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UniProtKB/Swiss-Prot entry Q8R086


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SUOX_MOUSE
Primary accession number Q8R086
Secondary accession numbers Q3U3S5 Q3UEP6
Integrated into Swiss-Prot on June 20, 2003
Sequence was last modified on July 10, 2007 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 55)
Name and origin of the protein
Protein name Sulfite oxidase, mitochondrial [Precursor]
Synonym EC 1.8.3.1
Gene name
Name: Suox
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD;
TISSUE=Liver;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-286, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1021/pr0604155; PubMed=17203969 [NCBI, ExPASy, EBI, Israel, Japan]
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry.";
J. Proteome Res. 6:250-262(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AK149422; BAE28865.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK154608; BAE32710.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC027197; AAH27197.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_776094.2; -.
UniGene Mm.23352
3D structure databases
HSSP P51687; 1MJ4. [HSSP ENTRY / PDB]
ModBase Q8R086.
Protein-protein interaction databases
IntAct Q8R086; -.
PTM databases
PhosphoSite Q8R086; -.
2D gel databases
REPRODUCTION-2DPAGE Q8R086; -.
Organism-specific databases
MGI MGI:2446117; Suox.
Gene expression databases
ArrayExpress Q8R086; -.
CleanEx MM_SUOX; -.
GermOnline ENSMUSG00000049858; Mus musculus.
Ontologies
GO
GO:0005758; Cellular component: mitochondrial intermembrane space (inferred from electronic annotation from UniProtKB-SubCell).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037; Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030151; Molecular function: molybdenum ion binding (inferred from electronic annotation from InterPro).
GO:0008482; Molecular function: sulfite oxidase activity (inferred from electronic annotation from EC).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001199; Cyt_B5.
IPR005066; MoCF_OxRdtse_dimer.
IPR008335; Mopterin_OxRdtase_euk.
IPR000572; OxRdtase_Mopterin-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.10.120.10; Cyt_B5; 1.
G3DSA:2.60.40.650; MoCF_oxrdtse_dimer; 1.
G3DSA:3.90.420.10; Oxred_molyb_bd; 1.
Pfam PF00173; Cyt-b5; 1.
PF03404; Mo-co_dimer; 1.
PF00174; Oxidored_molyb; 1.
Pfam graphical view of domain structure.
PRINTS PR00363; CYTOCHROMEB5.
PR00407; EUMOPTERIN.
ProDom PD000612; Cyt_B5; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00191; CYTOCHROME_B5_1; 1.
PS50255; CYTOCHROME_B5_2; 1.
PS00559; MOLYBDOPTERIN_EUK; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q8R086.
Genome annotation databases
Ensembl ENSMUSG00000049858; Mus musculus. [Contig view]
GeneID 211389; -.
KEGG mmu:211389; -.
Phylogenomic databases
HOVERGEN Q8R086; -.
Other
NextBio 373222; -.
SOURCE Suox; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Heme; Iron; Metal-binding; Mitochondrion; Molybdenum; Oxidoreductase; Phosphoprotein; Transit peptide.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    80  80     Mitochondrion (By similarity). 
CHAIN   81   546  466     Sulfite oxidase, mitochondrial. PRO_0000006483
DOMAIN   83   162  80     Cytochrome b5 heme-binding. 
REGION   166   182  17     Hinge (By similarity). 
REGION   183   546  364     Molybdenum-pterin domain (By similarity). 
REGION   216   220  5     Molybdenum-pterin-binding (By similarity). 
REGION   321   323  3     Molybdenum-pterin-binding (By similarity). 
REGION   367   380  14     Molybdenum-pterin-binding (By similarity). 
METAL   119   119        Iron (heme axial ligand) (By similarity). 
METAL   144   144        Iron (heme axial ligand) (By similarity). 
METAL   265   265        Molybdenum-pterin (By similarity). 
METAL   318   318        Molybdenum-pterin (By similarity). 
MOD_RES   286   286        Phosphothreonine. 
CONFLICT   455   455        G -> S (in Ref. 1; BAE28865). 
Sequence information
Length: 546 AA [This is the length of the unprocessed precursor] Molecular weight: 60756 Da [This is the MW of the unprocessed precursor] CRC64: A10ADF73FFA8DE51 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLLQLYRSVV VRLPQAIRVK STPLRLCIQA CSTNDSLEPQ HPSLTFSDDN SRTRRWKVMG 

        70         80         90        100        110        120 
TLLGLGVVLV YHEHRCRASQ ESPRMYSKED VRSHNNPKTG VWVTLGSEVF DVTKFVDLHP 

       130        140        150        160        170        180 
GGPSKLMLAA GGPLEPFWAL YAVHNQPHVR ELLAEYKIGE LNPEDSMSPS VEASDPYADD 

       190        200        210        220        230        240 
PIRHPALRIN SQRPFNAEPP PELLTEGYIT PNPIFFTRNH LPVPNLDPHT YRLHVVGAPG 

       250        260        270        280        290        300 
GQSLSLSLDD LHKFPKHEVT VTLQCAGNRR SEMSKVKEVK GLEWRTGAIS TARWAGARLC 

       310        320        330        340        350        360 
DVLAQAGHRL CDSEAHVCFE GLDSDPTGTA YGASIPLARA MDPEAEVLLA YEMNGQPLPR 

       370        380        390        400        410        420 
DHGFPVRVVV PGVVGARHVK WLGRVSVESE ESYSHWQRRD YKGFSPSVDW DTVNFDLAPS 

       430        440        450        460        470        480 
IQELPIQSAI TQPQDGAIVE SGEVTIKGYA WSGGGRAVIR VDVSVDGGLT WQEAELEGEE 

       490        500        510        520        530        540 
QCPRKAWAWR IWQLKAQVPA EQKELNIICK AVDDSYNVQP DTVAPIWNLR GVLSNAWHRV 


HVQVVP 

Q8R086 in FASTA format

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View entry in raw text format (no links)
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