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P63300 (SELW_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Selenoprotein W

Short name=SelW
Gene names
Name:Sepw1
Synonyms:Selw
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length88 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role as a glutathione (GSH)-dependent antioxidant. May be involved in a redox-related process. May play a role in the myopathies of selenium deficiency. Ref.2 Ref.3 Ref.7

Subunit structure

Interacts with DPYSL2, PRDX1, YWHAB, YWHAG, HSP70 and HSP90. Ref.3 Ref.8

Subcellular location

Cytoplasm.

Tissue specificity

In the embryo, expressed in the developing nervous system and in mesoderm-derived tissues such as heart and limbs. In the adult, predominantly expressed in brain, skeletal muscle and heart. Ref.3 Ref.7

Developmental stage

Expression is first detected in the newly implanted embryo. Levels increase gradually during embryonic development with a steady increase during the second week and a dramatic increase by the end of gestation. Expression increases gradually in proliferating myotubes but is low in terminally differentiated myobutubes. Ref.7

Induction

Down-regulated by hydrogen peroxide. Increased levels are detected after treatment with L-buthionine sulfoxide (BSO) before exposure to hydrogen peroxide. Ref.7

Sequence similarities

Belongs to the SelWTH family. SELW subfamily.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversitySelenocysteine
   DomainRedox-active center
   Molecular functionAntioxidant
   PTMGlutathionylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

oxidation-reduction process

Traceable author statement Ref.2. Source: GOC

   Cellular_componentcytoplasm

Traceable author statement Ref.2. Source: UniProtKB

plasma membrane

Traceable author statement Ref.2. Source: UniProtKB

   Molecular_functionantioxidant activity

Inferred from electronic annotation. Source: UniProtKB-KW

oxidoreductase activity

Traceable author statement Ref.2. Source: UniProtKB

selenium binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 8887Selenoprotein W
PRO_0000097680

Amino acid modifications

Non-standard residue131Selenocysteine
Modified residue371S-glutathionyl cysteine By similarity
Cross-link10 ↔ 13Cysteinyl-selenocysteine (Cys-Sec); redox-active By similarity

Experimental info

Mutagenesis101C → S: Disrupts redox reaction.
Mutagenesis131U → C: Increased sensitivity to hydrogen peroxide-induced toxicity. Ref.2
Mutagenesis131U → S: Impairs protection against hydrogen peroxide-induced toxicity. Ref.2
Mutagenesis371C → S: Impairs protection against hydrogen peroxide-induced toxicity. Ref.2

Secondary structure

.............. 88
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P63300 [UniParc].

Last modified February 26, 2008. Version 3.
Checksum: 03E297B668D3D7E0

FASTA889,687
        10         20         30         40         50         60 
MALAVRVVYC GAUGYKPKYL QLKEKLEHEF PGCLDICGEG TPQVTGFFEV TVAGKLVHSK 

        70         80 
KRGDGYVDTE SKFRKLVTAI KAALAQCQ 

« Hide

References

« Hide 'large scale' references
[1]"Conserved features of selenocysteine insertion sequence (SECIS) elements in selenoprotein W cDNAs from five species."
Gu Q.-P., Beilstein M.A., Vendeland S.C., Lugade A., Ream W., Whanger P.D.
Gene 193:187-196(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Skeletal muscle.
[2]"Selenoprotein W is a glutathione-dependent antioxidant in vivo."
Jeong D., Kim T.S., Chung Y.W., Lee B.J., Kim I.Y.
FEBS Lett. 517:225-228(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF SEC-13 AND CYS-37.
Tissue: Brain.
[3]"SelT, SelW, SelH, and Rdx12: genomics and molecular insights into the functions of selenoproteins of a novel thioredoxin-like family."
Dikiy A., Novoselov S.V., Fomenko D.E., Sengupta A., Carlson B.A., Cerny R.L., Ginalski K., Grishin N.V., Hatfield D.L., Gladyshev V.N.
Biochemistry 46:6871-6882(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH YWHAB; YWHAG; DPYSL2; PRDX1; HSP70 AND HSP90, TISSUE SPECIFICITY.
Tissue: Brain.
[4]Bellingham J., Gregory-Evans C.Y.
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6J.
Tissue: Fetus.
[5]"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: Kidney and Stomach.
[6]"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].
Strain: C57BL/6.
Tissue: Brain.
[7]"Selenoprotein W during development and oxidative stress."
Loflin J., Lopez N., Whanger P.D., Kioussi C.
J. Inorg. Biochem. 100:1679-1684(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, INDUCTION.
[8]"Solution structure of selenoprotein W and NMR analysis of its interaction with 14-3-3 proteins."
Aachmann F.L., Fomenko D.E., Soragni A., Gladyshev V.N., Dikiy A.
J. Biol. Chem. 282:37036-37044(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF MUTANT SER-10/CYS-13, INTERACTION WITH YWHAB AND YWHAG.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U67890 mRNA. Translation: AAC53317.1.
AF241527 mRNA. Translation: AAF64481.1.
AF015284 mRNA. Translation: AAB69860.1.
AK002870 mRNA. Translation: BAC55247.1.
AK028124 mRNA. Translation: BAC55256.1.
BC052719 mRNA. Translation: AAH52719.2.
CCDSCCDS39778.1.
RefSeqNP_033182.1. NM_009156.2.
UniGeneMm.42829.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2NPBNMR-A1-88[»]
ProteinModelPortalP63300.
SMRP63300. Positions 1-88.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000038943.

PTM databases

PhosphoSiteP63300.

Proteomic databases

PaxDbP63300.
PRIDEP63300.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000044355; ENSMUSP00000038943; ENSMUSG00000041571.
GeneID20364.
KEGGmmu:20364.
UCSCuc009fgp.1. mouse.

Organism-specific databases

CTD6415.
MGIMGI:1100878. Sepw1.

Phylogenomic databases

eggNOGNOG84296.
GeneTreeENSGT00530000064138.
HOGENOMHOG000286957.
HOVERGENHBG059755.
InParanoidP63300.
OMAKKRGDGY.
OrthoDBEOG7QRQXF.
PhylomeDBP63300.
TreeFamTF326627.

Gene expression databases

BgeeP63300.
CleanExMM_SEPW1.
GenevestigatorP63300.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR011893. Selenoprotein_Rdx-typ.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF10262. Rdx. 1 hit.
[Graphical view]
SUPFAMSSF52833. SSF52833. 1 hit.
TIGRFAMsTIGR02174. CXXU_selWTH. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP63300.
NextBio298265.
PROP63300.
SOURCESearch...

Entry information

Entry nameSELW_MOUSE
AccessionPrimary (citable) accession number: P63300
Secondary accession number(s): O35965, P49904, Q9JIC2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: February 26, 2008
Last modified: July 9, 2014
This is version 81 of the entry and version 3 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

MGD cross-references

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