ID   SBP1_PONAB              Reviewed;         472 AA.
AC   Q5RF48;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Methanethiol oxidase {ECO:0000250|UniProtKB:Q13228};
DE            Short=MTO {ECO:0000250|UniProtKB:Q13228};
DE            EC=1.8.3.4 {ECO:0000250|UniProtKB:Q13228};
DE   AltName: Full=Selenium-binding protein 1;
GN   Name=SELENBP1; Synonyms=SBP;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the oxidation of methanethiol, an organosulfur
CC       compound known to be produced in substantial amounts by gut bacteria
CC       (By similarity). Selenium-binding protein which may be involved in the
CC       sensing of reactive xenobiotics in the cytoplasm. May be involved in
CC       intra-Golgi protein transport (By similarity).
CC       {ECO:0000250|UniProtKB:Q13228, ECO:0000250|UniProtKB:Q8VIF7}.
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:0000250|UniProtKB:Q13228};
CC   -!- PATHWAY: Organosulfur degradation. {ECO:0000250|UniProtKB:Q13228}.
CC   -!- SUBUNIT: Interacts with USP33. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytosol
CC       {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}. Note=May associate with Golgi membrane. May associate
CC       with the membrane of autophagosomes (By similarity). {ECO:0000250}.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the selenium-binding protein family.
CC       {ECO:0000305}.
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DR   EMBL; CR857313; CAH89609.1; -; mRNA.
DR   RefSeq; NP_001127175.1; NM_001133703.2.
DR   AlphaFoldDB; Q5RF48; -.
DR   SMR; Q5RF48; -.
DR   STRING; 9601.ENSPPYP00000001013; -.
DR   GeneID; 100174227; -.
DR   KEGG; pon:100174227; -.
DR   CTD; 8991; -.
DR   eggNOG; KOG0918; Eukaryota.
DR   InParanoid; Q5RF48; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0018549; F:methanethiol oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008430; F:selenium binding; IEA:InterPro.
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   2: Evidence at transcript 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_0000289062"
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         371
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13228"
FT   MOD_RES         467
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P17563"
SQ   SEQUENCE   472 AA;  52451 MW;  7F245AC7A5E7489E CRC64;
     MATKCGNCGP GYSTPLEAMK GPREEIVYLP CIYRNTGTEA PDYLATVDVD PKSPQYCQVI
     HRLPMPNLKD ELHHSGWNTC SSCFGDSTKS RTKLVLPSLI SSRIYVVDVG SEPRALKLHK
     VIEPKDIHAK CELAFLHTSH CLASGEVMIS SLGDVKGNGK GGFVLLDAET FEVKGTWERR
     GGAAPLGYDF WYQPRHNVMI STEWAAPNVL RDGFNPADVE AGLYGSHLYV WDWQRHEIVQ
     TLSLKDGLIP LEIRFLHNPD AAQGFVGCAL SSTIQRFYKN EGGTWSVEKV IQVPPKKVKG
     WLLPEMPGLI TDILLSLDDR FLYFSNWLHG DLRQYDISDP QRPRLTGQLF VGGSIVKGGP
     VQVLEDQELK SQPEPLVVKG KRVAGGPQMI QLSLDGKRLY VTTSLYSAWD KQFYPDLIRE
     GSVMLQVDVD TVKGGLKLNP NFLVDFGKEP LGPALAHELR YPGGDCSSDI WI