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Protein

Methionine-R-sulfoxide reductase B1

Gene

Msrb1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases, methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residue. Acts as a regulator of actin assembly by reducing methionine (R)-sulfoxide mediated by MICALs (MICAL1, MICAL2 or MICAL3) on actin, thereby promoting filament repolymerization. Plays a role in innate immunity by reducing oxidized actin, leading to actin repolymerization in macrophages.2 Publications

Catalytic activityi

L-methionine + oxidized thioredoxin = L-methionine R-oxide + reduced thioredoxin.2 Publications

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi23 – 231ZincPROSITE-ProRule annotation
Metal bindingi26 – 261ZincPROSITE-ProRule annotation
Metal bindingi71 – 711ZincPROSITE-ProRule annotation
Metal bindingi74 – 741ZincPROSITE-ProRule annotation
Active sitei95 – 951NucleophilePROSITE-ProRule annotation

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • methionine-R-sulfoxide reductase activity Source: MGI
  • peptide-methionine (R)-S-oxide reductase activity Source: UniProtKB
  • zinc ion binding Source: HGNC

GO - Biological processi

  • actin filament polymerization Source: UniProtKB
  • innate immune response Source: UniProtKB
  • protein repair Source: HGNC
  • response to oxidative stress Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Immunity, Innate immunity

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi1.8.4.12. 3474.
ReactomeiR-MMU-5676934. Protein repair.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine-R-sulfoxide reductase B1 (EC:1.8.4.-)
Short name:
MsrB1
Alternative name(s):
Selenoprotein R
Short name:
SelR
Selenoprotein X
Short name:
SelX
Gene namesi
Name:Msrb1
Synonyms:Sepr, Sepx1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1351642. Msrb1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytoskeleton Source: UniProtKB-SubCell
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 116116Methionine-R-sulfoxide reductase B1PRO_0000140322Add
BLAST

Proteomic databases

EPDiQ9JLC3.
MaxQBiQ9JLC3.
PaxDbiQ9JLC3.

PTM databases

iPTMnetiQ9JLC3.

Expressioni

Gene expression databases

BgeeiQ9JLC3.
CleanExiMM_SEPX1.
GenevisibleiQ9JLC3. MM.

Interactioni

GO - Molecular functioni

  • actin binding Source: UniProtKB

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000099300.

Structurei

Secondary structure

1
116
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi12 – 143Combined sources
Beta strandi19 – 235Combined sources
Turni24 – 263Combined sources
Beta strandi41 – 433Combined sources
Beta strandi56 – 594Combined sources
Beta strandi61 – 633Combined sources
Beta strandi67 – 704Combined sources
Turni72 – 754Combined sources
Beta strandi79 – 813Combined sources
Turni87 – 904Combined sources
Turni98 – 1003Combined sources
Beta strandi101 – 1055Combined sources
Beta strandi107 – 1093Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KV1NMR-A1-116[»]
ProteinModelPortaliQ9JLC3.
SMRiQ9JLC3. Positions 1-116.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9JLC3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 106106MsrBPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 MsrB (methionine-R-sulfoxide reductase) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0856. Eukaryota.
COG0229. LUCA.
GeneTreeiENSGT00510000047678.
HOGENOMiHOG000243424.
HOVERGENiHBG002192.
InParanoidiQ9JLC3.
KOiK07305.
OMAiLKVSCGR.
OrthoDBiEOG7VHSZD.
PhylomeDBiQ9JLC3.
TreeFamiTF329147.

Family and domain databases

Gene3Di2.170.150.20. 1 hit.
InterProiIPR028427. Met_Sox_Rdtase.
IPR002579. Met_Sox_Rdtase_MsrB.
IPR011057. Mss4-like.
[Graphical view]
PANTHERiPTHR10173. PTHR10173. 1 hit.
PfamiPF01641. SelR. 1 hit.
[Graphical view]
SUPFAMiSSF51316. SSF51316. 1 hit.
PROSITEiPS51790. MSRB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9JLC3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFCSFFGGE VFQNHFEPGV YVCAKCSYEL FSSHSKYAHS SPWPAFTETI
60 70 80 90 100
HPDSVTKCPE KNRPEALKVS CGKCGNGLGH EFLNDGPKRG QSRFUIFSSS
110
LKFVPKGKEA AASQGH
Length:116
Mass (Da):12,788
Last modified:February 26, 2008 - v3
Checksum:i7DE4E5EE86CAA333
GO

Non-standard residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-standard residuei95 – 951Selenocysteine

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF195142 mRNA. Translation: AAF13697.1.
AK002339 mRNA. Translation: BAC55245.1.
AK002652 mRNA. Translation: BAE43148.1.
AK003112 mRNA. Translation: BAC55248.1.
AK003624 mRNA. Translation: BAC55249.1.
BC090646 mRNA. Translation: AAH90646.1.
CCDSiCCDS28495.1.
RefSeqiNP_038787.1. NM_013759.2.
UniGeneiMm.28212.

