ID   QSOX2_MOUSE             Reviewed;         692 AA.
AC   Q3TMX7; A2ALE0; A2ALE1; Q3TZA5; Q8C9I4; Q8K0M2;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   24-JAN-2024, entry version 138.
DE   RecName: Full=Sulfhydryl oxidase 2;
DE            EC=1.8.3.2;
DE   AltName: Full=Quiescin Q6-like protein 1;
DE   Flags: Precursor;
GN   Name=Qsox2; Synonyms=Qscn6l1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Adipose tissue, Inner ear, and Thymus;
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., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., 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., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Pancreas, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Catalyzes the oxidation of sulfhydryl groups in peptide and
CC       protein thiols to disulfides with the reduction of oxygen to hydrogen
CC       peroxide. May contribute to disulfide bond formation in a variety of
CC       secreted proteins (By similarity). {ECO:0000250}.
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;
CC         Evidence={ECO:0000250|UniProtKB:O00391};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:O00391};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass membrane
CC       protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q3TMX7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3TMX7-2; Sequence=VSP_020501, VSP_020502;
CC       Name=3;
CC         IsoId=Q3TMX7-3; Sequence=VSP_020500;
CC   -!- SIMILARITY: Belongs to the quiescin-sulfhydryl oxidase (QSOX) family.
CC       {ECO:0000305}.
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DR   EMBL; AK042036; BAC31140.1; ALT_SEQ; mRNA.
DR   EMBL; AK140324; BAE24335.1; -; mRNA.
DR   EMBL; AK157992; BAE34304.1; -; mRNA.
DR   EMBL; AK165642; BAE38312.1; -; mRNA.
DR   EMBL; AL773595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC030934; AAH30934.1; -; mRNA.
DR   CCDS; CCDS15798.1; -. [Q3TMX7-2]
DR   RefSeq; NP_001289885.1; NM_001302956.1. [Q3TMX7-1]
DR   RefSeq; NP_705787.1; NM_153559.3. [Q3TMX7-2]
DR   AlphaFoldDB; Q3TMX7; -.
DR   SMR; Q3TMX7; -.
DR   BioGRID; 230654; 3.
DR   STRING; 10090.ENSMUSP00000037128; -.
DR   GlyCosmos; Q3TMX7; 4 sites, No reported glycans.
DR   GlyGen; Q3TMX7; 4 sites.
DR   iPTMnet; Q3TMX7; -.
DR   PhosphoSitePlus; Q3TMX7; -.
DR   EPD; Q3TMX7; -.
DR   MaxQB; Q3TMX7; -.
DR   PaxDb; 10090-ENSMUSP00000037128; -.
DR   PeptideAtlas; Q3TMX7; -.
DR   ProteomicsDB; 300297; -. [Q3TMX7-1]
DR   ProteomicsDB; 300298; -. [Q3TMX7-2]
DR   ProteomicsDB; 300299; -. [Q3TMX7-3]
DR   Pumba; Q3TMX7; -.
DR   Antibodypedia; 2576; 133 antibodies from 19 providers.
DR   DNASU; 227638; -.
DR   Ensembl; ENSMUST00000036187.9; ENSMUSP00000037128.9; ENSMUSG00000036327.19. [Q3TMX7-2]
DR   Ensembl; ENSMUST00000091263.12; ENSMUSP00000088807.6; ENSMUSG00000036327.19. [Q3TMX7-3]
DR   GeneID; 227638; -.
DR   KEGG; mmu:227638; -.
DR   UCSC; uc008iuj.2; mouse. [Q3TMX7-2]
DR   UCSC; uc008iuk.2; mouse. [Q3TMX7-1]
DR   AGR; MGI:2387194; -.
DR   CTD; 169714; -.
DR   MGI; MGI:2387194; Qsox2.
DR   VEuPathDB; HostDB:ENSMUSG00000036327; -.
DR   eggNOG; KOG1731; Eukaryota.
DR   GeneTree; ENSGT00940000159734; -.
DR   HOGENOM; CLU_020182_1_1_1; -.
DR   InParanoid; Q3TMX7; -.
DR   OMA; DSWDEGH; -.
DR   OrthoDB; 20090at2759; -.
DR   PhylomeDB; Q3TMX7; -.
DR   TreeFam; TF316749; -.
DR   BRENDA; 1.8.3.2; 3474.
DR   BioGRID-ORCS; 227638; 2 hits in 79 CRISPR screens.
DR   ChiTaRS; Qsox2; mouse.
DR   PRO; PR:Q3TMX7; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q3TMX7; Protein.
DR   Bgee; ENSMUSG00000036327; Expressed in spermatocyte and 209 other cell types or tissues.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0016971; F:flavin-dependent sulfhydryl oxidase activity; IBA:GO_Central.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   CDD; cd02992; PDI_a_QSOX; 1.
