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Database: UniProt
Entry: A0A2Y9MFY3_DELLE
LinkDB: A0A2Y9MFY3_DELLE
Original site: A0A2Y9MFY3_DELLE 
ID   A0A2Y9MFY3_DELLE        Unreviewed;       280 AA.
AC   A0A2Y9MFY3;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=thioredoxin-dependent peroxiredoxin {ECO:0000256|ARBA:ARBA00013017};
DE            EC=1.11.1.24 {ECO:0000256|ARBA:ARBA00013017};
GN   Name=PRDX4 {ECO:0000313|RefSeq:XP_022416183.1};
OS   Delphinapterus leucas (Beluga whale).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Monodontidae; Delphinapterus.
OX   NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022416183.1};
RN   [1] {ECO:0000313|RefSeq:XP_022416183.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022416183.1};
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC         disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC         COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC         ChEBI:CHEBI:50058; EC=1.11.1.24;
CC         Evidence={ECO:0000256|ARBA:ARBA00000280};
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00009796}.
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DR   RefSeq; XP_022416183.1; XM_022560475.2.
DR   AlphaFoldDB; A0A2Y9MFY3; -.
DR   STRING; 9749.A0A2Y9MFY3; -.
DR   Ensembl; ENSDLET00000005283; ENSDLEP00000004736; ENSDLEG00000003633.
DR   KEGG; dle:111167516; -.
DR   InParanoid; A0A2Y9MFY3; -.
DR   OrthoDB; 47465at2759; -.
DR   Proteomes; UP000248483; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0140313; F:molecular sequestering activity; IEA:Ensembl.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:Ensembl.
DR   GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR   GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR   GO; GO:2000255; P:negative regulation of male germ cell proliferation; IEA:Ensembl.
DR   GO; GO:0022417; P:protein maturation by protein folding; IEA:Ensembl.
DR   GO; GO:0072593; P:reactive oxygen species metabolic process; IEA:Ensembl.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
DR   GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR   CDD; cd03015; PRX_Typ2cys; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR019479; Peroxiredoxin_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR10681:SF166; PEROXIREDOXIN-4; 1.
DR   PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 1.
DR   Pfam; PF10417; 1-cysPrx_C; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Antioxidant {ECO:0000256|ARBA:ARBA00022862};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           36..280
FT                   /note="thioredoxin-dependent peroxiredoxin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016067386"
FT   DOMAIN          80..238
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   280 AA;  31303 MW;  51B50B2E314B6C7F CRC64;
     MEARRPPLPA TTSAPGRSRK LLLLPLLLFL LPAKALRGLD AEERPRTREE ECHFYAGGQV
     YPGEASRVSV ADHSLHLSKA KISKPAPYWE GTAVINGEFK ELKLTDYRGK YLVFFFYPLD
     FTFVCPTEII AFGDRIEEFR SINTEVVACS VDSQFTHLAW INTPRRQGGL GPISIPLLSD
     LNHQISKDYG VYLEDSGHTL RGLFIIDDKG ILRQITLNDL PVGRSVDETL RLVQAFQYTD
     KHGEVCPAGW KPGSETVSQI DFSVKRMAGA KKKTKKPTLG
//
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