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Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Antioxidant protein 2) (Ciliary body glutathione peroxidase) (Non-selenium glutathione peroxidase) (NSGPx) (PHGPx)

 PRDX6_BOVIN             Reviewed;         224 AA.
O77834; Q5E9F3;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 127.
RecName: Full=Peroxiredoxin-6;
EC=1.11.1.15 {ECO:0000269|PubMed:10409692, ECO:0000269|PubMed:2373154};
AltName: Full=1-Cys peroxiredoxin;
Short=1-Cys PRX;
AltName: Full=Acidic calcium-independent phospholipase A2 {ECO:0000303|PubMed:9787801};
Short=aiPLA2;
EC=3.1.1.4 {ECO:0000269|PubMed:9787801};
AltName: Full=Antioxidant protein 2;
AltName: Full=Ciliary body glutathione peroxidase;
AltName: Full=Non-selenium glutathione peroxidase;
Short=NSGPx;
AltName: Full=PHGPx;
Name=PRDX6; Synonyms=AOP2, GPX, PHGPX;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Ocular ciliary body;
PubMed=9748299; DOI=10.1074/jbc.273.40.26171;
Singh A.K., Shichi H.;
"A novel glutathione peroxidase in bovine eye. Sequence analysis, mRNA
level, and translation.";
J. Biol. Chem. 273:26171-26178(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
BIOPHYSICOCHEMICAL PROPERTIES.
TISSUE=Lung;
PubMed=10409692; DOI=10.1074/jbc.274.30.21326;
Fisher A.B., Dodia C., Manevich Y., Chen J.-W., Feinstein S.I.;
"Phospholipid hydroperoxides are substrates for non-selenium
glutathione peroxidase.";
J. Biol. Chem. 274:21326-21334(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Oviduct;
Rojas Garcia P.P., Einspanier R.;
"Glutathione peroxidase in the bovine oviduct.";
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=16305752; DOI=10.1186/1471-2164-6-166;
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
"Characterization of 954 bovine full-CDS cDNA sequences.";
BMC Genomics 6:166-166(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Crossbred X Angus; TISSUE=Ileum;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[6]
PROTEIN SEQUENCE OF 2-30, FUNCTION, CATALYTIC ACTIVITY, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=2373154; DOI=10.1016/0014-4835(90)90040-2;
Shichi H., Demar J.C.;
"Non-selenium glutathione peroxidase without glutathione S-transferase
activity from bovine ciliary body.";
Exp. Eye Res. 50:513-520(1990).
[7]
PROTEIN SEQUENCE OF 2-16, FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND SUBCELLULAR LOCATION.
PubMed=9787801; DOI=10.1016/S0305-0491(98)10046-9;
Akiba S., Dodia C., Chen X., Fisher A.B.;
"Characterization of acidic Ca(2+)-independent phospholipase A2 of
bovine lung.";
Comp. Biochem. Physiol. 120:393-404(1998).
[8]
INTERACTION WITH GSTP1, AND ACTIVATION BY GLUTATHIONE.
PubMed=15004285; DOI=10.1073/pnas.0400181101;
Manevich Y., Feinstein S.I., Fisher A.B.;
"Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires
glutathionylation mediated by heterodimerization with pi GST.";
Proc. Natl. Acad. Sci. U.S.A. 101:3780-3785(2004).
-!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction
of hydrogen peroxide and organic hydroperoxides to water and
alcohols, respectively. Can reduce H(2)O(2) and short chain
organic, fatty acid, and phospholipid hydroperoxides. Also has
phospholipase activity, and can therefore either reduce the
oxidized sn-2 fatty acyl grup of phospholipids (peroxidase
activity) or hydrolyze the sn-2 ester bond of phospholipids
(phospholipase activity). These activities are dependent on
binding to phospholipids at acidic pH and to oxidized phospholipds
at cytosolic pH. Plays a role in cell protection against oxidative
stress by detoxifying peroxides and in phospholipid homeostasis.
{ECO:0000269|PubMed:10409692, ECO:0000269|PubMed:2373154,
ECO:0000269|PubMed:9787801}.
-!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
{ECO:0000269|PubMed:10409692, ECO:0000269|PubMed:2373154}.
-!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1-
acylglycerophosphocholine + a carboxylate.
{ECO:0000269|PubMed:9787801}.
-!- COFACTOR:
Note=Does not need Ca(2+) as cofactor.
