SUOX_DROME
ID SUOX_DROME Reviewed; 573 AA.
AC Q9VWP4;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Sulfite oxidase, mitochondrial {ECO:0000305};
DE EC=1.8.3.1 {ECO:0000269|PubMed:30158546};
DE AltName: Full=Protein shopper {ECO:0000303|PubMed:30158546};
DE Flags: Precursor;
GN Name=shop {ECO:0000303|PubMed:30158546, ECO:0000312|FlyBase:FBgn0030966};
GN ORFNames=CG7280 {ECO:0000312|FlyBase:FBgn0030966};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=30158546; DOI=10.1038/s41467-018-05645-z;
RA Otto N., Marelja Z., Schoofs A., Kranenburg H., Bittern J., Yildirim K.,
RA Berh D., Bethke M., Thomas S., Rode S., Risse B., Jiang X., Pankratz M.,
RA Leimkuehler S., Klaembt C.;
RT "The sulfite oxidase Shopper controls neuronal activity by regulating
RT glutamate homeostasis in Drosophila ensheathing glia.";
RL Nat. Commun. 9:3514-3514(2018).
CC -!- FUNCTION: Required in ensheathing glial cells for normal larval
CC locomotion. Oxidizes sulfite which is required to maintain glutamate
CC homeostasis and as a consequence, neuronal network function.
CC {ECO:0000269|PubMed:30158546}.
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:0000269|PubMed:30158546};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:P51687};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently
CC per subunit. {ECO:0000250|UniProtKB:P51687};
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:0000269|PubMed:30158546}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the ensheathing glia with relatively
CC weak expression in the CNS cortex (at protein level).
CC {ECO:0000269|PubMed:30158546}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in larvae results in
CC reduced levels of sulfite oxidase activity. RNAi-mediated knockdown in
CC ensheathing glial cells results in larval locamotion defects, including
CC reduced run phases with more stops and an increase in head bending
CC frequency. RNAi-mediated knockdown in the cortex glia, astrocytes or
CC neurons has no effect on locomotion or head bending frequency.
CC {ECO:0000269|PubMed:30158546}.
CC -!- MISCELLANEOUS: Named 'shopper' because of the mutant locomotion
CC phenotype in which larvae stop and bend their heads more frequently.
CC {ECO:0000303|PubMed:30158546}.
CC -!- CAUTION: It is not obvious if the molybdenum-pterin domain is
CC functional; the conserved cysteine (position 339) is replaced by an
CC isoleucine. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014298; AAF48894.1; -; Genomic_DNA.
DR EMBL; AY069352; AAL39497.1; -; mRNA.
DR RefSeq; NP_573331.1; NM_133103.3.
DR AlphaFoldDB; Q9VWP4; -.
DR SMR; Q9VWP4; -.
DR BioGRID; 59187; 2.
DR STRING; 7227.FBpp0074426; -.
DR PaxDb; Q9VWP4; -.
DR PRIDE; Q9VWP4; -.
DR DNASU; 32878; -.
DR EnsemblMetazoa; FBtr0074655; FBpp0074426; FBgn0030966.
DR GeneID; 32878; -.
DR KEGG; dme:Dmel_CG7280; -.
DR UCSC; CG7280-RA; d. melanogaster.
DR CTD; 32878; -.
DR FlyBase; FBgn0030966; shop.
DR VEuPathDB; VectorBase:FBgn0030966; -.
DR eggNOG; KOG0535; Eukaryota.
DR eggNOG; KOG4576; Eukaryota.
DR GeneTree; ENSGT00390000003749; -.
DR HOGENOM; CLU_003827_5_1_1; -.
DR InParanoid; Q9VWP4; -.
DR OMA; WARHVQF; -.
DR OrthoDB; 804989at2759; -.
DR PhylomeDB; Q9VWP4; -.
DR Reactome; R-DME-1614517; Sulfide oxidation to sulfate.
DR UniPathway; UPA00096; -.
DR BioGRID-ORCS; 32878; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 32878; -.
DR PRO; PR:Q9VWP4; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0030966; Expressed in arthropod fat body and 25 other tissues.
DR Genevisible; Q9VWP4; DM.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISS:FlyBase.
DR GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IBA:GO_Central.
DR GO; GO:0008482; F:sulfite oxidase activity; IDA:FlyBase.
DR GO; GO:0007584; P:response to nutrient; ISS:FlyBase.
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 Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF03404; Mo-co_dimer; 1.
DR Pfam; PF00174; Oxidored_molyb; 1.
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.
PE 1: Evidence at protein level;
KW Heme; Iron; Metal-binding; Mitochondrion; Molybdenum; Oxidoreductase;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 35..573
FT /note="Sulfite oxidase, mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000006485"
FT DOMAIN 108..186
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT REGION 14..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..199
FT /note="Hinge"
FT /evidence="ECO:0000250"
FT REGION 200..423
FT /note="Moco domain"
FT /evidence="ECO:0000250"
FT REGION 424..567
FT /note="Homodimerization"
FT /evidence="ECO:0000250"
FT COMPBIAS 14..28
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 168
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 240..244
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250"
FT BINDING 287
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"
FT BINDING 344
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250"
FT BINDING 383
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250"
FT BINDING 388
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250"
FT BINDING 399..401
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250"
SQ SEQUENCE 573 AA; 64346 MW; 71AB1D2B3465D811 CRC64;
MRLLRPSWAG LLRGRHHQHQ RHHRRLLLTT SRGSNGEREE QQHSQWSSPG SRSEQLFYAA
FWAGGLTLGY HWLTDKKNHV LLEGQKVASE EELEATARLW HVTNRRELPT YRAEEVEQHN
SVEKRIWVTY GLGVYDVTDF VENHPGGDKI LMAAGSAIDP FWGIYQQHNT LEVLELLEGF
RIGNLEGLVV TNVDDELGSP WSQEPQRHAL LKPASKRPFN AEPPIGLLAE QFYTPNELFY
VRNHLPVPVI NPEDYELEIE GGAKDKTLTL DGIKALPKHS VTAAIMCGGN RRSEMTKVKA
VKGLSWGAGA VGNAKWSGAR LCDILREQGV QPDETKHVIF EGADLDPTSH PYGASIPLAK
ALDPRGDVIL AYEMNDEPLS RDHGFPIRVI VPGTVGARNV KWLTRIVVAD KESDSHWQQN
DYKGFSPSTD WDTVDFSKSD AIQAMPVTSA ICTPQPGARV KVDDDEGHIT VRGYAWSGGG
RKIVRVDLTN DEGVSWHVAE LEQEEMPDGR HYGWSLWTAR LPVSEAQRRA GDVEIWAKAV
DSAYNVQPEK FEHIWNLRGV LANAYHKVKV KII
