QSOX2_MOUSE
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 03-AUG-2022, entry version 130.
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 GlyGen; Q3TMX7; 4 sites.
DR iPTMnet; Q3TMX7; -.
DR PhosphoSitePlus; Q3TMX7; -.
DR EPD; Q3TMX7; -.
DR MaxQB; Q3TMX7; -.
DR PaxDb; Q3TMX7; -.
DR PeptideAtlas; Q3TMX7; -.
DR PRIDE; Q3TMX7; -.
DR ProteomicsDB; 300297; -. [Q3TMX7-1]
DR ProteomicsDB; 300298; -. [Q3TMX7-2]
DR ProteomicsDB; 300299; -. [Q3TMX7-3]
DR Antibodypedia; 2576; 113 antibodies from 19 providers.
DR DNASU; 227638; -.
DR Ensembl; ENSMUST00000036187; ENSMUSP00000037128; ENSMUSG00000036327. [Q3TMX7-2]
DR Ensembl; ENSMUST00000091263; ENSMUSP00000088807; ENSMUSG00000036327. [Q3TMX7-3]
DR GeneID; 227638; -.
DR KEGG; mmu:227638; -.
DR UCSC; uc008iuj.2; mouse. [Q3TMX7-2]
DR UCSC; uc008iuk.2; mouse. [Q3TMX7-1]
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; RHLNPKF; -.
DR OrthoDB; 498515at2759; -.
DR PhylomeDB; Q3TMX7; -.
DR TreeFam; TF316749; -.
DR BRENDA; 1.8.3.2; 3474.
DR BioGRID-ORCS; 227638; 2 hits in 74 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 206 other tissues.
DR Genevisible; Q3TMX7; MM.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0030173; C:integral component of Golgi membrane; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0016971; F:flavin-linked 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 Gene3D; 1.20.120.1960; -; 1.
DR Gene3D; 1.20.120.310; -; 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; PTHR22897; 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; SSF52833; SSF52833; 1.
DR SUPFAM; SSF69000; SSF69000; 1.
DR PROSITE; PS51324; ERV_ALR; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
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
