SBP1_RAT
ID SBP1_RAT Reviewed; 472 AA.
AC Q8VIF7;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
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;
DE AltName: Full=Selenium-binding protein 2;
GN Name=Selenbp1; Synonyms=Sbp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Oguri K., Ishida T., Noda Y.;
RT "PCB126-inducible 54 kDa protein in rat liver.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 PROTEIN SEQUENCE OF 104-114; 246-254 AND 412-419, TISSUE SPECIFICITY, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=15352247; DOI=10.1002/pmic.200300836;
RA Shipkova M., Beck H., Voland A., Armstrong V.W., Groene H.-J.,
RA Oellerich M., Wieland E.;
RT "Identification of protein targets for mycophenolic acid acyl glucuronide
RT in rat liver and colon tissue.";
RL Proteomics 4:2728-2738(2004).
RN [4]
RP PROTEIN SEQUENCE OF 221-231; 282-294 AND 369-381, AND INDUCTION.
RC TISSUE=Liver;
RX PubMed=8701438; DOI=10.1016/0378-4274(96)03668-5;
RA Ishii Y., Hatsumura M., Ishida T., Ariyoshi N., Oguri K.;
RT "Significant induction of a 54-kDa protein in rat liver with homologous
RT alignment to mouse selenium binding protein by a coplanar polychlorinated
RT biphenyl, 3,4,5,3',4'-pentachlorobiphenyl and 3-methylcholanthrene.";
RL Toxicol. Lett. 87:1-9(1996).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=17377489; DOI=10.4161/auto.3910;
RA Overbye A., Fengsrud M., Seglen P.O.;
RT "Proteomic analysis of membrane-associated proteins from rat liver
RT autophagosomes.";
RL Autophagy 3:300-322(2007).
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 (PubMed:10799528, PubMed:17377489).
CC {ECO:0000250|UniProtKB:Q13228, ECO:0000269|PubMed:10799528,
CC ECO:0000269|PubMed:17377489}.
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:0000269|PubMed:17377489}; Peripheral membrane protein
CC {ECO:0000269|PubMed:17377489}. Note=May associate with Golgi membrane
CC (PubMed:17377489). May associate with the membrane of autophagosomes
CC (PubMed:17377489). {ECO:0000269|PubMed:17377489}.
CC -!- TISSUE SPECIFICITY: Present in liver and colon (at protein level).
CC {ECO:0000269|PubMed:15352247}.
CC -!- INDUCTION: In liver, by 3,4,5,3',4'-pentachlorobiphenyl and 3-
CC methylcholanthrene (at protein level). {ECO:0000269|PubMed:8701438}.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: In vivo target of mycophenolic acid, the active
CC metabolite of the immunosuppressant mycophenolate mofetil.
CC -!- SIMILARITY: Belongs to the selenium-binding protein family.
CC {ECO:0000305}.
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DR EMBL; AB036799; BAB83134.1; -; mRNA.
DR EMBL; BC074008; AAH74008.1; -; mRNA.
DR RefSeq; NP_001316822.1; NM_001329893.1.
DR RefSeq; NP_543168.1; NM_080892.1.
DR AlphaFoldDB; Q8VIF7; -.
DR SMR; Q8VIF7; -.
DR BioGRID; 250861; 1.
DR IntAct; Q8VIF7; 1.
DR STRING; 10116.ENSRNOP00000028510; -.
DR iPTMnet; Q8VIF7; -.
DR PhosphoSitePlus; Q8VIF7; -.
DR PaxDb; Q8VIF7; -.
DR PRIDE; Q8VIF7; -.
DR Ensembl; ENSRNOT00000101667; ENSRNOP00000094007; ENSRNOG00000047158.
DR GeneID; 103689947; -.
DR GeneID; 140927; -.
DR KEGG; rno:103689947; -.
DR UCSC; RGD:620571; rat.
DR CTD; 8991; -.
DR RGD; 620571; Selenbp1.
DR eggNOG; KOG0918; Eukaryota.
DR GeneTree; ENSGT00390000014244; -.
DR InParanoid; Q8VIF7; -.
DR OrthoDB; 483905at2759; -.
DR PhylomeDB; Q8VIF7; -.
DR PRO; PR:Q8VIF7; -.
DR Proteomes; UP000002494; Chromosome 2.
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; ISO:RGD.
DR GO; GO:0008430; F:selenium binding; IEA:InterPro.
DR GO; GO:0050873; P:brown fat cell differentiation; ISO:RGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR008826; Se-bd.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
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_0000289063"
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:0000250|UniProtKB:P17563"
FT CONFLICT 227
FT /note="Missing (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 230..231
FT /note="VW -> RN (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="G -> H (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="C -> G (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="K -> P (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 472 AA; 52532 MW; 1DB681BF68E6E69B CRC64;
MATKCTKCGP GYATPLEAMK GPREEIVYLP CIYRNTGIEA PDYLATVDVD PKSPHYSQVI
HRLPMPHLKD ELHHSGWNTC SSCFGDSTKS RDKLILPSII SSRIYVVDVG SEPRAPKLHK
VIEPNEIHAK CNLGNLHTSH CLASGEVMIS SLGDPQGNGK GGFVLLDGET FEVKGTWEKP
GGEAPMGYDF WYQPRHNIMV STEWAAPNVF KDGFNPAHVE AGLYGSHIHV WDWQRHEIIQ
TLQMKDGLIP LEIRFLHDPD ATQGFVGCAL SSNIQRFYKN EGGTWSVEKV IQVPSKKVKG
WMLPEMPGLI TDILLSLDDR FLYFSNWLHG DIRQYDISNP KKPRLTGQIF LGGSIVKGGS
VQVLEDQELT CQPEPLVVKG KRVPGGPQMI QLSLDGKRLY VTTSLYSAWD KQFYPNLIRE
GSVMLQIDVD TANGGLKLNP NFLVDFGKEP LGPALAHELR YPGGDCSSDI WI
