Reviewed, UniProtKB/Swiss-Prot Q8INK9 (MSRB_DROME)

Names and origin

Protein names

Recommended name:
    Methionine-R-sulfoxide reductase B1
    EC=1.8.4.-
Alternative name(s):
    Selenoprotein R

Gene names

Name:	SelR
Synonyms:	MsrB, MsrB1
ORF Names:	CG6584

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	208 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)

Catalytic activity	Protein L-methionine + oxidized thioredoxin = protein L-methionine R-oxide + reduced thioredoxin. Ref.1
Cofactor	Binds 1 zinc ion per subunit.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
Sequence similarities	Belongs to the msrB Met sulfoxide reductase family.
Mass spectrometry	Molecular mass is 19439.6 Da from positions 2 - 156 (Q8INK9-2). Determined by ESI. Ref.6

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	Metal-binding Zinc
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	peptide-methionine-(S)-S-oxide reductase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct protein-methionine-R-oxide reductase activity Ref.1 Ref.6 Inferred from direct assay. Source: FlyBase zinc ion binding Ref.6 Inferred from direct assay. Source: FlyBase
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CG11899	Q9VAN0	1	EBI-218847,EBI-83690

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Isoform E Ref.3 (identifier: Q8INK9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: No experimental confirmation available.

Isoform A Ref.1 (identifier: Q8INK9-2)

Also known as: I;

The sequence of this isoform differs from the canonical sequence as follows:
     1-42: Missing.
     134-144: Missing.

Isoform B Ref.3 (identifier: Q8INK9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-42: Missing.

Note: No experimental confirmation available.

Isoform C Ref.3 (identifier: Q8INK9-4)

The sequence of this isoform differs from the canonical sequence as follows:
     134-144: Missing.

Note: No experimental confirmation available.

Isoform G (identifier: Q8INK9-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-42: Missing.
     135-208: GGNILLLIAH...TPTAAPIAQQ → VVISKTLGMV...ADPSTASSKK

Note: No experimental confirmation available.

Isoform H (identifier: Q8INK9-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-42: Missing.
     136-208: GNILLLIAHP...TPTAAPIAQQ → MVRTEVRCSR...ADPSTASSKK