{ECO:0000269|PubMed:9787801};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=25 uM for H(2)O(2) {ECO:0000269|PubMed:2373154};
KM=180 uM for H(2)O(2) {ECO:0000269|PubMed:10409692};
KM=22 uM for tert-butyl hydroperoxide
{ECO:0000269|PubMed:2373154};
KM=142 uM for tert-butyl hydroperoxide
{ECO:0000269|PubMed:10409692};
KM=170 uM for cumene hydroperoxide {ECO:0000269|PubMed:2373154};
KM=120 uM for cumene hydroperoxide
{ECO:0000269|PubMed:10409692};
KM=12 uM for triphenylcarbinyl hydroperoxide
{ECO:0000269|PubMed:2373154};
KM=34 uM for linoleic hydroperoxide
{ECO:0000269|PubMed:2373154};
KM=141 uM for linolenoyl hydroperoxide
{ECO:0000269|PubMed:10409692};
KM=135 uM for arachidonoyl hydroperoxide
{ECO:0000269|PubMed:10409692};
KM=120 uM for PLCP hydroperoxide {ECO:0000269|PubMed:10409692};
KM=129 uM for PACP hydroperoxide {ECO:0000269|PubMed:10409692};
KM=22 uM for 5-phenyl-3-pentenyl hydroperoxide
{ECO:0000269|PubMed:2373154};
KM=350 uM for dipalmitoyl phosphatidylcholine (at pH 4)
{ECO:0000269|PubMed:9787801};
Vmax=5.07 umol/min/mg enzyme for H(2)O(2)
{ECO:0000269|PubMed:2373154};
Vmax=1810 nmol/min/mg enzyme for H(2)O(2)
{ECO:0000269|PubMed:10409692};
Vmax=8.56 umol/min/mg enzyme for tert-butyl hydroperoxide
{ECO:0000269|PubMed:2373154};
Vmax=1270 nmol/min/mg enzyme for tert-butyl hydroperoxide
{ECO:0000269|PubMed:10409692};
Vmax=9.18 umol/min/mg enzyme for cumene hydroperoxide
{ECO:0000269|PubMed:2373154};
Vmax=1120 nmol/min/mg enzyme for cumene hydroperoxide
{ECO:0000269|PubMed:10409692};
Vmax=2.57 umol/min/mg enzyme for triphenylcarbinyl hydroperoxide
{ECO:0000269|PubMed:2373154};
Vmax=9.88 umol/min/mg enzyme for linoleic hydroperoxide
{ECO:0000269|PubMed:2373154};
Vmax=1390 nmol/min/mg enzyme for linolenoyl hydroperoxide
{ECO:0000269|PubMed:10409692};
Vmax=7.34 umol/min/mg enzyme for 5-phenyl-3-pentenyl
hydroperoxide {ECO:0000269|PubMed:2373154};
Vmax=1380 nmol/min/mg enzyme for arachidonoyl hydroperoxide
{ECO:0000269|PubMed:10409692};
Vmax=1500 nmol/min/mg enzyme for PLCP hydroperoxide
{ECO:0000269|PubMed:10409692};
Vmax=1640 nmol/min/mg enzyme for PACP hydroperoxide
{ECO:0000269|PubMed:10409692};
Vmax=4225 nmol/h/mg enzyme for dipalmitoyl phosphatidylcholine
(at pH 4) {ECO:0000269|PubMed:9787801};
pH dependence:
Optimum pH is 7-8. {ECO:0000269|PubMed:10409692};
-!- SUBUNIT: Homodimer (By similarity). Interacts with GSTP1; mediates
PRDX6 glutathionylation and regeneration (PubMed:15004285).
Interacts with APEX1. Interacts with STH. May interact with
FAM168B (By similarity). May interact with HTR2A (By similarity).
{ECO:0000250|UniProtKB:O08709, ECO:0000250|UniProtKB:P30041,
ECO:0000269|PubMed:15004285}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9787801}.
Lysosome {ECO:0000269|PubMed:9787801}. Note=Also found in lung
secretory organelles (lamellar bodies).
{ECO:0000269|PubMed:9787801}.
-!- PTM: Irreversibly inactivated by overoxidation of Cys-47 to
sulfinic acid (Cys-SO(2)H) and sulfonic acid (Cys-SO(3)H) forms
upon oxidative stress. {ECO:0000250|UniProtKB:P30041}.
-!- PTM: Phosphorylation at Thr-177 by MAP kinases increases the
phospholipase activity of the enzyme.
{ECO:0000250|UniProtKB:O35244}.
-!- MISCELLANEOUS: The active site is a conserved redox-active
cysteine residue, the peroxidatic cysteine (C(P)), which makes the
nucleophilic attack on the peroxide substrate. The peroxide
oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which
then reacts with another cysteine residue, the resolving cysteine
(C(R)), to form a disulfide bridge. The disulfide is subsequently
reduced by an appropriate electron donor to complete the catalytic
cycle. In this 1-Cys peroxiredoxin, no C(R) is present and C(P)
instead forms a disulfide with a cysteine from another protein or
with a small thiol molecule. C(P) is reactivated by
glutathionylation mediated by glutathione S-transferase Pi,
followed by spontaneous reduction of the enzyme with glutathione.
{ECO:0000305|PubMed:15004285}.
