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Database: UniProt
Entry: H3A722_LATCH
LinkDB: H3A722_LATCH
Original site: H3A722_LATCH 
ID   H3A722_LATCH            Unreviewed;       616 AA.
AC   H3A722;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 59.
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:ENSLACP00000005443.1};
OS   Latimeria chalumnae (Coelacanth).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Coelacanthiformes; Coelacanthidae; Latimeria.
OX   NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000005443.1, ECO:0000313|Proteomes:UP000008672};
RN   [1] {ECO:0000313|Proteomes:UP000008672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT   "The draft genome of Latimeria chalumnae.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLACP00000005443.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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|RuleBase:RU371123}.
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DR   EMBL; AFYH01183515; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01183516; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01183517; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01183518; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01183519; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01183520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01183521; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01183522; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; H3A722; -.
DR   STRING; 7897.ENSLACP00000005443; -.
DR   Ensembl; ENSLACT00000005491.1; ENSLACP00000005443.1; ENSLACG00000004842.1.
DR   eggNOG; KOG1731; Eukaryota.
DR   GeneTree; ENSGT00940000159504; -.
DR   HOGENOM; CLU_020182_1_0_1; -.
DR   InParanoid; H3A722; -.
DR   OMA; WPNIAPY; -.
DR   TreeFam; TF316749; -.
DR   Proteomes; UP000008672; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016971; F:flavin-dependent sulfhydryl oxidase activity; IEA:InterPro.
DR   Gene3D; 1.20.120.310; ERV/ALR sulfhydryl oxidase domain; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
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   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   SUPFAM; SSF69000; FAD-dependent thiol oxidase; 1.
DR   PROSITE; PS51324; ERV_ALR; 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:UP000008672};
KW   Transmembrane {ECO:0000256|RuleBase:RU371123};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU371123}.
FT   TRANSMEM        585..602
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU371123"
FT   DOMAIN          257..363
FT                   /note="ERV/ALR sulfhydryl oxidase"
FT                   /evidence="ECO:0000259|PROSITE:PS51324"
FT   REGION          433..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..453
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        454..477
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   616 AA;  71602 MW;  6734D424803CCE0F CRC64;
     DVQTLRHKII DLLETHEDVW PPACPPLEPA SMAEVRSFFQ TNSVHYLALI FEEEDSYIGR
     EVTLDMLQYE NIAVRRVWRT EKAMVSQFGV KSFPSCYLYF NNGTHAQIQV EMQVRSFYTY
     YLQRLPGVMR GGYKLMVIPD SQSGAIATTW KTFDSSKVYM ADLESALHYA LRVEVKPQRI
     LAGEELAALK GFVSVLAKYF PGRPTVKNLL RSMDSWLGSY RVSELSYSTF QDVVNNKLEV
     PSAVLADSVN WVGCQGSKPQ FRGYPCSLWT LFHVLTVQAA WKLLPGNKGG NPLEVLLAMH
     GYVKYFFGCR DCATKFEAMA AESMENIKDL DGAILWLWSR HNRVNSRLAG AVSEDPKFPK
     LQWPPPDLCP KCHNEVKGEH VWNMDAVLRF LKAHFYKENI SYDYLAREAH LLADQRDQLA
     AWREAEQQKQ LRERKEKIKE ENEKGQNELE KEEQRKEEEE EEEEEDEDDE RNEQPEEGDE
     TNVENVKQSR NPKPSFVQGK RKKKLQEEEI IVDLDSFIEH HYKSKALQAA AVRRNKGQRE
     EQRQDQQVQQ DAEMIDYREG LVPKKKHWIM LLGVGFSRLD LSLCVLFYFL SSLCLLGMCL
     YFRMRLKCRR ARHTYN
//
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