ID GSTA3_CHICK STANDARD; PRT; 228 AA. AC P26697; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 04-APR-2006, entry version 43. DE Glutathione S-transferase 3 (EC 2.5.1.18) (GST-CL3) (GST class-alpha). OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archosauria; Aves; Neognathae; Galliformes; Phasianidae; Phasianinae; OC Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=White leghorn; TISSUE=Liver; RX MEDLINE=92143826; PubMed=1339283; RA Chang L.-H., Fan J.-Y., Liu L.-F., Tsai S.-P., Tam M.F.; RT "Cloning and expression of a chick liver glutathione S-transferase CL RT 3 subunit with the use of a baculovirus expression system."; RL Biochem. J. 281:545-551(1992). CC -!- FUNCTION: Catalyzes the conjugation of GSH to a wide variety of CC electrophilic alkylating agents. Also involved in the metabolism CC of lipid hydroperoxides, prostaglandins and leukotriene A4 and in CC binding of non-substrate hydrophobic ligands such as bile acids, a CC number of drugs and thyroid hormones. This GST does not exhibit CC peroxidase activity. CC -!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione. CC -!- SUBUNIT: Homodimer or heterodimer (with a subunit from group CC CL-4). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- MISCELLANEOUS: The variations were found from AA sequencing and CC imply there are multiple forms of CL-3. CC -!- SIMILARITY: Belongs to the GST superfamily. Alpha family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M38219; AAA62731.1; -; mRNA. DR PIR; S19734; S19734. DR UniGene; Gga.788; -. DR PDB; 1VF1; X-ray; A=1-228. DR PDB; 1VF2; X-ray; A/B=1-228. DR PDB; 1VF3; X-ray; A/B=1-228. DR PDB; 1VF4; X-ray; A=1-228. DR Ensembl; ENSGALG00000016322; Gallus gallus. DR InterPro; IPR003080; GST_alpha. DR InterPro; IPR004046; GST_C. DR InterPro; IPR010987; GST_C_like. DR InterPro; IPR004045; GST_N. DR InterPro; IPR012336; Thiordxn-like_fd. DR InterPro; IPR012335; Thioredoxin_fold. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF02798; GST_N; 1. DR PRINTS; PR01266; GSTRNSFRASEA. KW 3D-structure; Direct protein sequencing; Polymorphism; Transferase. FT INIT_MET 0 0 FT CHAIN 1 228 Glutathione S-transferase 3. FT /FTId=PRO_0000185800. FT MOD_RES 1 1 Blocked amino end (Ala). FT VARIANT 44 44 L -> V. FT VARIANT 46 46 S -> A. FT VARIANT 48 48 I -> F. FT VARIANT 48 48 I -> V. FT VARIANT 51 51 F -> R. FT VARIANT 128 129 TS -> AN. FT VARIANT 134 135 AY -> VF. FT VARIANT 154 154 W -> R. FT VARIANT 157 158 IH -> VV. FT VARIANT 162 162 A -> T. FT VARIANT 165 165 M -> A. FT VARIANT 167 167 E -> V. FT STRAND 5 8 FT STRAND 10 11 FT TURN 13 15 FT HELIX 16 24 FT TURN 25 26 FT STRAND 30 33 FT STRAND 36 36 FT HELIX 37 46 FT TURN 47 47 FT STRAND 49 49 FT TURN 50 51 FT STRAND 52 52 FT STRAND 54 54 FT STRAND 56 59 FT TURN 60 61 FT STRAND 62 66 FT HELIX 67 77 FT TURN 78 79 FT STRAND 81 81 FT STRAND 83 84 FT HELIX 85 103 FT TURN 104 105 FT STRAND 106 107 FT HELIX 108 110 FT STRAND 111 111 FT HELIX 113 129 FT TURN 130 130 FT HELIX 131 142 FT STRAND 145 148 FT TURN 149 150 FT STRAND 151 151 FT HELIX 154 169 FT TURN 171 176 FT HELIX 178 189 FT STRAND 190 190 FT HELIX 191 197 FT STRAND 198 198 FT TURN 199 200 FT STRAND 201 202 FT HELIX 209 219 FT STRAND 220 220 FT STRAND 223 224 SQ SEQUENCE 228 AA; 26195 MW; C7450E146F41E787 CRC64; AAKPVLYYFN GRGKMESIRW LLAAAGVEFE EVFLETREQY EKLLQSGILM FQQVPMVEID GMKLVQTRAI LNYIAGKYNL YGKDLKERAL IDMYVGGTDD LMGFLLSFPF LSAEDKVKQC AFVVEKATSR YFPAYEKVLK DHGQDFLVGN RLSWADIHLL EAILMVEEKK SDALSGFPLL QAFKKRISSI PTIKKFLAPG SKRKPISDDK YVETVRRVLR MYYDVKPH //