Reviewed, UniProtKB/Swiss-Prot Q8R086 (SUOX_MOUSE)

Names and origin

Protein names

Recommended name:
    Sulfite oxidase, mitochondrial
    EC=1.8.3.1

Gene names

Name:

Suox

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	546 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Heme Iron Metal-binding Molybdenum
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial intermembrane space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro molybdenum ion binding Inferred from electronic annotation. Source: UniProtKB-KW sulfite oxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 80	80	Mitochondrion By similarity
	Chain	81 – 546	466	Sulfite oxidase, mitochondrial		PRO_0000006483
Regions
	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
Sites
	Metal binding	119	1	Iron (heme axial ligand) By similarity
	Metal binding	144	1	Iron (heme axial ligand) By similarity
	Metal binding	265	1	Molybdenum-pterin By similarity
	Metal binding	318	1	Molybdenum-pterin By similarity
Amino acid modifications
	Modified residue	286	1	Phosphothreonine Ref.3
Experimental info
	Sequence conflict	455	1	G → S in BAE28865. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8R086-1 [UniParc]. Last modified July 10, 2007. Version 2. Checksum: A10ADF73FFA8DE51	FASTA	546	60,756
	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

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. , 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: 16141072] [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: 15489334] [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: 17203969] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-286, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK149422 mRNA. Translation: BAE28865.1. AK154608 mRNA. Translation: BAE32710.1. Different initiation. BC027197 mRNA. Translation: AAH27197.1. Different initiation.
IPI	IPI00153144.
RefSeq	NP_776094.2.
UniGene	Mm.23352
3D structure databases
HSSP	HSSP built from PDB template 1MJ4 based on UniProtKB P51687.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8R086. 1 interaction.
PTM databases
PhosphoSite	Q8R086.
2-D gel databases
REPRODUCTION-2DPAGE	Q8R086.
Genome annotation databases
Ensembl	ENSMUSG00000049858. Mus musculus. [Contig view]
GeneID	211389.
KEGG	mmu:211389.
Organism-specific databases
MGI	MGI:2446117. Suox.
Phylogenomic databases
HOVERGEN	Q8R086.
OMA	Q8R086. RAVIRVD.
Enzyme and pathway databases
BRENDA	1.8.3.1. 244.
Gene expression databases
ArrayExpress	Q8R086.
Bgee	Q8R086.
CleanEx	MM_SUOX.
GermOnline	ENSMUSG00000049858. Mus musculus.
Family and domain databases
InterPro	IPR001199. Cyt_B5. IPR018506. Cyt_B5_heme-BS. IPR005066. MoCF_OxRdtse_dimer. IPR008335. Mopterin_OxRdtase_euk. IPR000572. OxRdtase_Mopterin-bd. [Graphical view]
Gene3D	G3DSA:3.10.120.10. Cyt_B5. 1 hit. G3DSA:2.60.40.650. MoCF_oxrdtse_dimer. 1 hit. G3DSA:3.90.420.10. Oxred_molyb_bd. 1 hit.
Pfam	PF00173. Cyt-b5. 1 hit. PF03404. Mo-co_dimer. 1 hit. PF00174. Oxidored_molyb. 1 hit. [Graphical view]
PRINTS	PR00363. CYTOCHROMEB5. PR00407. EUMOPTERIN.
ProDom	PD000612. Cyt_B5. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00191. CYTOCHROME_B5_1. 1 hit. PS50255. CYTOCHROME_B5_2. 1 hit. PS00559. MOLYBDOPTERIN_EUK. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	373222.
SOURCE	Search...

Entry information

Entry name

SUOX_MOUSE

Accession

Primary (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:	June 16, 2009
This is version 62 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)