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Q8R086 (SUOX_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sulfite oxidase, mitochondrial
EC=1.8.3.1
Gene names
Name:Suox
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length546 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Sulfite + O2 + H2O = sulfate + H2O2.

Cofactor

Binds 1 protoheme group By similarity.

Molybdenum (molybdopterin) By similarity.

Pathway

Energy metabolism; sulfur metabolism.

Subunit structure

Homodimer.

Subcellular location

Mitochondrion intermembrane space.

Sequence similarities

Contains 1 cytochrome b5 heme-binding domain.

Sequence caution

The sequence BAE32710.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 8080Mitochondrion By similarity
Chain81 – 546466Sulfite oxidase, mitochondrial
PRO_0000006483

Regions

Domain83 – 16280Cytochrome b5 heme-binding
Region166 – 18217Hinge By similarity
Region183 – 546364Molybdenum-pterin domain By similarity
Region216 – 2205Molybdenum-pterin-binding By similarity
Region321 – 3233Molybdenum-pterin-binding By similarity
Region367 – 38014Molybdenum-pterin-binding By similarity

Sites

Metal binding1191Iron (heme axial ligand) By similarity
Metal binding1441Iron (heme axial ligand) By similarity
Metal binding2651Molybdenum-pterin By similarity
Metal binding3181Molybdenum-pterin By similarity

Amino acid modifications

Modified residue2861Phosphothreonine Ref.3

Experimental info

Sequence conflict4551G → S in BAE28865. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8R086 [UniParc].

Last modified July 10, 2007. Version 2.
Checksum: A10ADF73FFA8DE51

FASTA54660,756
        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

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Liver.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.
[3]"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry."
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.
J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-286, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK149422 mRNA. Translation: BAE28865.1.
AK154608 mRNA. Translation: BAE32710.1. Different initiation.
BC027197 mRNA. Translation: AAH27197.2.
IPIIPI00153144.
RefSeqNP_776094.2. NM_173733.3.
UniGeneMm.23352.

3D structure databases

ProteinModelPortalQ8R086.
SMRQ8R086. Positions 82-544.
ModBaseSearch...

Protein-protein interaction databases

IntActQ8R086. 1 interaction.

PTM databases

PhosphoSiteQ8R086.

2D gel databases

REPRODUCTION-2DPAGEQ8R086.

Proteomic databases

PaxDbQ8R086.
PRIDEQ8R086.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000054764; ENSMUSP00000056195; ENSMUSG00000049858.
GeneID211389.
KEGGmmu:211389.
UCSCuc007hnt.2. mouse.

Organism-specific databases

CTD6821.
MGIMGI:2446117. Suox.

Phylogenomic databases

eggNOGCOG2041.
GeneTreeENSGT00390000003749.
HOGENOMHOG000252609.
HOVERGENHBG017865.
InParanoidQ8R086.
KOK00387.
OMAEMTQVKE.
OrthoDBEOG46Q6SF.

Enzyme and pathway databases

UniPathwayUPA00096.

Gene expression databases

BgeeQ8R086.
CleanExMM_SUOX.
GenevestigatorQ8R086.
GermOnlineENSMUSG00000049858. Mus musculus.

Family and domain databases

Gene3D2.60.40.650. 1 hit.
3.10.120.10. 1 hit.
3.90.420.10. 1 hit.
InterProIPR001199. Cyt_B5-like_heme/steroid-bd.
IPR018506. Cyt_B5_heme-BS.
IPR014756. Ig_E-set.
IPR005066. MoCF_OxRdtse_dimer.
IPR008335. Mopterin_OxRdtase_euk.
IPR000572. OxRdtase_Mopterin-bd_dom.
IPR022407. OxRdtase_Mopterin_BS.
[Graphical view]
PfamPF00173. Cyt-b5. 1 hit.
PF03404. Mo-co_dimer. 1 hit.
PF00174. Oxidored_molyb. 1 hit.
[Graphical view]
PRINTSPR00363. CYTOCHROMEB5.
PR00407. EUMOPTERIN.
SUPFAMSSF55856. Cyt_B5. 1 hit.
SSF81296. Ig_E-set. 1 hit.
SSF56524. Oxidored_molyb. 1 hit.
PROSITEPS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio373222.
SOURCESearch...

Entry information

Entry nameSUOX_MOUSE
AccessionPrimary (citable) accession number: Q8R086
Secondary accession number(s): Q3U3S5, Q3UEP6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: July 10, 2007
Last modified: April 3, 2013
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents