SPCS_MOUSE
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 03-AUG-2022, entry version 128.
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 iPTMnet; Q6P6M7; -.
DR PhosphoSitePlus; Q6P6M7; -.
DR EPD; Q6P6M7; -.
DR jPOST; Q6P6M7; -.
DR MaxQB; Q6P6M7; -.
DR PaxDb; Q6P6M7; -.
DR PeptideAtlas; Q6P6M7; -.
DR PRIDE; Q6P6M7; -.
DR ProteomicsDB; 261122; -.
DR Antibodypedia; 10200; 172 antibodies from 28 providers.
DR Ensembl; ENSMUST00000031069; ENSMUSP00000031069; ENSMUSG00000029173.
DR GeneID; 211006; -.
DR KEGG; mmu:211006; -.
DR UCSC; uc008xko.1; mouse.
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; HIINGAY; -.
DR OrthoDB; 680116at2759; -.
DR PhylomeDB; Q6P6M7; -.
DR TreeFam; TF314381; -.
DR BioCyc; MetaCyc:MON-14964; -.
DR UniPathway; UPA00906; UER00898.
DR BioGRID-ORCS; 211006; 27 hits in 74 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 217 other tissues.
DR ExpressionAtlas; Q6P6M7; baseline and differential.
DR Genevisible; Q6P6M7; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0005634; C:nucleus; IDA:HGNC-UCL.
DR GO; GO:0098621; F:phosphoseryl-selenocysteinyl-tRNA selenium transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IDA:HGNC-UCL.
DR GO; GO:0001514; P:selenocysteine incorporation; IDA:HGNC-UCL.
DR GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.640.10; -; 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 PANTHER; PTHR12944; PTHR12944; 1.
DR Pfam; PF05889; SepSecS; 1.
DR PIRSF; PIRSF017689; SepSecS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR03531; selenium_SpcS; 1.
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
