ID   SPCS_MOUSE              Reviewed;         504 AA.
AC   Q6P6M7; Q8BZS6;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 2.
DT   24-JAN-2024, entry version 136.
DE   RecName: Full=O-phosphoseryl-tRNA(Sec) selenium transferase;
DE            EC=2.9.1.2 {ECO:0000250|UniProtKB:Q9HD40};
DE   AltName: Full=Selenocysteine synthase;
DE            Short=Sec synthase;
DE   AltName: Full=Selenocysteinyl-tRNA(Sec) synthase;
DE   AltName: Full=Sep-tRNA:Sec-tRNA synthase;
DE            Short=SepSecS;
DE   AltName: Full=UGA suppressor tRNA-associated protein;
GN   Name=Sepsecs; Synonyms=D5Ertd135e;
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=Cecum;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Limb;
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Pancreas, 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   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 19-468 IN COMPLEX WITH PYRIDOXAL
RP   PHOSPHATE, SUBUNIT, SUBSTRATE-BINDING SITES, COFACTOR, MUTAGENESIS OF
RP   GLN-105 AND ARG-313, AND REGION.
RX   PubMed=18093968; DOI=10.1074/jbc.m709342200;
RA   Ganichkin O.M., Xu X.M., Carlson B.A., Mix H., Hatfield D.L.,
RA   Gladyshev V.N., Wahl M.C.;
RT   "Structure and catalytic mechanism of eukaryotic selenocysteine synthase.";
RL   J. Biol. Chem. 283:5849-5865(2008).
CC   -!- FUNCTION: Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl-
CC       tRNA(Sec) required for selenoprotein biosynthesis.
CC       {ECO:0000250|UniProtKB:Q9HD40}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-tRNA(Sec) + selenophosphate = L-
CC         selenocysteinyl-tRNA(Sec) + 2 phosphate; Xref=Rhea:RHEA:25041,
CC         Rhea:RHEA-COMP:9743, Rhea:RHEA-COMP:9947, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16144, ChEBI:CHEBI:43474, ChEBI:CHEBI:78551,
CC         ChEBI:CHEBI:78573; EC=2.9.1.2;
CC         Evidence={ECO:0000250|UniProtKB:Q9HD40};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:18093968};
CC   -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC       biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec)
CC       (archaeal/eukaryal route): step 2/2. {ECO:0000250|UniProtKB:Q9HD40}.
CC   -!- SUBUNIT: Homotetramer formed by a catalytic dimer and a non-catalytic
CC       dimer serving as a binding platform that orients tRNASec for catalysis.
CC       Each tetramer binds the CCA ends of two tRNAs which point to the active
CC       sites of the catalytic dimer (By similarity).
CC       {ECO:0000250|UniProtKB:Q9HD40, ECO:0000269|PubMed:18093968}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9HD40}.
CC   -!- SIMILARITY: Belongs to the SepSecS family. {ECO:0000305}.
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DR   EMBL; AK033654; BAC28410.1; -; mRNA.
DR   EMBL; BC062133; AAH62133.1; -; mRNA.
DR   CCDS; CCDS19286.1; -.
DR   RefSeq; NP_766078.1; NM_172490.3.
DR   PDB; 3BC8; X-ray; 1.65 A; A=19-468.
DR   PDB; 3BCA; X-ray; 2.25 A; A=19-468.
DR   PDB; 3BCB; X-ray; 1.85 A; A=19-468.
DR   PDBsum; 3BC8; -.
DR   PDBsum; 3BCA; -.
DR   PDBsum; 3BCB; -.
DR   AlphaFoldDB; Q6P6M7; -.
DR   SMR; Q6P6M7; -.
DR   BioGRID; 229199; 5.
DR   STRING; 10090.ENSMUSP00000031069; -.
DR   GlyGen; Q6P6M7; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q6P6M7; -.
DR   PhosphoSitePlus; Q6P6M7; -.
DR   SwissPalm; Q6P6M7; -.
DR   EPD; Q6P6M7; -.
DR   jPOST; Q6P6M7; -.
DR   MaxQB; Q6P6M7; -.
DR   PaxDb; 10090-ENSMUSP00000031069; -.
DR   PeptideAtlas; Q6P6M7; -.
DR   ProteomicsDB; 261122; -.
DR   Pumba; Q6P6M7; -.
DR   Antibodypedia; 10200; 184 antibodies from 28 providers.
DR   Ensembl; ENSMUST00000031069.13; ENSMUSP00000031069.7; ENSMUSG00000029173.13.
DR   GeneID; 211006; -.
DR   KEGG; mmu:211006; -.
DR   UCSC; uc008xko.1; mouse.
DR   AGR; MGI:1098791; -.
DR   CTD; 51091; -.
