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Sulfhydryl oxidase 1 (mSOx) (EC 1.8.3.2) (Quiescin Q6) (Skin sulfhydryl oxidase)

 QSOX1_MOUSE             Reviewed;         748 AA.
Q8BND5; Q3TDY9; Q3TE19; Q3TR29; Q3UEL4; Q8K041; Q9DBL6;
19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
23-MAY-2018, entry version 130.
RecName: Full=Sulfhydryl oxidase 1;
Short=mSOx;
EC=1.8.3.2;
AltName: Full=Quiescin Q6;
AltName: Full=Skin sulfhydryl oxidase;
Flags: Precursor;
Name=Qsox1; Synonyms=Qscn6, Sox;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=12354420; DOI=10.1016/S0923-1811(02)00061-0;
Matsuba S., Suga Y., Ishidoh K., Hashimoto Y., Takamori K.,
Kominami E., Wilhelm B., Seitz J., Ogawa H.;
"Sulfhydryl oxidase (SOx) from mouse epidermis: molecular cloning,
nucleotide sequence, and expression of recombinant protein in the
cultured cells.";
J. Dermatol. Sci. 30:50-62(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
STRAIN=C57BL/6J, and NOD;
TISSUE=Cerebellum, Liver, and Spinal ganglion;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 137-538 (ISOFORM 3).
STRAIN=C57BL/6J, and FVB/N; TISSUE=Eye, and Salivary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, and
Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Catalyzes the oxidation of sulfhydryl groups in peptide
and protein thiols to disulfides with the reduction of oxygen to
hydrogen peroxide. May contribute to disulfide bond formation in a
variety of secreted proteins (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: 2 R'C(R)SH + O(2) = R'C(R)S-S(R)CR' +
H(2)O(2).
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
Note=Binds 1 FAD per subunit. {ECO:0000250};
-!- SUBUNIT: Monomer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 1: Golgi apparatus membrane
{ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 2: Secreted. Note=Found in the
extracellular medium of quiescent cells but not in proliferating
cells.
-!- SUBCELLULAR LOCATION: Isoform 3: Secreted. Note=Found in the
extracellular medium of quiescent cells but not in proliferating
cells.
-!- SUBCELLULAR LOCATION: Isoform 4: Secreted. Note=Found in the
extracellular medium of quiescent cells but not in proliferating
cells.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q8BND5-1; Sequence=Displayed;
Name=2;
IsoId=Q8BND5-2; Sequence=VSP_020495, VSP_020496;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q8BND5-3; Sequence=VSP_020493, VSP_020494;
Name=4;
IsoId=Q8BND5-4; Sequence=VSP_020491, VSP_020492;
Note=No experimental confirmation available. Ref.2 (BAE37202)
sequence is in conflict in position: 127:C->Y. {ECO:0000305};
-!- TISSUE SPECIFICITY: Expressed in the seminal vesicles and skin.
{ECO:0000269|PubMed:12354420}.
-!- SIMILARITY: Belongs to the quiescin-sulfhydryl oxidase (QSOX)
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB044284; BAB21936.1; -; mRNA.
EMBL; AK004880; BAB23638.1; -; mRNA.
EMBL; AK083938; BAC39073.1; -; mRNA.
EMBL; AK149465; BAE28897.1; -; mRNA.
EMBL; AK163119; BAE37202.1; -; mRNA.
EMBL; AK166839; BAE39061.1; -; mRNA.
EMBL; AK169877; BAE41429.1; -; mRNA.
EMBL; AK169920; BAE41459.1; -; mRNA.
EMBL; AK170449; BAE41807.1; -; mRNA.
EMBL; BC034131; AAH34131.1; -; mRNA.
EMBL; BC076590; AAH76590.1; -; mRNA.
CCDS; CCDS15386.1; -. [Q8BND5-1]
CCDS; CCDS78713.1; -. [Q8BND5-3]
RefSeq; NP_001020116.1; NM_001024945.1. [Q8BND5-1]
RefSeq; NP_075757.1; NM_023268.2. [Q8BND5-3]
UniGene; Mm.27035; -.
PDB; 3T58; X-ray; 2.40 A; A/B/C/D=36-550.
PDB; 3T59; X-ray; 2.80 A; A/B/C/D=36-550.
PDB; 5D8I; X-ray; 2.05 A; A/B=36-275.
PDB; 5D93; X-ray; 2.20 A; A/D=36-275.
PDB; 5D96; X-ray; 2.30 A; A/D=36-275.
PDBsum; 3T58; -.
PDBsum; 3T59; -.
PDBsum; 5D8I; -.
PDBsum; 5D93; -.
PDBsum; 5D96; -.
ProteinModelPortal; Q8BND5; -.
SMR; Q8BND5; -.
STRING; 10090.ENSMUSP00000035658; -.
iPTMnet; Q8BND5; -.
PhosphoSitePlus; Q8BND5; -.
PaxDb; Q8BND5; -.
PeptideAtlas; Q8BND5; -.
PRIDE; Q8BND5; -.
