SBP1_HUMAN
ID SBP1_HUMAN Reviewed; 472 AA.
AC Q13228; A6NML9; A6PVW9; B2RDR3; B4DKP6; B4E1F3; Q49AQ8; Q96GX7;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 179.
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=SBP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Heart;
RX PubMed=9027582;
RX DOI=10.1002/(sici)1097-4644(199702)64:2<217::aid-jcb5>3.0.co;2-#;
RA Chang P.W.G., Tsui S.K.W., Liew C., Lee C., Waye M.M.Y., Fung K.;
RT "Isolation, characterization, and chromosomal mapping of a novel cDNA clone
RT encoding human selenium binding protein.";
RL J. Cell. Biochem. 64:217-224(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=Colon, Lung, and Synovial cell;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Colon, and Testis;
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 [7]
RP PROTEIN SEQUENCE OF 255-276, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [8]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=9679983;
RA Yang M., Sytkowski A.J.;
RT "Differential expression and androgen regulation of the human selenium-
RT binding protein gene hSP56 in prostate cancer cells.";
RL Cancer Res. 58:3150-3153(1998).
RN [9]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14991897; DOI=10.1002/path.1524;
RA Chen G., Wang H., Miller C.T., Thomas D.G., Gharib T.G., Misek D.E.,
RA Giordano T.J., Orringer M.B., Hanash S.M., Beer D.G.;
RT "Reduced selenium-binding protein 1 expression is associated with poor
RT outcome in lung adenocarcinomas.";
RL J. Pathol. 202:321-329(2004).
RN [10]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=16223876; DOI=10.1073/pnas.0507666102;
RA Glatt S.J., Everall I.P., Kremen W.S., Corbeil J., Sasik R., Khanlou N.,
RA Han M., Liew C.-C., Tsuang M.T.;
RT "Comparative gene expression analysis of blood and brain provides
RT concurrent validation of SELENBP1 up-regulation in schizophrenia.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:15533-15538(2005).
RN [11]
RP TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16380993; DOI=10.1002/ijc.21671;
RA Huang K.-C., Park D.C., Ng S.-K., Lee J.Y., Ni X., Ng W.-C., Bandera C.A.,
RA Welch W.R., Berkowitz R.S., Mok S.C., Ng S.-W.;
RT "Selenium binding protein 1 in ovarian cancer.";
RL Int. J. Cancer 118:2433-2440(2006).
RN [12]
RP TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16645984; DOI=10.1002/pmic.200500629;
RA Kim H., Kang H.J., You K.T., Kim S.H., Lee K.Y., Kim T.I., Kim C.,
RA Song S.Y., Kim H.-J., Lee C., Kim H.;
RT "Suppression of human selenium-binding protein 1 is a late event in
RT colorectal carcinogenesis and is associated with poor survival.";
RL Proteomics 6:3466-3476(2006).
RN [13]
RP INTERACTION WITH USP33.
RX PubMed=19118533; DOI=10.1016/j.bbrc.2008.12.110;
RA Jeong J.Y., Wang Y., Sytkowski A.J.;
RT "Human selenium binding protein-1 (hSP56) interacts with VDU1 in a
RT selenium-dependent manner.";
RL Biochem. Biophys. Res. Commun. 379:583-588(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111 AND SER-371, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE SPECIFICITY, INVOLVEMENT IN
RP EHMTO, VARIANTS EHMTO TRP-225; TYR-329 AND 347-GLY--ILE-472 DEL,
RP CHARACTERIZATION OF VARIANTS EHMTO TRP-225; TYR-329 AND 347-GLY--ILE-472
RP DEL, AND BIOPHYSICOCHEMICAL PROPERTIES.
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=4.8 nM for methanethiol {ECO:0000269|PubMed:29255262};
CC -!- PATHWAY: Organosulfur degradation. {ECO:0000269|PubMed:29255262}.
CC -!- SUBUNIT: Interacts with USP33. {ECO:0000269|PubMed:19118533}.
CC -!- INTERACTION:
CC Q13228; Q9UJ68: MSRA; NbExp=3; IntAct=EBI-711619, EBI-19157918;
CC Q13228; O43422: THAP12; NbExp=3; IntAct=EBI-711619, EBI-2828217;
CC Q13228; Q15645: TRIP13; NbExp=6; IntAct=EBI-711619, EBI-358993;
CC Q13228; Q8TEY7-2: USP33; NbExp=5; IntAct=EBI-711619, EBI-719307;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14991897}. Cytoplasm,
CC cytosol {ECO:0000269|PubMed:14991897, ECO:0000269|PubMed:16223876}.
CC Membrane {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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q13228-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13228-2; Sequence=VSP_038440;
CC Name=3;
CC IsoId=Q13228-3; Sequence=VSP_045425;
CC Name=4;
CC IsoId=Q13228-4; Sequence=VSP_055126;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in liver, lung,
CC colon, prostate, kidney and pancreas. In brain, present both in neurons
CC and glia (at protein level). Down-regulated in lung adenocarcinoma,
CC colorectal carcinoma and ovarian cancer. Two-fold up-regulated in brain
CC and blood from schizophrenia patients. {ECO:0000269|PubMed:14991897,
CC ECO:0000269|PubMed:16223876, ECO:0000269|PubMed:16380993,
CC ECO:0000269|PubMed:16645984, ECO:0000269|PubMed:29255262,
CC ECO:0000269|PubMed:9679983}.
