ERV1_ORYSJ
ID ERV1_ORYSJ Reviewed; 194 AA.
AC Q10Q80;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=FAD-linked sulfhydryl oxidase ERV1 {ECO:0000305};
DE EC=1.8.3.2 {ECO:0000305};
DE AltName: Full=Mitochondrial sulfhydryl oxidase ERV1 {ECO:0000305};
GN Name=ERV1 {ECO:0000305};
GN OrderedLocusNames=Os03g0206300 {ECO:0000312|EMBL:BAS82866.1},
GN LOC_Os03g10850 {ECO:0000312|EMBL:ABF94551.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
CC -!- FUNCTION: FAD-dependent sulfhydryl oxidase that catalyzes disulfide
CC bond formation (By similarity). Required for the import and folding of
CC small cysteine-containing proteins in the mitochondrial intermembrane
CC space. Forms a redox cycle with MIA40 that involves a disulfide relay
CC system. Important for maintaining the cysteine residues in MIA40 in an
CC oxidized state (By similarity). {ECO:0000250|UniProtKB:P27882,
CC ECO:0000255|PROSITE-ProRule:PRU00654}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + 2 R'C(R)SH = H2O2 + R'C(R)S-S(R)CR';
CC Xref=Rhea:RHEA:17357, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:16520, ChEBI:CHEBI:17412; EC=1.8.3.2;
CC Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Note=FAD. {ECO:0000255|PROSITE-ProRule:PRU00654};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8GXX0}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q8GXX0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q10Q80-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q10Q80-2; Sequence=VSP_058587, VSP_058588;
CC -!- PTM: Contains three disulfide bonds; one catalytic disulfide (Cys-119
CC to Cys-122), one structural disulfide (Cys-148 to Cys-165), and one
CC shuttle disulfide (Cys-177 to Cys-182). {ECO:0000250|UniProtKB:Q8GXX0}.
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DR EMBL; DP000009; ABF94551.1; -; Genomic_DNA.
DR EMBL; AP008209; BAH92037.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS82866.1; -; Genomic_DNA.
DR EMBL; AK102625; BAG95646.1; -; mRNA.
DR RefSeq; XP_015628639.1; XM_015773153.1. [Q10Q80-1]
DR AlphaFoldDB; Q10Q80; -.
DR SMR; Q10Q80; -.
DR STRING; 4530.OS03T0206300-01; -.
DR PaxDb; Q10Q80; -.
DR PRIDE; Q10Q80; -.
DR EnsemblPlants; Os03t0206300-01; Os03t0206300-01; Os03g0206300. [Q10Q80-2]
DR GeneID; 9270137; -.
DR Gramene; Os03t0206300-01; Os03t0206300-01; Os03g0206300. [Q10Q80-2]
DR KEGG; osa:9270137; -.
DR eggNOG; KOG3355; Eukaryota.
DR HOGENOM; CLU_105631_0_0_1; -.
DR InParanoid; Q10Q80; -.
DR OrthoDB; 1537996at2759; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0016971; F:flavin-linked sulfhydryl oxidase activity; IBA:GO_Central.
DR Gene3D; 1.20.120.310; -; 1.
DR InterPro; IPR039799; ALR/ERV.
DR InterPro; IPR036774; ERV/ALR_sulphydryl_oxid_sf.
DR InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
DR PANTHER; PTHR12645; PTHR12645; 1.
DR Pfam; PF04777; Evr1_Alr; 1.
DR SUPFAM; SSF69000; SSF69000; 1.
DR PROSITE; PS51324; ERV_ALR; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; FAD; Flavoprotein; Mitochondrion;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..194
FT /note="FAD-linked sulfhydryl oxidase ERV1"
FT /id="PRO_0000437986"
FT DOMAIN 72..172
FT /note="ERV/ALR sulfhydryl oxidase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT REGION 44..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 177..182
FT /note="Required for dimerization and substrate specificity"
FT /evidence="ECO:0000250|UniProtKB:Q8GXX0"
FT COMPBIAS 47..66
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 76
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8GXX0"
FT BINDING 81..84
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8GXX0"
FT BINDING 121..125
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8GXX0"
FT BINDING 148..155
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8GXX0"
FT BINDING 160
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8GXX0"
FT BINDING 171..172
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8GXX0"
FT DISULFID 119..122
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT DISULFID 148..165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT DISULFID 177..182
FT /evidence="ECO:0000250|UniProtKB:Q8GXX0"
FT VAR_SEQ 110..122
FT /note="MAIISRLYPCKEC -> VSIKQDKQLVISL (in isoform 2)"
FT /id="VSP_058587"
FT VAR_SEQ 123..194
FT /note="Missing (in isoform 2)"
FT /id="VSP_058588"
SQ SEQUENCE 194 AA; 21604 MW; FB44E4BEC4C10B5F CRC64;
MPPPAWGWGS NPLEPVVHTV AAFSRRLLIA PDAAPDEARL RPLLSLSLSP PPTPPSPPPP
PPEVLKKDSK AAPLTKEEVG RATWMLLHTI AAQFPDEPTR QQRRDARELM AIISRLYPCK
ECAEHFKEVL KANPVQAGSQ AEFSQWLCYV HNVVNRSLGK PIFPCQRVNA RWGKLDCPER
SCDLEGSNDI IPNR
