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Q6P6M7 (SPCS_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
O-phosphoseryl-tRNA(Sec) selenium transferase

EC=2.9.1.2
Alternative name(s):
Selenocysteine synthase
Short name=Sec synthase
Selenocysteinyl-tRNA(Sec) synthase
Sep-tRNA:Sec-tRNA synthase
Short name=SepSecS
UGA suppressor tRNA-associated protein
Gene names
Name:Sepsecs
Synonyms:D5Ertd135e
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length504 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis By similarity.

Catalytic activity

O-phospho-L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + phosphate.

Cofactor

Pyridoxal phosphate. Ref.3

Pathway

Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (archaeal/eukaryal route): step 2/2.

Subunit structure

Homotetramer formed by a catalytic dimer and a non-catalytic dimer serving as a binding platform that orients tRNASec for catalysis. Ref.3

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the SepSecS family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 504504O-phosphoseryl-tRNA(Sec) selenium transferase
PRO_0000219876

Regions

Region1 – 4444Tetramerization
Region96 – 10611Phosphate loop (P-loop)

Sites

Binding site751PLP
Binding site971Substrate
Binding site981Substrate
Binding site1051Substrate
Binding site2711tRNA variable arm By similarity
Binding site3131Substrate
Binding site3981tRNA discriminator base By similarity
Site741May act as a substrate filter by repelling compounds with a negatively charged alpha-carboxylate

Amino acid modifications

Modified residue2841N6-(pyridoxal phosphate)lysine

Experimental info

Mutagenesis1051Q → E: 50% of wild-type activity. Ref.3
Mutagenesis3131R → E: Virtually inactive. Ref.3
Mutagenesis3131R → S: 30% of wild-type activity. Ref.3
Sequence conflict3001E → D in AAH62133. Ref.2

Secondary structure

.................................................................... 504
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q6P6M7 [UniParc].

Last modified March 29, 2005. Version 2.
Checksum: E106674A0C80D98B

FASTA50455,326
        10         20         30         40         50         60 
MNPESFAAGE RRVSPAYVRQ GCEARRAHEH LIRLLLEQGK CPEDGWDEST LELFLHELAV 

        70         80         90        100        110        120 
MDSNNFLGNC GVGEREGRVA SALVARRHYR FIHGIGRSGD ISAVQPKAAG SSLLNKITNS 

       130        140        150        160        170        180 
LVLNVIKLAG VHSVASCFVV PMATGMSLTL CFLTLRHKRP KAKYIIWPRI DQKSCFKSMV 

       190        200        210        220        230        240 
TAGFEPVVIE NVLEGDELRT DLKAVEAKIQ ELGPEHILCL HSTTACFAPR VPDRLEELAV 

       250        260        270        280        290        300 
ICANYDIPHV VNNAYGLQSS KCMHLIQQGA RVGRIDAFVQ SLDKNFMVPV GGAIIAGFNE 

       310        320        330        340        350        360 
PFIQDISKMY PGRASASPSL DVLITLLSLG CSGYRKLLKE RKEMFVYLST QLKKLAEAHN 

       370        380        390        400        410        420 
ERLLQTPHNP ISLAMTLKTI DGHHDKAVTQ LGSMLFTRQV SGARAVPLGN VQTVSGHTFR 

       430        440        450        460        470        480 
GFMSHADNYP CAYLNAAAAI GMKMQDVDLF IKRLDKCLNI VRKEQTRASV VSGADRNKAE 

       490        500 
DADIEEMALK LDDVLGDVGQ GPAL 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Cecum.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Limb.
[3]"Structure and catalytic mechanism of eukaryotic selenocysteine synthase."
Ganichkin O.M., Xu X.M., Carlson B.A., Mix H., Hatfield D.L., Gladyshev V.N., Wahl M.C.
J. Biol. Chem. 283:5849-5865(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 19-468 IN COMPLEX WITH PYRIDOXAL PHOSPHATE, SUBUNIT, SUBSTRATE-BINDING SITES, COFACTOR, MUTAGENESIS OF GLN-105 AND ARG-313.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK033654 mRNA. Translation: BAC28410.1.
BC062133 mRNA. Translation: AAH62133.1.
RefSeqNP_766078.1. NM_172490.3.
UniGeneMm.244719.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3BC8X-ray1.65A19-468[»]
3BCAX-ray2.25A19-468[»]
3BCBX-ray1.85A19-468[»]
ProteinModelPortalQ6P6M7.
SMRQ6P6M7. Positions 23-467.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-1857229.
STRING10090.ENSMUSP00000031069.

PTM databases

PhosphoSiteQ6P6M7.

Proteomic databases

PaxDbQ6P6M7.
PRIDEQ6P6M7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031069; ENSMUSP00000031069; ENSMUSG00000029173.
GeneID211006.
KEGGmmu:211006.
UCSCuc008xko.1. mouse.

Organism-specific databases

CTD51091.
MGIMGI:1098791. Sepsecs.

Phylogenomic databases

eggNOGCOG0076.
GeneTreeENSGT00390000007332.
HOGENOMHOG000254245.
HOVERGENHBG061363.
InParanoidQ6P6M7.
KOK03341.
OMANPISMAM.
OrthoDBEOG71G9TX.
TreeFamTF314381.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14964.
UniPathwayUPA00906; UER00898.

Gene expression databases

ArrayExpressQ6P6M7.
BgeeQ6P6M7.
GenevestigatorQ6P6M7.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
InterProIPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR019872. Sec-tRNA_Se_transferase.
IPR008829. SLA/LP_auto_ag.
[Graphical view]
PANTHERPTHR12944. PTHR12944. 1 hit.
PfamPF05889. SLA_LP_auto_ag. 1 hit.
[Graphical view]
PIRSFPIRSF017689. SepSecS. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR03531. selenium_SpcS. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ6P6M7.
NextBio373121.
PROQ6P6M7.
SOURCESearch...

Entry information

Entry nameSPCS_MOUSE
AccessionPrimary (citable) accession number: Q6P6M7
Secondary accession number(s): Q8BZS6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: February 19, 2014
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot