMTDRERDKV IPLIIQGFKD 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
