ID   SBP1_BOVIN              Reviewed;         472 AA.
AC   Q2KJ32;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=56 kDa selenium-binding protein;
DE            Short=SBP56;
DE            Short=SP56;
DE   AltName: Full=Selenium-binding protein 1;
GN   Name=SELENBP1; Synonyms=SBP;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 103-114; 212-220; 320-325 AND 436-448, FUNCTION, AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Brain;
RX   PubMed=10799528; DOI=10.1074/jbc.275.19.14457;
RA   Porat A., Sagiv Y., Elazar Z.;
RT   "A 56-kDa selenium-binding protein participates in intra-Golgi protein
RT   transport.";
RL   J. Biol. Chem. 275:14457-14465(2000).
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. {ECO:0000250|UniProtKB:Q13228,
CC       ECO:0000269|PubMed:10799528}.
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|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   -!- 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; BC105545; AAI05546.1; -; mRNA.
DR   RefSeq; NP_001039513.1; NM_001046048.1.
DR   AlphaFoldDB; Q2KJ32; -.
DR   SMR; Q2KJ32; -.
DR   STRING; 9913.ENSBTAP00000010644; -.
DR   PaxDb; Q2KJ32; -.
DR   PeptideAtlas; Q2KJ32; -.
DR   PRIDE; Q2KJ32; -.
DR   Ensembl; ENSBTAT00000010644; ENSBTAP00000010644; ENSBTAG00000008091.
DR   GeneID; 510154; -.
DR   KEGG; bta:510154; -.
DR   CTD; 8991; -.
DR   VEuPathDB; HostDB:ENSBTAG00000008091; -.
DR   VGNC; VGNC:34422; SELENBP1.
DR   eggNOG; KOG0918; Eukaryota.
DR   GeneTree; ENSGT00390000014244; -.
DR   HOGENOM; CLU_032512_0_0_1; -.
DR   InParanoid; Q2KJ32; -.
DR   OMA; FDSEFNC; -.
DR   OrthoDB; 483905at2759; -.
DR   TreeFam; TF315241; -.
DR   Proteomes; UP000009136; Chromosome 3.
DR   Bgee; ENSBTAG00000008091; Expressed in cortex of kidney and 103 other tissues.
DR   ExpressionAtlas; Q2KJ32; baseline and differential.
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   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Membrane; Nucleus;
KW   Oxidoreductase; Phosphoprotein; Protein transport; Reference proteome;
KW   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_0000289061"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13228"
FT   MOD_RES         467
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P17563"
SQ   SEQUENCE   472 AA;  52555 MW;  6F9E2D774BC7E150 CRC64;
     MATKCGKCGP GYPSPLEAMK GPREELVYLP CIYRNTGTEA PDYLATVDVN PKSPQYSQVI
     HRLPMPNLKD ELHHSGWNTC SSCFGDSTKS RTKLLLPSLI SSRVYVVDVA TEPRAPKLHK
     VVEPEEIHAK CDLSYLHTSH CLASGEVMIS ALGDPRGNGK GGFVLLDGET FEVKGTWEQP
     GGAAPMGYDF WYQPRHNVMI STEWAAPNVL RDGFNPADVE AGLYGQHLYV WDWQRHERVQ
     TLTLQDGLIP LEIRFLHNPA ADQGFVGCAL GSNIQRFYKN QGGTWSVEKV IQVPPKKVKG
     WILPEMPSLI TDILLSLDDR FLYFSNWLHG DLRQYDISDP KRPRLVGQIF LGGSIVKGGP
     VQVLEDQELK CQPEPLVVKG KRVAGGPQMI QLSLDGTRLY VTTSLYSAWD KQFYPDLIRE
     GSVMLQIDVD TVRGGLKLNP NFLVDFGKEP LGPALAHELR YPGGDCSSDI WL