SBP1_MOUSE
ID SBP1_MOUSE Reviewed; 472 AA.
AC P17563; Q91X87;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Methanethiol oxidase {ECO:0000303|PubMed:29255262};
DE Short=MTO {ECO:0000303|PubMed:29255262};
DE EC=1.8.3.4 {ECO:0000269|PubMed:29255262};
DE AltName: Full=56 kDa selenium-binding protein;
DE Short=SBP56;
DE Short=SP56;
DE AltName: Full=Selenium-binding protein 1;
GN Name=Selenbp1; Synonyms=Lpsb;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=2225343; DOI=10.1093/carcin/11.11.2071;
RA Bansel M.P., Mukhopadhyay T., Scott J., Cook R.G., Mukhopadhyay R.,
RA Medina D.;
RT "DNA sequencing of a mouse liver protein that binds selenium: implications
RT for selenium's mechanism of action in cancer prevention.";
RL Carcinogenesis 11:2071-2073(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION AT SER-467.
RX PubMed=15378723; DOI=10.1002/rcm.1604;
RA Jin W.-H., Dai J., Zhou H., Xia Q.-C., Zou H.-F., Zeng R.;
RT "Phosphoproteome analysis of mouse liver using immobilized metal affinity
RT purification and linear ion trap mass spectrometry.";
RL Rapid Commun. Mass Spectrom. 18:2169-2176(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=29255262; DOI=10.1038/s41588-017-0006-7;
RA Pol A., Renkema G.H., Tangerman A., Winkel E.G., Engelke U.F.,
RA de Brouwer A.P.M., Lloyd K.C., Araiza R.S., van den Heuvel L., Omran H.,
RA Olbrich H., Oude Elberink M., Gilissen C., Rodenburg R.J., Sass J.O.,
RA Schwab K.O., Schaefer H., Venselaar H., Sequeira J.S., Op den Camp H.J.M.,
RA Wevers R.A.;
RT "Mutations in SELENBP1, encoding a novel human methanethiol oxidase, cause
RT extraoral halitosis.";
RL Nat. Genet. 50:120-129(2018).
CC -!- FUNCTION: Catalyzes the oxidation of methanethiol, an organosulfur
CC compound known to be produced in substantial amounts by gut bacteria
CC (PubMed:29255262). Selenium-binding protein which may be involved in
CC the sensing of reactive xenobiotics in the cytoplasm. May be involved
CC in intra-Golgi protein transport (By similarity).
CC {ECO:0000250|UniProtKB:Q8VIF7, ECO:0000269|PubMed:29255262}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + methanethiol + O2 = formaldehyde + H(+) + H2O2 +
CC hydrogen sulfide; Xref=Rhea:RHEA:11812, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16007,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:16842, ChEBI:CHEBI:29919; EC=1.8.3.4;
CC Evidence={ECO:0000269|PubMed:29255262};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5 nM for methanethiol {ECO:0000269|PubMed:29255262};
CC -!- PATHWAY: Organosulfur degradation. {ECO:0000269|PubMed:29255262}.
CC -!- SUBUNIT: Interacts with USP33. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13228}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q13228}. Membrane
CC {ECO:0000250|UniProtKB:Q8VIF7}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q8VIF7}. Note=May associate with Golgi membrane
CC (By similarity). May associate with the membrane of autophagosomes (By
CC similarity). {ECO:0000250|UniProtKB:Q8VIF7}.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver, kidney and, to a lesser
CC extent, lung.
CC -!- PTM: The N-terminus is blocked. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: SELENBP1 knockout results in accumulation of
CC dimethylsulfoxide in the plasma. Methanethiol oxidase activity measured
CC in tissues from knockout mice is significantly lower that in normal
CC tissues. {ECO:0000269|PubMed:29255262}.
CC -!- SIMILARITY: Belongs to the selenium-binding protein family.
CC {ECO:0000305}.
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DR EMBL; M32032; AAA40104.1; -; mRNA.
DR EMBL; BC011202; AAH11202.1; -; mRNA.
DR CCDS; CCDS38540.1; -.
DR PIR; S27878; S27878.
DR RefSeq; NP_033176.2; NM_009150.3.
DR AlphaFoldDB; P17563; -.
