ID A0A3B3T809_9TELE Unreviewed; 405 AA.
AC A0A3B3T809;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Glutathione S-transferase LANCL1 {ECO:0000256|ARBA:ARBA00039457};
DE EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452};
DE AltName: Full=LanC-like protein 1 {ECO:0000256|ARBA:ARBA00043169};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000038795.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000038795.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-chloro-2,4-dinitrobenzene + glutathione = 2,4-dinitrophenyl-
CC S-glutathione + chloride + H(+); Xref=Rhea:RHEA:51220,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17996, ChEBI:CHEBI:34718,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:133977; EC=2.5.1.18;
CC Evidence={ECO:0000256|ARBA:ARBA00035808};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + RX = a halide anion + an S-substituted
CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:90779; EC=2.5.1.18;
CC Evidence={ECO:0000256|ARBA:ARBA00000710};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cytoplasm
CC {ECO:0000256|ARBA:ARBA00004496}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the LanC-like protein family.
CC {ECO:0000256|ARBA:ARBA00007179}.
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DR AlphaFoldDB; A0A3B3T809; -.
DR Ensembl; ENSPKIT00000019790.1; ENSPKIP00000038795.1; ENSPKIG00000016438.1.
DR GeneTree; ENSGT00530000063186; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0031179; P:peptide modification; IEA:InterPro.
DR CDD; cd04794; euk_LANCL; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR007822; LANC-like.
DR InterPro; IPR020464; LanC-like_prot_euk.
DR PANTHER; PTHR12736:SF5; GLUTATHIONE S-TRANSFERASE LANCL1; 1.
DR PANTHER; PTHR12736; LANC-LIKE PROTEIN; 1.
DR Pfam; PF05147; LANC_like; 1.
DR PRINTS; PR01951; LANCEUKARYTE.
DR PRINTS; PR01950; LANCSUPER.
DR SMART; SM01260; LANC_like; 1.
DR SUPFAM; SSF158745; LanC-like; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ SEQUENCE 405 AA; 45495 MW; E5BFC5ED7223967D CRC64;
MINTENRTPV WGGREAGTKT AWKRERKIQL TSDFIGRLRA KVTELLSQME NGLRSADPRD
CSGYTGWAGI ALLYLHLDSV FGESSFLQRA LDHVSRSLQC LTRRTVTFLC GDSGPLAVAA
VVYHRLGRSQ EAEECLGRLL QMHESVVKGK GNLPDELLYG RVGYLYSLIF INQQFGHEKV
PSQYIQQICE AVLASGENLS RKRQTQEQTP LLYEWYQEYY VGAAHGLAGI YYFLMQPGFG
VGEERRLRLV KPSVDYVQRL KFPSGNYPPC IGDSRDLLVH WCHGSPGVIH MLLQAHKVYG
GDGYLGDALQ CGEVIWTWGL LQKGYGLCHG AAGNAYAFLA LYKATGDLKH LYRACKFAEW
CMDYGKHGCR TPDTPFSLFE GMAGTVYFLA DLTQPLRSKF PAYEI
//