DR   MGI; MGI:1098791; Sepsecs.
DR   VEuPathDB; HostDB:ENSMUSG00000029173; -.
DR   eggNOG; KOG3843; Eukaryota.
DR   GeneTree; ENSGT00390000007332; -.
DR   HOGENOM; CLU_022508_0_0_1; -.
DR   InParanoid; Q6P6M7; -.
DR   OMA; MSHANDY; -.
DR   OrthoDB; 121300at2759; -.
DR   PhylomeDB; Q6P6M7; -.
DR   TreeFam; TF314381; -.
DR   BioCyc; MetaCyc:MONOMER-14964; -.
DR   UniPathway; UPA00906; UER00898.
DR   BioGRID-ORCS; 211006; 27 hits in 78 CRISPR screens.
DR   EvolutionaryTrace; Q6P6M7; -.
DR   PRO; PR:Q6P6M7; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q6P6M7; Protein.
DR   Bgee; ENSMUSG00000029173; Expressed in chest muscle and 220 other cell types or tissues.
DR   ExpressionAtlas; Q6P6M7; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
DR   GO; GO:0005634; C:nucleus; IDA:HGNC-UCL.
DR   GO; GO:0098621; F:O-phosphoseryl-tRNA(Sec) selenium transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000049; F:tRNA binding; IDA:HGNC-UCL.
DR   GO; GO:0001717; P:conversion of seryl-tRNAsec to selenocys-tRNAsec; IEA:InterPro.
DR   GO; GO:0001514; P:selenocysteine incorporation; IDA:HGNC-UCL.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR019872; Sec-tRNA_Se_transferase.
DR   InterPro; IPR008829; SepSecS/SepCysS.
DR   NCBIfam; TIGR03531; selenium_SpcS; 1.
DR   PANTHER; PTHR12944:SF2; O-PHOSPHOSERYL-TRNA(SEC) SELENIUM TRANSFERASE; 1.
DR   PANTHER; PTHR12944; SOLUBLE LIVER ANTIGEN/LIVER PANCREAS ANTIGEN; 1.
DR   Pfam; PF05889; SepSecS; 1.
DR   PIRSF; PIRSF017689; SepSecS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   Genevisible; Q6P6M7; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Phosphoprotein; Protein biosynthesis;
KW   Pyridoxal phosphate; Reference proteome; RNA-binding; Selenium;
KW   Transferase; tRNA-binding.
FT   CHAIN           1..504
FT                   /note="O-phosphoseryl-tRNA(Sec) selenium transferase"
FT                   /id="PRO_0000219876"
FT   REGION          1..44
FT                   /note="Tetramerization"
FT                   /evidence="ECO:0000269|PubMed:18093968"
FT   REGION          96..106
FT                   /note="Phosphate loop (P-loop)"
FT                   /evidence="ECO:0000269|PubMed:18093968"
FT   BINDING         75
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000269|PubMed:18093968"
FT   BINDING         97
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:18093968"
FT   BINDING         98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:18093968"
FT   BINDING         105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:18093968"
FT   BINDING         271
FT                   /ligand="tRNA"
FT                   /ligand_id="ChEBI:CHEBI:17843"
FT                   /ligand_part="tRNA variable arm"
FT                   /evidence="ECO:0000269|PubMed:18093968"
FT   BINDING         313
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:18093968"
FT   BINDING         398
FT                   /ligand="tRNA"
FT                   /ligand_id="ChEBI:CHEBI:17843"
FT                   /ligand_part="tRNA discriminator base"
FT                   /evidence="ECO:0000269|PubMed:18093968"
FT   BINDING         463
FT                   /ligand="tRNA"
FT                   /ligand_id="ChEBI:CHEBI:17843"
FT                   /ligand_part="tRNA acceptor arm"
FT                   /evidence="ECO:0000269|PubMed:18093968"
FT   SITE            74
FT                   /note="May act as a substrate filter by repelling compounds
FT                   with a negatively charged alpha-carboxylate"
FT                   /evidence="ECO:0000269|PubMed:18093968"
FT   MOD_RES         14
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HD40"
FT   MOD_RES         284
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000269|PubMed:18093968"
FT   MUTAGEN         105
FT                   /note="Q->E: 50% of wild-type activity."
FT                   /evidence="ECO:0000269|PubMed:18093968"
FT   MUTAGEN         313
FT                   /note="R->E: Virtually inactive."
FT                   /evidence="ECO:0000269|PubMed:18093968"
FT   MUTAGEN         313
FT                   /note="R->S: 30% of wild-type activity."
