ID   QSOX2_MOUSE             Reviewed;         692 AA.
AC   Q3TMX7; Q3TZA5; Q8C9I4; Q8K0M2;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 41.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; 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.,
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] (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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Catalyzes the oxidation of sulfhydryl groups in peptide
CC       and protein thiols to disulfides with the reduction of oxygen to
CC       hydrogen peroxide. May contribute to disulfide bond formation in a
CC       variety of secreted proteins (By similarity).
CC   -!- CATALYTIC ACTIVITY: 4 R'C(R)SH + O(2) = 2 R'C(R)S-S(R)CR' + 2
CC       H(2)O.
CC   -!- COFACTOR: Binds 1 FAD per subunit (Potential).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein (By
CC       similarity).
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         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q3TMX7-3; Sequence=VSP_020500;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the quiescin-sulfhydryl oxidase (QSOX)
CC       family.
CC   -!- SIMILARITY: Contains 1 ERV/ALR sulfhydryl oxidase domain.
CC   -!- SIMILARITY: Contains 1 thioredoxin domain.
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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; BC030934; AAH30934.1; -; mRNA.
DR   IPI; IPI00169589; -.
DR   IPI; IPI00474916; -.
DR   IPI; IPI00788406; -.
DR   UniGene; Mm.116769; -.
DR   PhosphoSite; Q3TMX7; -.
DR   Ensembl; ENSMUSG00000036327; Mus musculus.
DR   MGI; MGI:2387194; Qsox2.
DR   HOVERGEN; Q3TMX7; -.
DR   OMA; Q3TMX7; EEMATES.
DR   BRENDA; 1.8.3.2; 244.
DR   Bgee; Q3TMX7; -.
DR   CleanEx; MM_QSOX2; -.
DR   GermOnline; ENSMUSG00000036327; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016972; F:thiol oxidase activity; IEA:EC.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
DR   InterPro; IPR006863; Evr1_Alr.
DR   InterPro; IPR017936; Thioredoxin-like.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:1.20.120.310; Evr1_Alr; 1.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   Pfam; PF04777; Evr1_Alr; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   PROSITE; PS51324; ERV_ALR; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; FAD; Flavoprotein; Glycoprotein; Membrane;
KW   Oxidoreductase; Signal; Transmembrane.
FT   SIGNAL        1     38       Potential.
FT   CHAIN        39    692       Sulfhydryl oxidase 2.
FT                                /FTId=PRO_0000249539.
FT   TRANSMEM    656    676       Potential.
FT   DOMAIN       54    172       Thioredoxin.
FT   DOMAIN      415    524       ERV/ALR sulfhydryl oxidase.
FT   CARBOHYD     71     71       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    172    172       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    212    212       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    260    260       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ       1    165       Missing (in isoform 3).
FT                                /FTId=VSP_020500.
FT   VAR_SEQ     574    666       EWEAQGREQEEGKGLNPSGKSWRHHDTGSLRPPHILGPRTD
FT                                LSKSLHHRLDLRLQSPQGPQALKEAKAVVPFLGVGFSSLDM
FT                                SLCVVLYVASS -> SVLRARPWLGQMARLSHVNLLPHFPV
FT                                EEVSSLKPGVLCLKTNKPRSSLGVSKDEHSWSVSLRIGPI
FT                                (in isoform 2).
FT                                /FTId=VSP_020501.
FT   VAR_SEQ     667    692       Missing (in isoform 2).
FT                                /FTId=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
//