DR SMR; P17563; -.
DR BioGRID; 203156; 10.
DR IntAct; P17563; 2.
DR MINT; P17563; -.
DR STRING; 10090.ENSMUSP00000088349; -.
DR iPTMnet; P17563; -.
DR PhosphoSitePlus; P17563; -.
DR SwissPalm; P17563; -.
DR REPRODUCTION-2DPAGE; IPI00623845; -.
DR REPRODUCTION-2DPAGE; P17563; -.
DR SWISS-2DPAGE; P17563; -.
DR EPD; P17563; -.
DR jPOST; P17563; -.
DR MaxQB; P17563; -.
DR PaxDb; P17563; -.
DR PeptideAtlas; P17563; -.
DR PRIDE; P17563; -.
DR ProteomicsDB; 255462; -.
DR DNASU; 20341; -.
DR Ensembl; ENSMUST00000090839; ENSMUSP00000088349; ENSMUSG00000068874.
DR GeneID; 20341; -.
DR KEGG; mmu:20341; -.
DR UCSC; uc008qhf.1; mouse.
DR CTD; 8991; -.
DR MGI; MGI:96825; Selenbp1.
DR VEuPathDB; HostDB:ENSMUSG00000068874; -.
DR eggNOG; KOG0918; Eukaryota.
DR GeneTree; ENSGT00390000014244; -.
DR HOGENOM; CLU_032512_0_0_1; -.
DR InParanoid; P17563; -.
DR OMA; FDSEFNC; -.
DR OrthoDB; 483905at2759; -.
DR PhylomeDB; P17563; -.
DR TreeFam; TF315241; -.
DR BioGRID-ORCS; 20341; 0 hits in 53 CRISPR screens.
DR ChiTaRS; Selenbp1; mouse.
DR PRO; PR:P17563; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P17563; protein.
DR Bgee; ENSMUSG00000068874; Expressed in right lung lobe and 203 other tissues.
DR ExpressionAtlas; P17563; baseline and differential.
DR Genevisible; P17563; MM.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0018549; F:methanethiol oxidase activity; ISO:MGI.
DR GO; GO:0008430; F:selenium binding; TAS:MGI.
DR GO; GO:0050873; P:brown fat cell differentiation; IDA:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR008826; Se-bd.
DR PANTHER; PTHR23300; PTHR23300; 1.
DR Pfam; PF05694; SBP56; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Membrane; Nucleus; Oxidoreductase; Phosphoprotein;
KW Protein transport; Reference proteome; Selenium; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q13228"
FT CHAIN 2..472
FT /note="Methanethiol oxidase"
FT /id="PRO_0000174634"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q13228"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13228"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15378723"
FT CONFLICT 270..272
FT /note="LSS -> SAP (in Ref. 1; AAA40104)"
FT /evidence="ECO:0000305"
FT CONFLICT 305..306
FT /note="EM -> GV (in Ref. 1; AAA40104)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="P -> A (in Ref. 1; AAA40104)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 472 AA; 52514 MW; 099BCE085668DE36 CRC64;
MATKCTKCGP GYSTPLEAMK GPREEIVYLP CIYRNTGTEA PDYLATVDVD PKSPQYSQVI
HRLPMPYLKD ELHHSGWNTC SSCFGDSTKS RNKLILPGLI SSRIYVVDVG SEPRAPKLHK
VIEASEIQAK CNVSSLHTSH CLASGEVMVS TLGDLQGNGK GSFVLLDGET FEVKGTWEKP
GDAAPMGYDF WYQPRHNVMV STEWAAPNVF KDGFNPAHVE AGLYGSRIFV WDWQRHEIIQ
TLQMTDGLIP LEIRFLHDPS ATQGFVGCAL SSNIQRFYKN AEGTWSVEKV IQVPSKKVKG
WMLPEMPGLI TDILLSLDDR FLYFSNWLHG DIRQYDISNP QKPRLAGQIF LGGSIVRGGS
VQVLEDQELT CQPEPLVVKG KRIPGGPQMI QLSLDGKRLY ATTSLYSAWD KQFYPDLIRE
GSMMLQIDVD TVNGGLKLNP NFLVDFGKEP LGPALAHELR YPGGDCSSDI WI
