SQOR_MOUSE
ID SQOR_MOUSE Reviewed; 450 AA.
AC Q9R112; Q8BW20; Q91XA1; Q9D891;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Sulfide:quinone oxidoreductase, mitochondrial {ECO:0000305};
DE Short=SQOR;
DE EC=1.8.5.8 {ECO:0000250|UniProtKB:Q9Y6N5};
DE AltName: Full=Sulfide quinone oxidoreductase {ECO:0000250|UniProtKB:Q9Y6N5};
DE Flags: Precursor;
GN Name=Sqor {ECO:0000250|UniProtKB:Q9Y6N5};
GN Synonyms=Sqrdl {ECO:0000312|MGI:MGI:1929899};
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 STRAIN=C57BL/6 X CBA; TISSUE=Liver;
RA Huang L., Gitschier J.;
RT "Positional cloning of the pallid gene in the pallid mutant.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Small intestine;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343, AND IDENTIFICATION BY
RP 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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-134 AND LYS-173, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Catalyzes the oxidation of hydrogen sulfide with the help of
CC a quinone, such as ubiquinone-10, giving rise to thiosulfate and
CC ultimately to sulfane (molecular sulfur) atoms. Requires an additional
CC electron acceptor; can use sulfite, sulfide or cyanide (in vitro). It
CC is believed the in vivo electron acceptor is glutathione.
CC {ECO:0000250|UniProtKB:Q9Y6N5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + hydrogen sulfide + sulfite + ubiquinone-10 =
CC thiosulfate + ubiquinol-10; Xref=Rhea:RHEA:38359, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:33542,
CC ChEBI:CHEBI:46245, ChEBI:CHEBI:64183;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6N5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38360;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6N5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + glutathione + H(+) + hydrogen sulfide = a quinol +
CC S-sulfanylglutathione; Xref=Rhea:RHEA:55156, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24646, ChEBI:CHEBI:29919, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:58905, ChEBI:CHEBI:132124; EC=1.8.5.8;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6N5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55157;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6N5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + H(+) + hydrogen sulfide + ubiquinone-10 = S-
CC sulfanylglutathione + ubiquinol-10; Xref=Rhea:RHEA:62608,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29919, ChEBI:CHEBI:46245,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58905, ChEBI:CHEBI:64183;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6N5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62609;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6N5};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6N5};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:Q9Y6N5};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9Y6N5}.
CC -!- SIMILARITY: Belongs to the SQRD family. {ECO:0000305}.
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DR EMBL; AF174535; AAD50300.1; -; mRNA.
DR EMBL; AK008290; BAB25580.1; -; mRNA.
DR EMBL; AK075598; BAC35847.1; -; mRNA.
DR EMBL; AL928950; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011153; AAH11153.1; -; mRNA.
DR CCDS; CCDS16669.1; -.
DR RefSeq; NP_001155975.1; NM_001162503.1.
DR RefSeq; NP_067482.4; NM_021507.5.
DR RefSeq; XP_006500029.1; XM_006499966.1.
DR AlphaFoldDB; Q9R112; -.
DR SMR; Q9R112; -.
DR BioGRID; 208481; 6.
DR IntAct; Q9R112; 2.
DR MINT; Q9R112; -.
DR STRING; 10090.ENSMUSP00000106133; -.
DR iPTMnet; Q9R112; -.
DR PhosphoSitePlus; Q9R112; -.
DR SwissPalm; Q9R112; -.
DR EPD; Q9R112; -.
DR jPOST; Q9R112; -.
DR MaxQB; Q9R112; -.
DR PaxDb; Q9R112; -.
DR PeptideAtlas; Q9R112; -.
DR PRIDE; Q9R112; -.
DR ProteomicsDB; 261583; -.
DR DNASU; 59010; -.
DR Ensembl; ENSMUST00000005953; ENSMUSP00000005953; ENSMUSG00000005803.
DR Ensembl; ENSMUST00000110506; ENSMUSP00000106133; ENSMUSG00000005803.
DR GeneID; 59010; -.
DR KEGG; mmu:59010; -.
DR UCSC; uc008mbh.2; mouse.
DR CTD; 58472; -.
DR MGI; MGI:1929899; Sqor.
DR VEuPathDB; HostDB:ENSMUSG00000005803; -.
DR eggNOG; KOG3851; Eukaryota.
DR GeneTree; ENSGT00390000019406; -.
DR HOGENOM; CLU_030742_2_1_1; -.
DR InParanoid; Q9R112; -.
DR OMA; FPWVYYN; -.
DR OrthoDB; 1267127at2759; -.
DR PhylomeDB; Q9R112; -.
DR TreeFam; TF314384; -.
DR Reactome; R-MMU-1614517; Sulfide oxidation to sulfate.
DR BioGRID-ORCS; 59010; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Sqor; mouse.
DR PRO; PR:Q9R112; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9R112; protein.
DR Bgee; ENSMUSG00000005803; Expressed in right colon and 201 other tissues.
DR ExpressionAtlas; Q9R112; baseline and differential.
DR Genevisible; Q9R112; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0071949; F:FAD binding; IBA:GO_Central.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0070224; F:sulfide:quinone oxidoreductase activity; ISS:UniProtKB.
DR GO; GO:0070813; P:hydrogen sulfide metabolic process; ISS:UniProtKB.
DR GO; GO:0070221; P:sulfide oxidation, using sulfide:quinone oxidoreductase; ISS:UniProtKB.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR015904; Sulphide_quinone_reductase.
DR PANTHER; PTHR10632; PTHR10632; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Acetylation; Disulfide bond; FAD; Flavoprotein; Mitochondrion;
KW Oxidoreductase; Phosphoprotein; Quinone; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..450
FT /note="Sulfide:quinone oxidoreductase, mitochondrial"
FT /id="PRO_0000022409"
FT ACT_SITE 201
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N5"
FT ACT_SITE 379
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N5"
FT BINDING 53..54
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N5"
FT BINDING 75
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N5"
FT BINDING 83
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N5"
FT BINDING 118
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N5"
FT BINDING 336
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N5"
FT BINDING 344..347
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N5"
FT MOD_RES 134
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 173
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT DISULFID 201..379
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N5"
FT CONFLICT 6
FT /note="T -> A (in Ref. 3; AAH11153)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="S -> T (in Ref. 2; BAB25580)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="G -> D (in Ref. 1; AAD50300 and 3; AAH11153)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="F -> L (in Ref. 1; AAD50300)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 450 AA; 50282 MW; CBA500CE60803C8F CRC64;
MAPLVTVVSS PRARLFACFL RLGTQQAGPL QLHTGACCTA KNHYEVLVLG GGAGGITMAT
RMKRRVGAEN VAIVEPSERH FYQPIWTLVG AGAKELSLSV RSTLSVIPSG VQWIQDRVAE
LNPDENCIRT DSGKEISYRY LIIALGIQLD YEKIKGLPEG FAYPKIGSNY SVKTVEKTWK
ALQGFKEGNA LFTFPNTPVK CAGAPQKIMY LSEAYFRKTG KRPKANIIFN TALGTIFGVK
KYADALQEII RERDVSVNYK HNLIEVRPDK QEAVFEILDK PGETHVIPYE MLHVTPPMSA
PDVLKRSPVA DSAGWVDVDK ETLQHKKYPN VFGIGDCTNL PTSKTAAAVA AQSGILDRTM
CLIMKNQRPI KKYDGYTSCP LVTGYNRVIL AEFDYTAQPL ETFPFDQSKE RITMYLMKAD
MMPFLYWNMM LRGYWGGPAF LRKLFHLGMN