Genome annotation databases

EnsembliENSMUST00000101800; ENSMUSP00000099300; ENSMUSG00000075705.
ENSMUST00000115262; ENSMUSP00000110917; ENSMUSG00000075705.
GeneIDi27361.
KEGGimmu:27361.
UCSCiuc008ayh.1. mouse.

Keywords - Coding sequence diversityi

Selenocysteine

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF195142 mRNA. Translation: AAF13697.1.
AK002339 mRNA. Translation: BAC55245.1.
AK002652 mRNA. Translation: BAE43148.1.
AK003112 mRNA. Translation: BAC55248.1.
AK003624 mRNA. Translation: BAC55249.1.
BC090646 mRNA. Translation: AAH90646.1.
CCDSiCCDS28495.1.
RefSeqiNP_038787.1. NM_013759.2.
UniGeneiMm.28212.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KV1NMR-A1-116[»]
ProteinModelPortaliQ9JLC3.
SMRiQ9JLC3. Positions 1-116.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000099300.

PTM databases

iPTMnetiQ9JLC3.

Proteomic databases

EPDiQ9JLC3.
MaxQBiQ9JLC3.
PaxDbiQ9JLC3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000101800; ENSMUSP00000099300; ENSMUSG00000075705.
ENSMUST00000115262; ENSMUSP00000110917; ENSMUSG00000075705.
GeneIDi27361.
KEGGimmu:27361.
UCSCiuc008ayh.1. mouse.

Organism-specific databases

CTDi51734.
MGIiMGI:1351642. Msrb1.

Phylogenomic databases

eggNOGiKOG0856. Eukaryota.
COG0229. LUCA.
GeneTreeiENSGT00510000047678.
HOGENOMiHOG000243424.
HOVERGENiHBG002192.
InParanoidiQ9JLC3.
KOiK07305.
OMAiLKVSCGR.
OrthoDBiEOG7VHSZD.
PhylomeDBiQ9JLC3.
TreeFamiTF329147.

Enzyme and pathway databases

BRENDAi1.8.4.12. 3474.
ReactomeiR-MMU-5676934. Protein repair.

Miscellaneous databases

EvolutionaryTraceiQ9JLC3.
PROiQ9JLC3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JLC3.
CleanExiMM_SEPX1.
GenevisibleiQ9JLC3. MM.

Family and domain databases

Gene3Di2.170.150.20. 1 hit.
InterProiIPR028427. Met_Sox_Rdtase.
IPR002579. Met_Sox_Rdtase_MsrB.
IPR011057. Mss4-like.
[Graphical view]
PANTHERiPTHR10173. PTHR10173. 1 hit.
PfamiPF01641. SelR. 1 hit.
[Graphical view]
SUPFAMiSSF51316. SSF51316. 1 hit.
PROSITEiPS51790. MSRB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "New mammalian selenocysteine-containing proteins identified with an algorithm that searches for selenocysteine insertion sequence elements."
    Kryukov G.V., Kryukov V.M., Gladyshev V.N.
    J. Biol. Chem. 274:33888-33897(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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: Heart and Kidney.
  3. "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/6J.
    Tissue: Brain.
  4. "Selenoprotein R is a zinc-containing stereo-specific methionine sulfoxide reductase."
    Kryukov G.V., Kumar R.A., Koc A., Sun Z., Gladyshev V.N.
    Proc. Natl. Acad. Sci. U.S.A. 99:4245-4250(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME ACTIVITY.
  5. "Methionine sulfoxide reduction in mammals: characterization of methionine-R-sulfoxide reductases."
    Kim H.-Y., Gladyshev V.N.
    Mol. Biol. Cell 15:1055-1064(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COFACTOR, SUBCELLULAR LOCATION.
  6. "MsrB1 and MICALs regulate actin assembly and macrophage function via reversible stereoselective methionine oxidation."
    Lee B.C., Peterfi Z., Hoffmann F.W., Moore R.E., Kaya A., Avanesov A., Tarrago L., Zhou Y., Weerapana E., Fomenko D.E., Hoffmann P.R., Gladyshev V.N.
    Mol. Cell 51:397-404(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
  7. "NMR assignments of 1H, 13C and 15N spectra of methionine sulfoxide reductase B1 from Mus musculus."
    Sal L.S., Aachmann F.L., Kim H.Y., Gladyshev V.N., Dikiy A.
    Biomol. NMR. Assign. 1:131-133(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiMSRB1_MOUSE
AccessioniPrimary (citable) accession number: Q9JLC3
Secondary accession number(s): Q545U8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: February 26, 2008
Last modified: June 8, 2016
This is version 115 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.