Ensembl; ENSMUST00000035325; ENSMUSP00000035658; ENSMUSG00000033684. [Q8BND5-1]
Ensembl; ENSMUST00000111764; ENSMUSP00000107394; ENSMUSG00000033684. [Q8BND5-2]
Ensembl; ENSMUST00000194632; ENSMUSP00000142301; ENSMUSG00000033684. [Q8BND5-3]
GeneID; 104009; -.
KEGG; mmu:104009; -.
UCSC; uc007dbo.1; mouse. [Q8BND5-3]
UCSC; uc007dbp.1; mouse. [Q8BND5-1]
UCSC; uc007dbq.1; mouse. [Q8BND5-4]
UCSC; uc011wtx.1; mouse. [Q8BND5-2]
CTD; 5768; -.
MGI; MGI:1330818; Qsox1.
eggNOG; KOG1731; Eukaryota.
eggNOG; ENOG410XVJT; LUCA.
GeneTree; ENSGT00390000008045; -.
HOVERGEN; HBG080360; -.
InParanoid; Q8BND5; -.
KO; K10758; -.
OMA; MMVLAFK; -.
OrthoDB; EOG091G038J; -.
PhylomeDB; Q8BND5; -.
TreeFam; TF316749; -.
BRENDA; 1.8.3.2; 3474.
Reactome; R-MMU-114608; Platelet degranulation.
Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-MMU-6798695; Neutrophil degranulation.
Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
PRO; PR:Q8BND5; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000033684; -.
CleanEx; MM_QSOX1; -.
Genevisible; Q8BND5; MM.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0030173; C:integral component of Golgi membrane; ISS:UniProtKB.
GO; GO:0045171; C:intercellular bridge; ISO:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0016971; F:flavin-linked sulfhydryl oxidase activity; ISS:UniProtKB.
GO; GO:0003756; F:protein disulfide isomerase activity; ISS:UniProtKB.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0016242; P:negative regulation of macroautophagy; ISO:MGI.
Gene3D; 1.20.120.310; -; 1.
InterPro; IPR036774; ERV/ALR_sulphydryl_oxid_sf.
InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR013766; Thioredoxin_domain.
Pfam; PF04777; Evr1_Alr; 1.
Pfam; PF00085; Thioredoxin; 1.
SUPFAM; SSF52833; SSF52833; 1.
SUPFAM; SSF69000; SSF69000; 1.
PROSITE; PS51324; ERV_ALR; 1.
PROSITE; PS51352; THIOREDOXIN_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Disulfide bond;
FAD; Flavoprotein; Glycoprotein; Golgi apparatus; Membrane;
Oxidoreductase; Reference proteome; Secreted; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 32 {ECO:0000255}.
CHAIN 33 748 Sulfhydryl oxidase 1.
/FTId=PRO_0000249534.
TRANSMEM 711 731 Helical. {ECO:0000255}.
DOMAIN 33 159 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
DOMAIN 399 506 ERV/ALR sulfhydryl oxidase.
{ECO:0000255|PROSITE-ProRule:PRU00654}.
NP_BIND 481 488 FAD. {ECO:0000250}.
ACT_SITE 73 73 Nucleophile. {ECO:0000250}.
ACT_SITE 76 76 Nucleophile. {ECO:0000250}.
BINDING 404 404 FAD. {ECO:0000250}.
BINDING 411 411 FAD. {ECO:0000250}.
BINDING 415 415 FAD. {ECO:0000250}.
BINDING 454 454 FAD. {ECO:0000250}.
BINDING 458 458 FAD. {ECO:0000250}.
BINDING 503 503 FAD. {ECO:0000250}.
BINDING 506 506 FAD. {ECO:0000250}.
CARBOHYD 133 133 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 246 246 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 73 76 Redox-active. {ECO:0000255|PROSITE-
ProRule:PRU00654, ECO:0000255|PROSITE-
ProRule:PRU00691}.
DISULFID 396 408 {ECO:0000255|PROSITE-ProRule:PRU00654}.
DISULFID 452 455 {ECO:0000255|PROSITE-ProRule:PRU00654}.
DISULFID 512 515 {ECO:0000255|PROSITE-ProRule:PRU00654}.
VAR_SEQ 126 154 FFQAFTKNGSGATLPGAGANVQTLRMRLI -> VCEGGATV
EWFWPSTQSSVPHFPGTFLGC (in isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_020491.
VAR_SEQ 155 748 Missing (in isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_020492.
VAR_SEQ 567 568 VM -> LL (in isoform 3).
{ECO:0000303|PubMed:12354420,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_020493.
VAR_SEQ 569 748 Missing (in isoform 3).
{ECO:0000303|PubMed:12354420,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_020494.
VAR_SEQ 660 661 VN -> LL (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_020495.
VAR_SEQ 662 748 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_020496.
CONFLICT 637 637 M -> I (in Ref. 2; BAE41429).
{ECO:0000305}.
CONFLICT 656 656 F -> L (in Ref. 2; BAE41429).
{ECO:0000305}.
STRAND 41 44 {ECO:0000244|PDB:5D8I}.
STRAND 46 48 {ECO:0000244|PDB:5D8I}.