FT                   /evidence="ECO:0000269|PubMed:18093968"
FT   CONFLICT        300
FT                   /note="E -> D (in Ref. 2; AAH62133)"
FT                   /evidence="ECO:0000305"
FT   HELIX           24..38
FT                   /evidence="ECO:0007829|PDB:3BC8"
FT   HELIX           48..60
FT                   /evidence="ECO:0007829|PDB:3BC8"
FT   HELIX           63..65
FT                   /evidence="ECO:0007829|PDB:3BC8"
FT   HELIX           82..87
FT                   /evidence="ECO:0007829|PDB:3BC8"
FT   TURN            88..90
FT                   /evidence="ECO:0007829|PDB:3BC8"
FT   STRAND          95..97
FT                   /evidence="ECO:0007829|PDB:3BCB"
FT   HELIX           109..129
FT                   /evidence="ECO:0007829|PDB:3BC8"
FT   STRAND          136..142
FT                   /evidence="ECO:0007829|PDB:3BC8"
FT   HELIX           144..158
FT                   /evidence="ECO:0007829|PDB:3BC8"
FT   STRAND          164..168
FT                   /evidence="ECO:0007829|PDB:3BC8"
FT   HELIX           173..181
FT                   /evidence="ECO:0007829|PDB:3BC8"
FT   STRAND          185..189
FT                   /evidence="ECO:0007829|PDB:3BC8"
FT   STRAND          192..194
FT                   /evidence="ECO:0007829|PDB:3BC8"
FT   STRAND          197..199
FT                   /evidence="ECO:0007829|PDB:3BC8"
FT   HELIX           202..212
FT                   /evidence="ECO:0007829|PDB:3BC8"
FT   HELIX           214..216
FT                   /evidence="ECO:0007829|PDB:3BC8"
FT   STRAND          217..225
FT                   /evidence="ECO:0007829|PDB:3BC8"
FT   HELIX           235..245
FT                   /evidence="ECO:0007829|PDB:3BC8"
FT   STRAND          249..252
FT                   /evidence="ECO:0007829|PDB:3BC8"
FT   TURN            254..258
FT                   /evidence="ECO:0007829|PDB:3BC8"
FT   HELIX           260..272
FT                   /evidence="ECO:0007829|PDB:3BC8"
FT   STRAND          277..281
FT                   /evidence="ECO:0007829|PDB:3BC8"
FT   STRAND          293..298
FT                   /evidence="ECO:0007829|PDB:3BC8"
FT   HELIX           300..309
FT                   /evidence="ECO:0007829|PDB:3BC8"
FT   HELIX           317..358
FT                   /evidence="ECO:0007829|PDB:3BC8"
FT   STRAND          370..376
FT                   /evidence="ECO:0007829|PDB:3BC8"
FT   TURN            378..380
FT                   /evidence="ECO:0007829|PDB:3BC8"
FT   STRAND          381..385
FT                   /evidence="ECO:0007829|PDB:3BC8"
FT   HELIX           387..397
FT                   /evidence="ECO:0007829|PDB:3BC8"
FT   STRAND          404..406
FT                   /evidence="ECO:0007829|PDB:3BC8"
FT   STRAND          411..414
FT                   /evidence="ECO:0007829|PDB:3BC8"
FT   STRAND          417..420
FT                   /evidence="ECO:0007829|PDB:3BC8"
FT   TURN            421..425
FT                   /evidence="ECO:0007829|PDB:3BC8"
FT   STRAND          433..437
FT                   /evidence="ECO:0007829|PDB:3BC8"
FT   HELIX           444..465
FT                   /evidence="ECO:0007829|PDB:3BC8"
SQ   SEQUENCE   504 AA;  55326 MW;  E106674A0C80D98B CRC64;
     MNPESFAAGE RRVSPAYVRQ GCEARRAHEH LIRLLLEQGK CPEDGWDEST LELFLHELAV
     MDSNNFLGNC GVGEREGRVA SALVARRHYR FIHGIGRSGD ISAVQPKAAG SSLLNKITNS
     LVLNVIKLAG VHSVASCFVV PMATGMSLTL CFLTLRHKRP KAKYIIWPRI DQKSCFKSMV
     TAGFEPVVIE NVLEGDELRT DLKAVEAKIQ ELGPEHILCL HSTTACFAPR VPDRLEELAV
     ICANYDIPHV VNNAYGLQSS KCMHLIQQGA RVGRIDAFVQ SLDKNFMVPV GGAIIAGFNE
     PFIQDISKMY PGRASASPSL DVLITLLSLG CSGYRKLLKE RKEMFVYLST QLKKLAEAHN
     ERLLQTPHNP ISLAMTLKTI DGHHDKAVTQ LGSMLFTRQV SGARAVPLGN VQTVSGHTFR
     GFMSHADNYP CAYLNAAAAI GMKMQDVDLF IKRLDKCLNI VRKEQTRASV VSGADRNKAE
     DADIEEMALK LDDVLGDVGQ GPAL
//