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
//