Gene name: PRDX6

Uniprot entry:

P30041

Protein names:

Peroxiredoxin-6 (EC 1.11.1.27) (1-Cys peroxiredoxin) (1-Cys PRX) (24 kDa protein) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Antioxidant protein 2) (Glutathione-dependent peroxiredoxin) (Liver 2D page spot 40) (Lysophosphatidylcholine acyltransferase 5) (LPC acyltransferase 5) (LPCAT-5) (Lyso-PC acyltransferase 5) (EC 2.3.1.23) (Non-selenium glutathione peroxidase) (NSGPx) (Red blood cells page spot 12)

Protein sequence:

1_MPGGL 6_ LLGDV 11_ APNFE 16_ ANTTV 21_ GRIRF 26_ HDFLG 31_ DSWGI 36_ LFSHP 41_ RDFTP 46_ VCTTE 51_ LGRAA 56_ KLAPE 61_ FAKRN 66_ VKLIA 71_ LSIDS 76_ VEDHL 81_ AWSKD 86_ INAYN 91_ CEEPT 96_ EKLPF 101_ PIIDD 106_ RNREL 111_ AILLG 116_ MLDPA 121_ EKDEK 126_ GMPVT 131_ ARVVF 136_ VFGPD 141_ KKLKL 146_ SILYP 151_ ATTGR 156_ NFDEI 161_ LRVVI 166_ SLQLT 171_ AEKRV 176_ ATPVD 181_ WKDGD 186_ SVMVL 191_ PTIPE 196_ EEAKK 201_ LFPKG 206_ VFTKE 211_ LPSGK 216_KYLRY

Protein annotations

Protein functions:

1: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (PubMed:10893423, PubMed:9497358). Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides (PubMed:10893423). Also has phospholipase activity, can therefore either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or hydrolyze the sn-2 ester bond of phospholipids (phospholipase activity) (PubMed:10893423, PubMed:26830860). These activities are dependent on binding to phospholipids at acidic pH and to oxidized phospholipds at cytosolic pH (PubMed:10893423). Plays a role in cell protection against oxidative stress by detoxifying peroxides and in phospholipid homeostasis (PubMed:10893423). Exhibits acyl-CoA-dependent lysophospholipid acyltransferase which mediates the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (PubMed:26830860). Shows a clear preference for LPC as the lysophospholipid and for palmitoyl CoA as the fatty acyl substrate (PubMed:26830860)