CC -!- INDUCTION: Down-regulated by androgen in prostate cancer cells.
CC {ECO:0000269|PubMed:9679983}.
CC -!- PTM: Phosphorylated. {ECO:0000305|PubMed:14991897}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000250}.
CC -!- DISEASE: Extraoral halitosis due to methanethiol oxidase deficiency
CC (EHMTO) [MIM:618148]: An autosomal recessive malodor condition
CC characterized by extraoral blood-borne halitosis resulting from the
CC accumulation of sulfur-containing metabolites. In extraoral blood-borne
CC halitosis, malodorant compounds are carried to the lungs, where they
CC enter the breath. Affected individuals have a cabbage-like breath odor,
CC high levels of methanethiol and dimethylsulfide in oral and nasal
CC breath, and elevated urinary excretion of dimethylsulfoxide in the
CC absence of intake of dimethylsulfide-containing food or use of sulfur-
CC containing medication, lower-gastrointestinal problems, and known
CC metabolic defects, such as methionine adenosyltransferase deficiency
CC and tyrosinemia. {ECO:0000269|PubMed:29255262}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the selenium-binding protein family.
CC {ECO:0000305}.
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DR EMBL; U29091; AAB02395.1; -; mRNA.
DR EMBL; CR456852; CAG33133.1; -; mRNA.
DR EMBL; AK296661; BAG59258.1; -; mRNA.
DR EMBL; AK303815; BAG64765.1; -; mRNA.
DR EMBL; AK315643; BAG38010.1; -; mRNA.
DR EMBL; AL391069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53443.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53445.1; -; Genomic_DNA.
DR EMBL; BC009084; AAH09084.1; -; mRNA.
DR EMBL; BC032997; AAH32997.1; -; mRNA.
DR CCDS; CCDS58027.1; -. [Q13228-3]
DR CCDS; CCDS60266.1; -. [Q13228-4]
DR CCDS; CCDS995.1; -. [Q13228-1]
DR PIR; G01872; G01872.
DR RefSeq; NP_001245217.1; NM_001258288.1. [Q13228-3]
DR RefSeq; NP_001245218.1; NM_001258289.1. [Q13228-4]
DR RefSeq; NP_003935.2; NM_003944.3. [Q13228-1]
DR AlphaFoldDB; Q13228; -.
DR SMR; Q13228; -.
DR BioGRID; 114472; 187.
DR CORUM; Q13228; -.
DR IntAct; Q13228; 44.
DR MINT; Q13228; -.
DR STRING; 9606.ENSP00000397261; -.
DR GlyGen; Q13228; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13228; -.
DR PhosphoSitePlus; Q13228; -.
DR SwissPalm; Q13228; -.
DR BioMuta; SELENBP1; -.
DR DMDM; 148840437; -.
DR REPRODUCTION-2DPAGE; IPI00012303; -.
DR REPRODUCTION-2DPAGE; Q13228; -.
DR UCD-2DPAGE; Q13228; -.
DR EPD; Q13228; -.
DR jPOST; Q13228; -.
DR MassIVE; Q13228; -.
DR MaxQB; Q13228; -.
DR PaxDb; Q13228; -.
DR PeptideAtlas; Q13228; -.
DR PRIDE; Q13228; -.
DR ProteomicsDB; 1722; -.
DR ProteomicsDB; 5753; -.
DR ProteomicsDB; 59234; -. [Q13228-1]
DR ProteomicsDB; 59235; -. [Q13228-2]
DR Antibodypedia; 1584; 391 antibodies from 30 providers.
DR DNASU; 8991; -.
DR Ensembl; ENST00000368868.10; ENSP00000357861.5; ENSG00000143416.21. [Q13228-1]
DR Ensembl; ENST00000426705.6; ENSP00000397261.2; ENSG00000143416.21. [Q13228-4]
DR Ensembl; ENST00000447402.7; ENSP00000413960.3; ENSG00000143416.21. [Q13228-3]
DR GeneID; 8991; -.
DR KEGG; hsa:8991; -.
DR MANE-Select; ENST00000368868.10; ENSP00000357861.5; NM_003944.4; NP_003935.2.
DR UCSC; uc010pcy.4; human. [Q13228-1]
DR CTD; 8991; -.
DR DisGeNET; 8991; -.
DR GeneCards; SELENBP1; -.
DR HGNC; HGNC:10719; SELENBP1.
DR HPA; ENSG00000143416; Tissue enhanced (intestine).
DR MalaCards; SELENBP1; -.
DR MIM; 604188; gene.
DR MIM; 618148; phenotype.
DR neXtProt; NX_Q13228; -.
DR OpenTargets; ENSG00000143416; -.