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.6
	Chain	2 – 208	207	Methionine-R-sulfoxide reductase B1		PRO_0000140323
Sites
	Active site	177	1	Nucleophile
	Metal binding	93	1	Zinc Ref.6
	Metal binding	96	1	Zinc Ref.6
	Metal binding	154	1	Zinc Ref.6
	Metal binding	157	1	Zinc Ref.6
Amino acid modifications
	Disulfide bond	111 ↔ 177		Ref.6
Natural variations
	Alternative sequence	1 – 42	42	Missing in isoform A, isoform B, isoform G and isoform H.		VSP_008300
	Alternative sequence	134 – 144	11	Missing in isoform A and isoform C. Ref.1 Ref.3		VSP_008301
	Alternative sequence	135 – 208	74	GGNIL…PIAQQ → VVISKTLGMVRTEVRCSRCS AHMGHVFDDGPPPKHRRFCI NSASIDFVKSATPSKADPST ASSKK in isoform G.		VSP_035868
	Alternative sequence	136 – 208	73	GNILL…PIAQQ → MVRTEVRCSRCSAHMGHVFD DGPPPKHRRFCINSASIDFV KSATPSKADPSTASSKK in isoform H.		VSP_035869
Experimental info
	Mutagenesis	93	1	C → G: Loss of activity and zinc binding. Ref.6
	Mutagenesis	96	1	C → G or S: Loss of activity and zinc binding. Ref.6
	Mutagenesis	111	1	C → S: Thioredoxin-dependent activity reduced, but no change in DTT-dependent activity. Ref.6
	Mutagenesis	154	1	C → G or S: Loss of activity and zinc binding. Ref.6
	Mutagenesis	157	1	C → S: Loss of activity and zinc binding. Ref.6
	Mutagenesis	160	1	H → G: Loss of thioredoxin-dependent activity, 81% DTT-dependent activity. Ref.6
	Mutagenesis	163	1	H → G: Loss of thioredoxin-dependent activity, 80% DTT-dependent activity. Ref.6
	Mutagenesis	177	1	C → K or S: Loss of activity. Ref.6
	Mutagenesis	180	1	S → G: Loss of thioredoxin-dependent activity, 85% DTT-dependent activity. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform E [UniParc]. Last modified January 23, 2007. Version 3. Checksum: A8193586F60C1DCF	FASTA	208	23,299
	10 20 30 40 50 60 MFALSARHAL RRTRIFAIPR FFADSRQDSD NPDKRYSGPA ATMDNKSEKV TVNKEELRKR 70 80 90 100 110 120 LTPVQYQVTQ EAGTERPFTG CYNKHYEKGV YQCIVCHQDL FSSETKYDSG CGWPAFNDVL 130 140 150 160 170 180 DKGKVTLHRD ASIPGGNILL LIAHPERIRT EVRCARCNAH MGHVFEDGPK PTRKRYCINS 190 200 ASIEFVNADP ATSSPPVATP TAAPIAQQ
	Isoform A (I). Checksum: 0DFC748D90B50AEB	FASTA	155	17,407
	10 20 30 40 50 60 MDNKSEKVTV NKEELRKRLT PVQYQVTQEA GTERPFTGCY NKHYEKGVYQ CIVCHQDLFS 70 80 90 100 110 120 SETKYDSGCG WPAFNDVLDK GKVTLHRDAS IPERIRTEVR CARCNAHMGH VFEDGPKPTR 130 140 150 KRYCINSASI EFVNADPATS SPPVATPTAA PIAQQ
	Isoform B. Checksum: A78A1762CDD48A16	FASTA	166	18,506
	10 20 30 40 50 60 MDNKSEKVTV NKEELRKRLT PVQYQVTQEA GTERPFTGCY NKHYEKGVYQ CIVCHQDLFS 70 80 90 100 110 120 SETKYDSGCG WPAFNDVLDK GKVTLHRDAS IPGGNILLLI AHPERIRTEV RCARCNAHMG 130 140 150 160 HVFEDGPKPT RKRYCINSAS IEFVNADPAT SSPPVATPTA APIAQQ
	Isoform C. Checksum: 1DD417F98337BC18	FASTA	197	22,200
	10 20 30 40 50 60 MFALSARHAL RRTRIFAIPR FFADSRQDSD NPDKRYSGPA ATMDNKSEKV TVNKEELRKR 70 80 90 100 110 120 LTPVQYQVTQ EAGTERPFTG CYNKHYEKGV YQCIVCHQDL FSSETKYDSG CGWPAFNDVL 130 140 150 160 170 180 DKGKVTLHRD ASIPERIRTE VRCARCNAHM GHVFEDGPKP TRKRYCINSA SIEFVNADPA 190 TSSPPVATPT AAPIAQQ
	Isoform G. Checksum: 15F1C3D5C6B1E856	FASTA	157	17,572
	10 20 30 40 50 60 MDNKSEKVTV NKEELRKRLT PVQYQVTQEA GTERPFTGCY NKHYEKGVYQ CIVCHQDLFS 70 80 90 100 110 120 SETKYDSGCG WPAFNDVLDK GKVTLHRDAS IPVVISKTLG MVRTEVRCSR CSAHMGHVFD 130 140 150 DGPPPKHRRF CINSASIDFV KSATPSKADP STASSKK
	Isoform H. Checksum: 8DE3E2648881E0DE	FASTA	150	16,831
