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 29-MAY-2013, entry version 93.
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;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; 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.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA 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.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-286, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=17203969; DOI=10.1021/pr0604155;
RA Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT "Protein phosphorylation and expression profiling by Yin-yang
RT multidimensional liquid chromatography (Yin-yang MDLC) mass
RT spectrometry.";
RL J. Proteome Res. 6:250-262(2007).
CC -!- CATALYTIC ACTIVITY: Sulfite + O(2) + H(2)O = sulfate + H(2)O(2).
CC -!- COFACTOR: Binds 1 protoheme group (By similarity).
CC -!- COFACTOR: Molybdenum (molybdopterin) (By similarity).
CC -!- PATHWAY: Energy metabolism; sulfur metabolism.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC -!- SIMILARITY: Contains 1 cytochrome b5 heme-binding domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE32710.1; Type=Erroneous initiation;
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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 IPI; IPI00153144; -.
DR RefSeq; NP_776094.2; NM_173733.3.
DR UniGene; Mm.23352; -.
DR ProteinModelPortal; Q8R086; -.
DR SMR; Q8R086; 82-544.
DR IntAct; Q8R086; 1.
DR MINT; MINT-1860734; -.
DR PhosphoSite; Q8R086; -.
DR REPRODUCTION-2DPAGE; Q8R086; -.
DR PaxDb; Q8R086; -.
DR PRIDE; Q8R086; -.
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 eggNOG; COG2041; -.
DR GeneTree; ENSGT00390000003749; -.
DR HOGENOM; HOG000252609; -.
DR HOVERGEN; HBG017865; -.
DR InParanoid; Q8R086; -.
DR KO; K00387; -.
DR OMA; EMTQVKE; -.
DR OrthoDB; EOG46Q6SF; -.
DR UniPathway; UPA00096; -.
DR NextBio; 373222; -.
DR Bgee; Q8R086; -.
DR CleanEx; MM_SUOX; -.
DR Genevestigator; Q8R086; -.
DR GermOnline; ENSMUSG00000049858; Mus musculus.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0008482; F:sulfite oxidase activity; IEA:EC.
DR GO; GO:0006790; P:sulfur compound metabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.60.40.650; -; 1.
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; 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; 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 SUPFAM; SSF55856; Cyt_B5; 1.
DR SUPFAM; SSF81296; Ig_E-set; 1.
DR SUPFAM; SSF56524; Oxidored_molyb; 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 Complete proteome; Heme; Iron; Metal-binding; Mitochondrion;
KW Molybdenum; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Transit peptide.
FT TRANSIT 1 80 Mitochondrion (By similarity).
FT CHAIN 81 546 Sulfite oxidase, mitochondrial.
FT /FTId=PRO_0000006483.
FT DOMAIN 83 162 Cytochrome b5 heme-binding.
FT REGION 166 182 Hinge (By similarity).
FT REGION 183 546 Molybdenum-pterin domain (By similarity).
FT REGION 216 220 Molybdenum-pterin-binding (By
FT similarity).
FT REGION 321 323 Molybdenum-pterin-binding (By
FT similarity).
FT REGION 367 380 Molybdenum-pterin-binding (By
FT similarity).
FT METAL 119 119 Iron (heme axial ligand) (By similarity).
FT METAL 144 144 Iron (heme axial ligand) (By similarity).
FT METAL 265 265 Molybdenum-pterin (By similarity).
FT METAL 318 318 Molybdenum-pterin (By similarity).
FT MOD_RES 286 286 Phosphothreonine.
FT CONFLICT 455 455 G -> S (in Ref. 1; BAE28865).
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
//