DR Orphanet; 562538; Autosomal recessive extra-oral halitosis.
DR PharmGKB; PA35641; -.
DR VEuPathDB; HostDB:ENSG00000143416; -.
DR eggNOG; KOG0918; Eukaryota.
DR GeneTree; ENSGT00390000014244; -.
DR HOGENOM; CLU_032512_0_0_1; -.
DR InParanoid; Q13228; -.
DR OMA; FDSEFNC; -.
DR OrthoDB; 483905at2759; -.
DR PhylomeDB; Q13228; -.
DR TreeFam; TF315241; -.
DR PathwayCommons; Q13228; -.
DR SignaLink; Q13228; -.
DR BioGRID-ORCS; 8991; 17 hits in 1086 CRISPR screens.
DR ChiTaRS; SELENBP1; human.
DR GeneWiki; SELENBP1; -.
DR GenomeRNAi; 8991; -.
DR Pharos; Q13228; Tbio.
DR PRO; PR:Q13228; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q13228; protein.
DR Bgee; ENSG00000143416; Expressed in mucosa of transverse colon and 200 other tissues.
DR ExpressionAtlas; Q13228; baseline and differential.
DR Genevisible; Q13228; HS.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0018549; F:methanethiol oxidase activity; IMP:FlyBase.
DR GO; GO:0008430; F:selenium binding; TAS:ProtInc.
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; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Disease variant; Membrane; Nucleus; Oxidoreductase; Phosphoprotein;
KW Protein transport; Reference proteome; Selenium; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..472
FT /note="Methanethiol oxidase"
FT /id="PRO_0000174633"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17563"
FT VAR_SEQ 1..64
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038440"
FT VAR_SEQ 1
FT /note="M -> MRLEWGPRPAALPWPAGMCAAERAEGAFTLQSVAQPMRPIAST (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055126"
FT VAR_SEQ 59..120
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045425"
FT VARIANT 225
FT /note="G -> W (in EHMTO; loss of methanethiol oxidation in
FT patient cells; dbSNP:rs758495626)"
FT /evidence="ECO:0000269|PubMed:29255262"
FT /id="VAR_080207"
FT VARIANT 329
FT /note="H -> Y (in EHMTO; loss of methanethiol oxidation in
FT patient cells; dbSNP:rs1553204840)"
FT /evidence="ECO:0000269|PubMed:29255262"
FT /id="VAR_080208"
FT VARIANT 347..472
FT /note="Missing (in EHMTO; loss of methanethiol oxidation in
FT patient cells)"
FT /evidence="ECO:0000269|PubMed:29255262"
FT /id="VAR_080209"
FT CONFLICT 80
FT /note="C -> Y (in Ref. 1; AAB02395)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="T -> N (in Ref. 1; AAB02395)"
FT /evidence="ECO:0000305"
FT CONFLICT 114..116
FT /note="RAP -> GPQ (in Ref. 1; AAB02395)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="F -> C (in Ref. 1; AAB02395)"
FT /evidence="ECO:0000305"
FT CONFLICT 260..262
FT /note="DAA -> SAT (in Ref. 1; AAB02395)"
FT /evidence="ECO:0000305"
FT CONFLICT 270..273
FT /note="LSST -> SAPN (in Ref. 1; AAB02395)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="Y -> C (in Ref. 3; BAG59258)"
FT /evidence="ECO:0000305"
FT CONFLICT 280..282
FT /note="NEG -> TRE (in Ref. 1; AAB02395)"
FT /evidence="ECO:0000305"
FT CONFLICT 305..306
FT /note="EM -> GV (in Ref. 1; AAB02395)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="D -> E (in Ref. 1; AAB02395)"
FT /evidence="ECO:0000305"
FT CONFLICT 442
FT /note="F -> C (in Ref. 1; AAB02395)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 472 AA; 52391 MW; 6DC68F9B45FEC1BC CRC64;
MATKCGNCGP GYSTPLEAMK GPREEIVYLP CIYRNTGTEA PDYLATVDVD PKSPQYCQVI
HRLPMPNLKD ELHHSGWNTC SSCFGDSTKS RTKLVLPSLI SSRIYVVDVG SEPRAPKLHK
VIEPKDIHAK CELAFLHTSH CLASGEVMIS SLGDVKGNGK GGFVLLDGET FEVKGTWERP
GGAAPLGYDF WYQPRHNVMI STEWAAPNVL RDGFNPADVE AGLYGSHLYV WDWQRHEIVQ
TLSLKDGLIP LEIRFLHNPD AAQGFVGCAL SSTIQRFYKN EGGTWSVEKV IQVPPKKVKG
WLLPEMPGLI TDILLSLDDR FLYFSNWLHG DLRQYDISDP QRPRLTGQLF LGGSIVKGGP
VQVLEDEELK SQPEPLVVKG KRVAGGPQMI QLSLDGKRLY ITTSLYSAWD KQFYPDLIRE
GSVMLQVDVD TVKGGLKLNP NFLVDFGKEP LGPALAHELR YPGGDCSSDI WI