TURN 50 52 {ECO:0000244|PDB:5D8I}.
HELIX 53 57 {ECO:0000244|PDB:5D8I}.
STRAND 61 69 {ECO:0000244|PDB:5D8I}.
HELIX 74 89 {ECO:0000244|PDB:5D8I}.
HELIX 91 93 {ECO:0000244|PDB:5D8I}.
TURN 94 96 {ECO:0000244|PDB:5D8I}.
STRAND 97 103 {ECO:0000244|PDB:5D8I}.
HELIX 107 115 {ECO:0000244|PDB:5D8I}.
STRAND 120 127 {ECO:0000244|PDB:5D8I}.
STRAND 133 135 {ECO:0000244|PDB:5D8I}.
STRAND 137 139 {ECO:0000244|PDB:5D93}.
HELIX 146 159 {ECO:0000244|PDB:5D8I}.
TURN 160 162 {ECO:0000244|PDB:5D8I}.
HELIX 176 179 {ECO:0000244|PDB:5D8I}.
HELIX 182 185 {ECO:0000244|PDB:5D8I}.
STRAND 189 196 {ECO:0000244|PDB:5D8I}.
HELIX 202 209 {ECO:0000244|PDB:5D8I}.
TURN 210 212 {ECO:0000244|PDB:5D8I}.
STRAND 216 222 {ECO:0000244|PDB:5D8I}.
HELIX 226 231 {ECO:0000244|PDB:5D8I}.
STRAND 236 244 {ECO:0000244|PDB:5D8I}.
STRAND 249 251 {ECO:0000244|PDB:5D8I}.
HELIX 259 267 {ECO:0000244|PDB:5D8I}.
STRAND 269 271 {ECO:0000244|PDB:5D96}.
HELIX 293 296 {ECO:0000244|PDB:3T58}.
STRAND 301 303 {ECO:0000244|PDB:3T59}.
HELIX 304 316 {ECO:0000244|PDB:3T58}.
HELIX 319 321 {ECO:0000244|PDB:3T58}.
STRAND 323 326 {ECO:0000244|PDB:3T58}.
HELIX 327 343 {ECO:0000244|PDB:3T58}.
HELIX 348 363 {ECO:0000244|PDB:3T58}.
STRAND 367 370 {ECO:0000244|PDB:3T58}.
HELIX 371 380 {ECO:0000244|PDB:3T58}.
HELIX 383 386 {ECO:0000244|PDB:3T58}.
STRAND 403 405 {ECO:0000244|PDB:3T58}.
HELIX 406 426 {ECO:0000244|PDB:3T58}.
HELIX 437 449 {ECO:0000244|PDB:3T58}.
HELIX 453 466 {ECO:0000244|PDB:3T58}.
HELIX 467 469 {ECO:0000244|PDB:3T58}.
HELIX 473 491 {ECO:0000244|PDB:3T58}.
STRAND 505 507 {ECO:0000244|PDB:3T58}.
TURN 509 511 {ECO:0000244|PDB:3T58}.
HELIX 513 515 {ECO:0000244|PDB:3T59}.
HELIX 528 538 {ECO:0000244|PDB:3T58}.
HELIX 541 543 {ECO:0000244|PDB:3T58}.
SEQUENCE 748 AA; 82785 MW; 0499F6B8DAB5A8D1 CRC64;
MRRCGRLSGP PSLLLLLLLL SPLLFSGPGA YAARLSVLYS SSDPLTLLDA DSVRPTVLGS
SSAWAVEFFA SWCGHCIAFA PTWKELANDV KDWRPALNLA VLDCAEETNS AVCREFNIAG
FPTVRFFQAF TKNGSGATLP GAGANVQTLR MRLIDALESH RDTWPPACPP LEPAKLNDID
GFFTRNKADY LALVFEREDS YLGREVTLDL SQYHAVAVRR VLNTESDLVN KFGVTDFPSC
YLLLRNGSVS RVPVLVESRS FYTSYLRGLP GLTRDAPPTT ATPVTADKIA PTVWKFADRS
KIYMADLESA LHYILRVEVG KFSVLEGQRL VALKKFVAVL AKYFPGQPLV QNFLHSINDW
LQKQQKKRIP YSFFKAALDS RKEDAVLTEK VNWVGCQGSE PHFRGFPCSL WVLFHFLTVQ
ANRYSEAHPQ EPADGQEVLQ AMRSYVQFFF GCRDCADHFE QMAAASMHQV RSPSNAILWL
WTSHNRVNAR LSGALSEDPH FPKVQWPPRE LCSACHNELN GQVPLWDLGA TLNFLKAHFS
PANIVIDSSA SRHTGRRGSP EATPELVMDT LKLESRNSVL GHEQAASAES PGATALDVPA
EKPEASGPQE LYTGLRMGGA SPGQGPPERM EDHQRDMQEN APGQQHLSKR DTEALFLPEV
NHLQGPLELR RGGRSPKQLA PILEEEPEAL AIQGQGQWLQ VLGGGISHLD ISLCVGLYSV
SFMGLLAMYT YFRARLRTPK GHASYPTA


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