	10 20 30 40 50 60 MDNKSEKVTV NKEELRKRLT PVQYQVTQEA GTERPFTGCY NKHYEKGVYQ CIVCHQDLFS 70 80 90 100 110 120 SETKYDSGCG WPAFNDVLDK GKVTLHRDAS IPGMVRTEVR CSRCSAHMGH VFDDGPPPKH 130 140 150 RRFCINSASI DFVKSATPSK ADPSTASSKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 11929995] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), ENZYME ACTIVITY, ZINC-BINDING.
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
[4]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A; G AND H). Strain: Berkeley. Tissue: Embryo and Head.
[5]	Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B). Strain: Berkeley. Tissue: Embryo.
[6]	"Reaction mechanism, evolutionary analysis, and role of zinc in Drosophila methionine-R-sulfoxide reductase." Kumar R.A., Koc A., Cerny R.L., Gladyshev V.N. J. Biol. Chem. 277:37527-37535(2002) [PubMed: 12145281] [Abstract] Cited for: ZINC-BINDING, DISULFIDE BOND, MASS SPECTROMETRY, MUTAGENESIS OF CYS-93; CYS-96; CYS-111; CYS-154; CYS-157; HIS-160; HIS-163; CYS-177 AND SER-180.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF486578 mRNA. Translation: AAM10931.1. AE014297 Genomic DNA. Translation: AAF54569.1. AE014297 Genomic DNA. Translation: AAN13490.1. AE014297 Genomic DNA. Translation: AAN13491.1. AE014297 Genomic DNA. Translation: AAN13492.1. AE014297 Genomic DNA. Translation: AAN13493.2. AE014297 Genomic DNA. Translation: AAS65138.1. AE014297 Genomic DNA. Translation: ACL83495.1. AY070627 mRNA. Translation: AAL48098.1. BT001621 mRNA. Translation: AAN71376.1. BT001854 mRNA. Translation: AAN71615.1. BT011487 mRNA. Translation: AAR99145.1.
RefSeq	NP_001138036.1. NP_650030.1. NP_731522.1. NP_731523.1. NP_731524.1. NP_731525.2. NP_996195.1.
UniGene	Dm.1144
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8INK9. 1 interaction.
STRING	Q8INK9.
Proteomic databases
PRIDE	Q8INK9.
Genome annotation databases
Ensembl	FBtr0082291; FBpp0081768; FBgn0037847; Drosophila melanogaster. [Genome view] FBtr0082292; FBpp0081769; FBgn0037847; Drosophila melanogaster. [Genome view] FBtr0082294; FBpp0081771; FBgn0037847; Drosophila melanogaster. [Genome view] FBtr0082295; FBpp0081772; FBgn0037847; Drosophila melanogaster. [Genome view] FBtr0273345; FBpp0271853; FBgn0037847; Drosophila melanogaster. [Genome view] FBtr0273346; FBpp0271854; FBgn0037847; Drosophila melanogaster. [Genome view] FBtr0273347; FBpp0271855; FBgn0037847; Drosophila melanogaster. [Genome view]
GeneID	41309.
KEGG	dme:Dmel_CG6584.
Organism-specific databases
CTD	41309.
FlyBase	FBgn0037847. SelR.
Phylogenomic databases
HOGENOM	Q8INK9.
OMA	MVERIEL
OrthoDB	EOG9W0XM8
Gene expression databases
ArrayExpress	Q8INK9.
Bgee	Q8INK9.
GermOnline	CG6584. Drosophila melanogaster.
Family and domain databases
InterPro	IPR002579. Methionine_sulphoxide_MsrB. IPR011057. Mss4-like. [Graphical view]
Gene3D	G3DSA:2.170.150.20. MsrB. 1 hit.
Pfam	PF01641. SelR. 1 hit. [Graphical view]
TIGRFAMs	TIGR00357. MsrB. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	823244.

Entry information

Entry name

MSRB_DROME

Accession

Primary (citable) accession number: Q8INK9
Secondary accession number(s): A4V2P1 , B7Z0V7, Q53XF3, Q8IGC0, Q8IGS8, Q8INK8, Q8INL0, Q8STJ0, Q9VGV4

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2003
Last sequence update:	January 23, 2007
Last modified:	November 24, 2009
This is version 63 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project