-!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; AF080228; AAC63016.1; -; mRNA.
EMBL; AF090194; AAC84043.1; -; mRNA.
EMBL; AJ243848; CAB64802.1; -; mRNA.
EMBL; BT020967; AAX08984.1; -; mRNA.
EMBL; BC102172; AAI02173.1; -; mRNA.
RefSeq; NP_777068.1; NM_174643.1.
UniGene; Bt.49705; -.
ProteinModelPortal; O77834; -.
SMR; O77834; -.
STRING; 9913.ENSBTAP00000006383; -.
PeroxiBase; 4423; Bt1CysPrx.
PaxDb; O77834; -.
PeptideAtlas; O77834; -.
PRIDE; O77834; -.
Ensembl; ENSBTAT00000006383; ENSBTAP00000006383; ENSBTAG00000004855.
GeneID; 282438; -.
KEGG; bta:282438; -.
CTD; 9588; -.
eggNOG; KOG0854; Eukaryota.
eggNOG; COG0450; LUCA.
GeneTree; ENSGT00550000074794; -.
HOGENOM; HOG000022346; -.
HOVERGEN; HBG105234; -.
InParanoid; O77834; -.
KO; K11188; -.
OMA; YPIIADD; -.
OrthoDB; EOG091G0IWK; -.
TreeFam; TF105183; -.
BRENDA; 1.11.1.15; 908.
Reactome; R-BTA-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-BTA-6798695; Neutrophil degranulation.
Proteomes; UP000009136; Chromosome 16.
Bgee; ENSBTAG00000004855; -.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:AgBase.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0045296; F:cadherin binding; IEA:Ensembl.
GO; GO:0047499; F:calcium-independent phospholipase A2 activity; IEA:Ensembl.
GO; GO:0004602; F:glutathione peroxidase activity; IEA:Ensembl.
GO; GO:0004601; F:peroxidase activity; ISS:AgBase.
GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC.
GO; GO:0102567; F:phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine); IEA:UniProtKB-EC.
GO; GO:0102568; F:phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine); IEA:UniProtKB-EC.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0046475; P:glycerophospholipid catabolic process; IEA:Ensembl.
GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IEA:Ensembl.
GO; GO:0000302; P:response to reactive oxygen species; ISS:AgBase.
InterPro; IPR000866; AhpC/TSA.
InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
InterPro; IPR019479; Peroxiredoxin_C.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR013766; Thioredoxin_domain.
Pfam; PF10417; 1-cysPrx_C; 1.
Pfam; PF00578; AhpC-TSA; 1.
PIRSF; PIRSF000239; AHPC; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS51352; THIOREDOXIN_2; 1.
1: Evidence at protein level;
Acetylation; Antioxidant; Complete proteome; Cytoplasm;
Direct protein sequencing; Hydrolase; Lipid degradation;
Lipid metabolism; Lysosome; Multifunctional enzyme; Oxidoreductase;
Peroxidase; Phosphoprotein; Redox-active center; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P30041}.
CHAIN 2 224 Peroxiredoxin-6.
/FTId=PRO_0000135101.
DOMAIN 5 169 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
REGION 31 40 Required and sufficient for targeting to
lysosomes and lamellar bodies.
{ECO:0000250|UniProtKB:O35244}.
ACT_SITE 47 47 Cysteine sulfenic acid (-SOH)
intermediate; for peroxidase activity.
{ECO:0000250|UniProtKB:P30041}.
ACT_SITE 140 140 For phospholipase activity.
{ECO:0000250|UniProtKB:O35244}.
SITE 32 32 Important for phospholipase activity.
{ECO:0000250|UniProtKB:O35244}.
MOD_RES 44 44 Phosphothreonine.
{ECO:0000250|UniProtKB:P30041}.
MOD_RES 63 63 N6-acetyllysine.
{ECO:0000250|UniProtKB:P30041}.
MOD_RES 89 89 Phosphotyrosine.
{ECO:0000250|UniProtKB:P30041}.
MOD_RES 177 177 Phosphothreonine; by MAPK.
{ECO:0000250|UniProtKB:O35244}.
MOD_RES 209 209 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P30041}.
MOD_RES 209 209 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:O08709}.
SEQUENCE 224 AA; 25067 MW; 4013D59C4D9FC05E CRC64;
MPGGLLLGDE APNFEANTTI GRIRFHDYLG DSWGILFSHP RDFTPVCTTE LGRAAKLAPE
FAKRNVKMIA LSIDSVEDHL AWSKDINAYN GEEPTEKLPF PIIDDKNRDL AIQLGMLDPA
EKDEKGMPVT ARVVFIFGPD KKLKLSILYP ATTGRNFDEI LRVIISLQLT AEKRVATPVD
WKNGDSVMVL PTIPEEEAKK LFPKGVFTKE LPSGKKYLRY TPQP


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