ID   ERV2_SCHPO              Reviewed;         192 AA.
AC   Q9Y806;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 120.
DE   RecName: Full=FAD-linked sulfhydryl oxidase erv2;
DE            EC=1.8.3.2;
GN   Name=erv2; ORFNames=SPBC146.04;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: FAD-dependent sulfhydryl oxidase that catalyzes disulfide
CC       bond formation in the endoplasmic reticulum lumen.
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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00654};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass type III membrane protein {ECO:0000250}; Lumenal side
CC       {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
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DR   EMBL; CU329671; CAB46757.1; -; Genomic_DNA.
DR   PIR; T39418; T39418.
DR   RefSeq; NP_595393.1; NM_001021300.2.
DR   AlphaFoldDB; Q9Y806; -.
DR   SMR; Q9Y806; -.
DR   BioGRID; 276274; 7.
DR   IntAct; Q9Y806; 1.
DR   STRING; 284812.Q9Y806; -.
DR   iPTMnet; Q9Y806; -.
DR   PaxDb; 4896-SPBC146-04-1; -.
DR   EnsemblFungi; SPBC146.04.1; SPBC146.04.1:pep; SPBC146.04.
DR   GeneID; 2539721; -.
DR   KEGG; spo:SPBC146.04; -.
DR   PomBase; SPBC146.04; erv2.
DR   VEuPathDB; FungiDB:SPBC146.04; -.
DR   eggNOG; KOG3355; Eukaryota.
DR   HOGENOM; CLU_070631_2_2_1; -.
DR   InParanoid; Q9Y806; -.
DR   PhylomeDB; Q9Y806; -.
DR   PRO; PR:Q9Y806; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:PomBase.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:0016971; F:flavin-dependent sulfhydryl oxidase activity; IBA:GO_Central.
DR   GO; GO:0034975; P:protein folding in endoplasmic reticulum; IC:PomBase.
DR   GO; GO:0042026; P:protein refolding; ISS:PomBase.
DR   Gene3D; 1.20.120.310; ERV/ALR sulfhydryl oxidase domain; 1.
DR   InterPro; IPR039799; ALR/ERV.
DR   InterPro; IPR036774; ERV/ALR_sulphydryl_oxid_sf.
DR   InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
DR   PANTHER; PTHR12645; ALR/ERV; 1.
DR   PANTHER; PTHR12645:SF1; FAD-LINKED SULFHYDRYL OXIDASE ERV2; 1.
DR   Pfam; PF04777; Evr1_Alr; 1.
DR   SUPFAM; SSF69000; FAD-dependent thiol oxidase; 1.
DR   PROSITE; PS51324; ERV_ALR; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Disulfide bond; Endoplasmic reticulum; FAD; Flavoprotein;
KW   Membrane; Nucleus; Oxidoreductase; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..192
FT                   /note="FAD-linked sulfhydryl oxidase erv2"
FT                   /id="PRO_0000339122"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        9..29
FT                   /note="Helical; Signal-anchor"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..192
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          61..162
FT                   /note="ERV/ALR sulfhydryl oxidase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT   BINDING         74
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q12284"
FT   BINDING         138
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q12284"
FT   BINDING         141
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q12284"
FT   BINDING         145
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q12284"
FT   BINDING         162
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q12284"
FT   DISULFID        138..155
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
SQ   SEQUENCE   192 AA;  22389 MW;  A14DCB3F731AB47B CRC64;
     MILNRRIQVI LPTLLILSFI IWIFHSVMVD KDWRLFMPEI KSLPDREGQG RKPIEMMSTK
     HDNNTNNLMV NAYWKLIHTV VSNYPNRPTL DERDILRHYL FSSAITMPCG EYSVELQKIL
     DVHPPQTSSR KAATTWACKV HNQLNEKMNQ PKTSCDGFNE RYVIGSPTYR ESEAENVPER
     VQVINEDHDY SG
//