DR   Gene3D; 1.20.120.310; ERV/ALR sulfhydryl oxidase domain; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR   Gene3D; 1.20.120.1960; QSOX sulfhydryl oxidase domain; 1.
DR   InterPro; IPR036774; ERV/ALR_sulphydryl_oxid_sf.
DR   InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
DR   InterPro; IPR040986; QSOX_FAD-bd_dom.
DR   InterPro; IPR042568; QSOX_FAD-bd_sf.
DR   InterPro; IPR041269; QSOX_Trx1.
DR   InterPro; IPR039798; Sulfhydryl_oxidase.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR22897; QUIESCIN Q6-RELATED SULFHYDRYL OXIDASE; 1.
DR   PANTHER; PTHR22897:SF7; SULFHYDRYL OXIDASE 2; 1.
DR   Pfam; PF04777; Evr1_Alr; 1.
DR   Pfam; PF18371; FAD_SOX; 1.
DR   Pfam; PF18108; QSOX_Trx1; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF69000; FAD-dependent thiol oxidase; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51324; ERV_ALR; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
DR   Genevisible; Q3TMX7; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Disulfide bond; FAD; Flavoprotein; Glycoprotein;
KW   Membrane; Oxidoreductase; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..38
FT                   /evidence="ECO:0000255"
FT   CHAIN           39..692
FT                   /note="Sulfhydryl oxidase 2"
FT                   /id="PRO_0000249539"
FT   TRANSMEM        656..676
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          54..172
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          415..524
FT                   /note="ERV/ALR sulfhydryl oxidase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT   REGION          568..607
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        577..603
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        85
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        88
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         420
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:O00391"
FT   BINDING         427
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:O00391"
FT   BINDING         431
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:O00391"
FT   BINDING         472
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:O00391"
FT   BINDING         476
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:O00391"
FT   BINDING         499..506
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:O00391"
FT   BINDING         521
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:O00391"
FT   BINDING         524
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:O00391"
FT   CARBOHYD        71
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        172
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        212
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        260
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        85..88
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654,
FT                   ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        116..125
FT                   /evidence="ECO:0000250|UniProtKB:O00391"
FT   DISULFID        412..424
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT   DISULFID        470..473
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT   DISULFID        530..533
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT   VAR_SEQ         1..165
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_020500"
FT   VAR_SEQ         574..666
FT                   /note="EWEAQGREQEEGKGLNPSGKSWRHHDTGSLRPPHILGPRTDLSKSLHHRLDL
FT                   RLQSPQGPQALKEAKAVVPFLGVGFSSLDMSLCVVLYVASS -> SVLRARPWLGQMAR
FT                   LSHVNLLPHFPVEEVSSLKPGVLCLKTNKPRSSLGVSKDEHSWSVSLRIGPI (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_020501"
FT   VAR_SEQ         667..692
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_020502"
SQ   SEQUENCE   692 AA;  77775 MW;  3BDC7058817484A1 CRC64;
     MAAARAVARD PGAYARQPPS LRAARLPRLL FLLAVVAAVG PREGGGARLY REGSDAVWLL
     DSGSVRSATG NSSAAWLVQF HSSWCGHCIG YAPTWRALAA DVRDWAAAIR VAALDCAEEK
     NQDVCRTYDI HFYPTFRYFK AFTKEFTTGE NFKGPDRELR TVRQTMIDFL QNHTEGTWPP
     ACPPLDPIQS SDILSFMDSH SGQYHAIVFE SNGSYVGREV ILDLIPYENI MVSRALDTDK
     AFLGTLGITS VPSCYLIYPN GSHGLVNVAK PLRSFFSSHL KSLPDVRKKS LFLPEKSNKE
     EKSEVVVWKE FDRAKLYTAD LESGLHYLLR VELAAHRSLA GAQLKTFRDF VTVVAKLFPG
     RPAVKKLLET LQEWLANLPL DKIPYNAILD LVNNKMQISG IFLTSHVKWV GCQGSRLELR
     GYPCSLWKLF HTLTVQASTH PEALAGTGFE GHPQAVLQAI RRYIRTFFGC KECGEHFEEM
     AKESMDSVKT PDQAVLWLWR KHNMVNSRLA GHLSEDPKFP KVPWPTPDLC PACHEEIKGL
     DSWNEGQVLL FLKQHYSRDN LVDAYSVDQG SPGEWEAQGR EQEEGKGLNP SGKSWRHHDT
     GSLRPPHILG PRTDLSKSLH HRLDLRLQSP QGPQALKEAK AVVPFLGVGF SSLDMSLCVV
     LYVASSLFLM IMYFFFRVRS KRWKVRLYHP AV
//