SUOX_MOUSE
ID SUOX_MOUSE Reviewed; 546 AA.
AC Q8R086; Q3U3S5; Q3UEP6;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Sulfite oxidase, mitochondrial;
DE EC=1.8.3.1;
DE Flags: Precursor;
GN Name=Suox;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Liver;
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 [2]
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC 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).
CC -!- FUNCTION: Catalyzes the oxidation of sulfite to sulfate, the terminal
CC reaction in the oxidative degradation of sulfur-containing amino acids.
CC {ECO:0000250|UniProtKB:Q07116}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + sulfite = H2O2 + sulfate; Xref=Rhea:RHEA:24600,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16189,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17359; EC=1.8.3.1;
CC Evidence={ECO:0000250|UniProtKB:Q07116};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24601;
CC Evidence={ECO:0000250|UniProtKB:Q07116};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:Q07116};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently
CC per subunit. {ECO:0000250|UniProtKB:Q07116};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC Evidence={ECO:0000250|UniProtKB:Q07116};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000250|UniProtKB:Q07116};
CC -!- PATHWAY: Energy metabolism; sulfur metabolism.
CC {ECO:0000250|UniProtKB:Q07116}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q07116}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000250|UniProtKB:Q07116}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE32710.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK149422; BAE28865.1; -; mRNA.
DR EMBL; AK154608; BAE32710.1; ALT_INIT; mRNA.
DR EMBL; BC027197; AAH27197.2; -; mRNA.
DR CCDS; CCDS24285.1; -.
DR RefSeq; NP_776094.2; NM_173733.3.
DR AlphaFoldDB; Q8R086; -.
DR SMR; Q8R086; -.
DR BioGRID; 229229; 1.
DR IntAct; Q8R086; 1.
DR STRING; 10090.ENSMUSP00000056195; -.
DR iPTMnet; Q8R086; -.
DR PhosphoSitePlus; Q8R086; -.
DR SwissPalm; Q8R086; -.
DR REPRODUCTION-2DPAGE; Q8R086; -.
DR EPD; Q8R086; -.
DR jPOST; Q8R086; -.
DR MaxQB; Q8R086; -.
DR PaxDb; Q8R086; -.
DR PeptideAtlas; Q8R086; -.
DR PRIDE; Q8R086; -.
DR ProteomicsDB; 257508; -.
DR Antibodypedia; 27840; 385 antibodies from 29 providers.
DR DNASU; 211389; -.
DR Ensembl; ENSMUST00000054764; ENSMUSP00000056195; ENSMUSG00000049858.
DR GeneID; 211389; -.
DR KEGG; mmu:211389; -.
DR UCSC; uc007hnt.2; mouse.
DR CTD; 6821; -.
DR MGI; MGI:2446117; Suox.
DR VEuPathDB; HostDB:ENSMUSG00000049858; -.
DR eggNOG; KOG0535; Eukaryota.
DR eggNOG; KOG4576; Eukaryota.
DR GeneTree; ENSGT00390000003749; -.
DR HOGENOM; CLU_003827_5_1_1; -.
DR InParanoid; Q8R086; -.
DR OMA; WARHVQF; -.
DR OrthoDB; 804989at2759; -.
DR PhylomeDB; Q8R086; -.
DR TreeFam; TF300905; -.
DR Reactome; R-MMU-1614517; Sulfide oxidation to sulfate.
DR UniPathway; UPA00096; -.
DR BioGRID-ORCS; 211389; 3 hits in 71 CRISPR screens.
DR PRO; PR:Q8R086; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8R086; protein.
DR Bgee; ENSMUSG00000049858; Expressed in seminal vesicle and 215 other tissues.
DR Genevisible; Q8R086; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0020037; F:heme binding; ISO:MGI.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0043546; F:molybdopterin cofactor binding; ISO:MGI.
DR GO; GO:0008482; F:sulfite oxidase activity; ISO:MGI.
DR GO; GO:0007584; P:response to nutrient; ISO:MGI.
DR GO; GO:0006790; P:sulfur compound metabolic process; IBA:GO_Central.
DR Gene3D; 3.10.120.10; -; 1.
DR Gene3D; 3.90.420.10; -; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR018506; Cyt_B5_heme-BS.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR005066; MoCF_OxRdtse_dimer.
DR InterPro; IPR008335; Mopterin_OxRdtase_euk.
DR InterPro; IPR000572; OxRdtase_Mopterin-bd_dom.
DR InterPro; IPR036374; OxRdtase_Mopterin-bd_sf.
DR InterPro; IPR022407; OxRdtase_Mopterin_BS.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF03404; Mo-co_dimer; 1.
DR Pfam; PF00174; Oxidored_molyb; 1.
DR PRINTS; PR00363; CYTOCHROMEB5.
DR PRINTS; PR00407; EUMOPTERIN.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
DR SUPFAM; SSF56524; SSF56524; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR PROSITE; PS00559; MOLYBDOPTERIN_EUK; 1.
PE 1: Evidence at protein level;
KW Heme; Iron; Metal-binding; Mitochondrion; Molybdenum; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..80
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:Q07116"
FT CHAIN 81..546
FT /note="Sulfite oxidase, mitochondrial"
FT /id="PRO_0000006483"
FT DOMAIN 83..162
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT REGION 166..175
FT /note="Hinge"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT REGION 176..402
FT /note="Moco domain"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT REGION 403..539
FT /note="Homodimerization"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT BINDING 119
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 144
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 146
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:P51687"
FT BINDING 148
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT BINDING 216..220
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT BINDING 265
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT BINDING 323
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT BINDING 362
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT BINDING 367
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT BINDING 378..380
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51687"
FT CONFLICT 455
FT /note="G -> S (in Ref. 1; BAE28865)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 546 AA; 60756 MW; A10ADF73FFA8DE51 CRC64;
MLLQLYRSVV VRLPQAIRVK STPLRLCIQA CSTNDSLEPQ HPSLTFSDDN SRTRRWKVMG
TLLGLGVVLV YHEHRCRASQ ESPRMYSKED VRSHNNPKTG VWVTLGSEVF DVTKFVDLHP
GGPSKLMLAA GGPLEPFWAL YAVHNQPHVR ELLAEYKIGE LNPEDSMSPS VEASDPYADD
PIRHPALRIN SQRPFNAEPP PELLTEGYIT PNPIFFTRNH LPVPNLDPHT YRLHVVGAPG
GQSLSLSLDD LHKFPKHEVT VTLQCAGNRR SEMSKVKEVK GLEWRTGAIS TARWAGARLC
DVLAQAGHRL CDSEAHVCFE GLDSDPTGTA YGASIPLARA MDPEAEVLLA YEMNGQPLPR
DHGFPVRVVV PGVVGARHVK WLGRVSVESE ESYSHWQRRD YKGFSPSVDW DTVNFDLAPS
IQELPIQSAI TQPQDGAIVE SGEVTIKGYA WSGGGRAVIR VDVSVDGGLT WQEAELEGEE
QCPRKAWAWR IWQLKAQVPA EQKELNIICK AVDDSYNVQP DTVAPIWNLR GVLSNAWHRV
HVQVVP
