P63300 (SELW_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Selenoprotein W
Short name=SelW

Gene names

Name:	Sepw1
Synonyms:	Selw

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	88 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Cytoplasm
Coding sequence diversity	Selenocysteine
Domain	Redox-active center
Molecular function	Antioxidant
PTM	Glutathionylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Traceable author statement Ref.2. Source: UniProtKB plasma membrane Traceable author statement Ref.2. Source: UniProtKB
Molecular_function	antioxidant 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 88

87

Selenoprotein W

PRO_0000097680

Amino acid modifications

Non-standard residue

13

1

Selenocysteine

Modified residue

37

1

S-glutathionyl cysteine By similarity

Cross-link

10 ↔ 13

Cysteinyl-selenocysteine (Cys-Sec); redox-active By similarity

Experimental info

Mutagenesis

10

1

C → S: Disrupts redox reaction.

Mutagenesis

13

1

U → C: Increased sensitivity to hydrogen peroxide-induced toxicity. Ref.2

Mutagenesis

13

1

U → S: Impairs protection against hydrogen peroxide-induced toxicity. Ref.2

Mutagenesis

37

1

C → S: Impairs protection against hydrogen peroxide-induced toxicity. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

88

Helix Strand Turn

Details...

Beta strand

3 – 8

6

Helix

15 – 29

15

Beta strand

34 – 38

5

Beta strand

49 – 52

4

Beta strand

55 – 59

5

Turn

60 – 63

4

Helix

70 – 87

18

Sequences

	Sequence		Length	Mass (Da)
	P63300 [UniParc]. Last modified February 26, 2008. Version 3. Checksum: 03E297B668D3D7E0	FASTA	88	9,687
	10 20 30 40 50 60 MALAVRVVYC GAUGYKPKYL QLKEKLEHEF PGCLDICGEG TPQVTGFFEV TVAGKLVHSK 70 80 KRGDGYVDTE SKFRKLVTAI KAALAQCQ

References

	« Hide 'large scale' referencesShow '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. , 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.

IPI

IPI00222578.

RefSeq

NP_033182.1. NM_009156.2.

UniGene

Mm.42829.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2NPB	NMR	-	A	1-88	[»]

ProteinModelPortal

P63300.

SMR

P63300. Positions 1-88.

ModBase

Search...

Protein-protein interaction databases

STRING

10090.ENSMUSP00000038943.

PTM databases

PhosphoSite

P63300.

Proteomic databases

PaxDb

P63300.

PRIDE

P63300.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000044355; ENSMUSP00000038943; ENSMUSG00000041571.

GeneID

20364.

KEGG

mmu:20364.

UCSC

uc009fgp.1. mouse.

Organism-specific databases

CTD

6415.

MGI

MGI:1100878. Sepw1.

Phylogenomic databases

eggNOG

NOG84296.

GeneTree

ENSGT00530000064138.

HOGENOM

HOG000286957.

HOVERGEN

HBG059755.

InParanoid

P63300.

OMA

TGFFEVM.

OrthoDB

EOG4NVZN4.

Gene expression databases

Bgee

P63300.

CleanEx

MM_SEPW1.

Genevestigator

P63300.

GermOnline

ENSMUSG00000041571. Mus musculus.

Family and domain databases

Gene3D

3.40.30.10. 1 hit.

InterPro

IPR011893. Selenoprotein_Rdx-typ.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

Pfam

PF10262. Rdx. 1 hit.
[Graphical view]

SUPFAM

SSF52833. Thiordxn-like_fd. 1 hit.

TIGRFAMs

TIGR02174. CXXU_selWTH. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P63300.

NextBio

298265.

SOURCE

Search...

Entry information

Entry name

SELW_MOUSE

Accession

Primary (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:	April 3, 2013
This is version 73 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program