ID H1A439_TAEGU Unreviewed; 802 AA.
AC H1A439;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Sulfhydryl oxidase {ECO:0000256|RuleBase:RU371123};
DE EC=1.8.3.2 {ECO:0000256|RuleBase:RU371123};
GN Name=QSOX1 {ECO:0000313|Ensembl:ENSTGUP00000017654.2};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000017654.2, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000017654.2, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000017654.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|RuleBase:RU371123}.
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 Evidence={ECO:0000256|ARBA:ARBA00000999,
CC ECO:0000256|RuleBase:RU371123};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU371123};
CC -!- SIMILARITY: Belongs to the quiescin-sulfhydryl oxidase (QSOX) family.
CC {ECO:0000256|ARBA:ARBA00006041, ECO:0000256|RuleBase:RU371123}.
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DR AlphaFoldDB; H1A439; -.
DR STRING; 59729.ENSTGUP00000017654; -.
DR Ensembl; ENSTGUT00000018057.2; ENSTGUP00000017654.2; ENSTGUG00000017374.2.
DR GeneTree; ENSGT00940000159504; -.
DR HOGENOM; CLU_020182_1_0_1; -.
DR InParanoid; H1A439; -.
DR OMA; RYFPFND; -.
DR OrthoDB; 20090at2759; -.
DR TreeFam; TF316749; -.
DR Proteomes; UP000007754; Chromosome 8.
DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
DR GO; GO:0045171; C:intercellular bridge; IEA:Ensembl.
DR GO; GO:0071949; F:FAD binding; IEA:Ensembl.
DR GO; GO:0016971; F:flavin-dependent sulfhydryl oxidase activity; IEA:Ensembl.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:Ensembl.
DR GO; GO:0085029; P:extracellular matrix assembly; IEA:Ensembl.
DR GO; GO:0016242; P:negative regulation of macroautophagy; IEA:Ensembl.
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:SF6; SULFHYDRYL OXIDASE 1; 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.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU371123};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU371123}; Membrane {ECO:0000256|RuleBase:RU371123};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU371123};
KW Reference proteome {ECO:0000313|Proteomes:UP000007754};
KW Transmembrane {ECO:0000256|RuleBase:RU371123};
KW Transmembrane helix {ECO:0000256|RuleBase:RU371123}.
FT TRANSMEM 769..786
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU371123"
FT DOMAIN 95..234
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 479..582
FT /note="ERV/ALR sulfhydryl oxidase"
FT /evidence="ECO:0000259|PROSITE:PS51324"
FT REGION 43..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 802 AA; 89640 MW; B8447E58151AD94B CRC64;
MPFVPSRKGR QKRGVKEEVC WARPHDAGRR EAQAVRGCGR AAAAEGIPAR PRPGPAPGAA
LRAAPGAKGG SGRCRPAWRA MWRRRARAGG RGGLPPLLLL FLLLRVPAAR PGRLYSASDP
LELLGPGAEG RLLGSSSAWA VEFFASWCGH CIHFAPTWRA LAHDIREWRP AVILAAIDCA
DEDNQQVCSD FGITGFPTMK FFRAFSNKPE DGIRITNPSA TVEDLRHAII TNLEQSQDAW
PPACPPLEPA SAEEVRTFFQ RNKDQYLALI FEKSNSFVGR EVALDMLQYE NIAVRRVLSS
EEELVQKFGV TSFPSGYLLF RNGSFSRLPV HVEARSFYTY YLRTLTGIAR GSYKLNATAS
ALNDTDRVSH PLRADRSKLY MADLESALHY SLRVEAARAS SLSGAQLAAF KCYVATLVKY
FPGRPCVQTY LQTLDAWLKN WTEPELPRTV LKEAMKNNRD ASQPSVLPTN VTWVGCQGSE
RHFRGYPCGL WTIFHLLTVQ AAQNGPDKEL PLEVLSTMRC YVRHFFGCQE CAEHFEAMAA
KSMDGVASRE EAVLWLWSHH NEVNARLAGG DTEDPKFPKL QWPPPDLCPQ CHKEERGVHA
WEEPAVLMFL KAHFSPANIY MDYAEPDPIP VAREGTGARL DTESPREERG RGEAEEREPE
GEARVEPRRP SIVRLNPKLR EGGEDIVDLD SFSEQHFKSQ ALRAAAGRRR RISKRDTMAL
PRGAAAGRER RHAPGVLLRD QEAAEGLRRS PWLRVLGLGF SRLDISLCVA LYFLSSMCLL
AMYTFFRLRT RARKGRPGFP MA
//
