LOCUS NP_999215 241 aa linear MAM 27-APR-2020
DEFINITION glutathione S-transferase omega-1 [Sus scrofa].
ACCESSION NP_999215
VERSION NP_999215.1
DBSOURCE REFSEQ: accession NM_214050.2
KEYWORDS RefSeq.
SOURCE Sus scrofa (pig)
ORGANISM Sus scrofa
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae;
Sus.
REFERENCE 1 (residues 1 to 241)
AUTHORS Uenishi H, Eguchi-Ogawa T, Shinkai H, Okumura N, Suzuki K, Toki D,
Hamasima N and Awata T.
TITLE PEDE (Pig EST Data Explorer) has been expanded into Pig Expression
Data Explorer, including 10 147 porcine full-length cDNA sequences
JOURNAL Nucleic Acids Res. 35 (Database issue), D650-D653 (2007)
PUBMED 17145712
REFERENCE 2 (residues 1 to 241)
AUTHORS Uenishi H, Eguchi T, Suzuki K, Sawazaki T, Toki D, Shinkai H,
Okumura N, Hamasima N and Awata T.
TITLE PEDE (Pig EST Data Explorer): construction of a database for ESTs
derived from porcine full-length cDNA libraries
JOURNAL Nucleic Acids Res. 32 (Database issue), D484-D488 (2004)
PUBMED 14681463
REFERENCE 3 (residues 1 to 241)
AUTHORS Rouimi P, Anglade P, Benzekri A, Costet P, Debrauwer L, Pineau T
and Tulliez J.
TITLE Purification and characterization of a glutathione S-transferase
Omega in pig: evidence for two distinct organ-specific transcripts
JOURNAL Biochem. J. 358 (Pt 1), 257-262 (2001)
PUBMED 11485575
COMMENT PROVISIONAL REFSEQ: This record has not yet been subject to final
NCBI review. The reference sequence was derived from AF188838.3.
##Evidence-Data-START##
Transcript exon combination :: AF188838.3, AK391766.1 [ECO:0000332]
RNAseq introns :: single sample supports all introns
SAMEA1876824, SAMEA1876828
[ECO:0000348]
##Evidence-Data-END##
FEATURES Location/Qualifiers
source 1..241
/organism="Sus scrofa"
/db_xref="taxon:9823"
/chromosome="14"
/map="14"
Protein 1..241
/product="glutathione S-transferase omega-1"
/EC_number="2.5.1.18"
/EC_number="1.8.5.1"
/EC_number="1.20.4.2"
/note="GSTO-1; glutathione-dependent dehydroascorbate
reductase; MMA(V) reductase; monomethylarsonic acid
reductase; S-(Phenacyl)glutathione reductase; glutathione
S-transferase omega 1-1"
/calculated_mol_wt=27288
Site 2
/site_type="acetylation"
/note="N-acetylserine.
/evidence=ECO:0000250|UniProtKB:P78417; propagated from
UniProtKB/Swiss-Prot (Q9N1F5.2)"
Region 5..94
/region_name="GST_N_Omega"
/note="GST_N family, Class Omega subfamily; GSTs are
cytosolic dimeric proteins involved in cellular
detoxification by catalyzing the conjugation of
glutathione (GSH) with a wide range of endogenous and
xenobiotic alkylating agents, including carcinogens;
cd03055"
/db_xref="CDD:239353"
Site order(7..8,29..31,33,36..37,39..41,43..44,55,57)
/site_type="other"
/note="C-terminal domain interface [polypeptide binding]"
/db_xref="CDD:239353"
Region 26..225
/region_name="GstA"
/note="Glutathione S-transferase [Posttranslational
modification, protein turnover, chaperones]; COG0625"
/db_xref="CDD:223698"
Site order(32,34,59,71..73,85..86)
/site_type="other"
/note="GSH binding site (G-site) [chemical binding]"
/db_xref="CDD:239353"
Site 32
/site_type="active"
/note="active site cysteine [active]"
/db_xref="CDD:239353"
Site 57
/site_type="acetylation"
/note="N6-acetyllysine.
/evidence=ECO:0000250|UniProtKB:P78417; propagated from
UniProtKB/Swiss-Prot (Q9N1F5.2)"
Site order(71,84..85,87..88,91)
/site_type="other"
/note="putative dimer interface [polypeptide binding]"
/db_xref="CDD:239353"
Region 85..86
/region_name="Glutathione binding.
/evidence=ECO:0000250|UniProtKB:P78417"
/note="propagated from UniProtKB/Swiss-Prot (Q9N1F5.2)"
Region 108..229
/region_name="GST_C_Omega"
/note="C-terminal, alpha helical domain of Class Omega
Glutathione S-transferases; cd03184"
/db_xref="CDD:198293"
Site order(114..115,118..119,122,152)
/site_type="other"
/note="putative dimer interface [polypeptide binding]"
/db_xref="CDD:198293"
Site order(121,124..125,128..129,180,183,222)
/site_type="other"
/note="substrate binding pocket (H-site) [chemical
binding]"
/db_xref="CDD:198293"
Site 143
/site_type="acetylation"
/note="N6-acetyllysine.
/evidence=ECO:0000250|UniProtKB:P78417; propagated from
UniProtKB/Swiss-Prot (Q9N1F5.2)"
Site 148
/site_type="acetylation"
/note="N6-acetyllysine.
/evidence=ECO:0000250|UniProtKB:P78417; propagated from
UniProtKB/Swiss-Prot (Q9N1F5.2)"
Site 152
/site_type="acetylation"
/note="N6-acetyllysine.
/evidence=ECO:0000250|UniProtKB:P78417; propagated from
UniProtKB/Swiss-Prot (Q9N1F5.2)"
Site order(172,175..176,179,182..183,211,215,225,229)
/site_type="other"
/note="N-terminal domain interface [polypeptide binding]"
/db_xref="CDD:198293"
CDS 1..241
/gene="GSTO1"
/gene_synonym="GSTO 1-1; SPG-R"
/coded_by="NM_214050.2:73..798"
/db_xref="GeneID:397117"
ORIGIN
1 msggsarslg kgsappgpvp eglirvysmr fcpfaqrtll vlnakgirhq vininlknkp
61 ewffqknpsg lvpvlensqg qliyesaitc eyldeaypgk kllpddpyek acqkmvfels
121 skvppllirf irreneadcs glkeelrkef skleevltkk kttyfggssl smidyliwpw
181 ferlealeln ecidhtpklk lwmaammkdp avsalhiepr dlrafndlyl qnspeacdyg
241 l
//
