ID   LANC1_DANRE             Reviewed;         405 AA.
AC   Q90ZL2;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Glutathione S-transferase LANCL1 {ECO:0000250|UniProtKB:O89112};
DE            EC=2.5.1.18 {ECO:0000250|UniProtKB:O89112};
DE   AltName: Full=LanC-like protein 1 {ECO:0000250|UniProtKB:O43813};
GN   Name=lancl1 {ECO:0000250|UniProtKB:O43813};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Pongratz M., Mayer H., Prohaska R.;
RT   "Molecular cloning of zebrafish LANCL1, encoding the lantibiotic synthetase
RT   C (LanC)-like protein 1.";
RL   Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Functions as glutathione transferase. Catalyzes conjugation
CC       of the glutathione (GSH) to artificial substrates 1-chloro-2,4-
CC       dinitrobenzene (CDNB) and p-nitrophenyl acetate (By similarity). Binds
CC       glutathione (By similarity). {ECO:0000250|UniProtKB:O43813,
CC       ECO:0000250|UniProtKB:O89112}.
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:0000250|UniProtKB:O89112};
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:0000250|UniProtKB:O89112};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O43813}. Cell
CC       membrane {ECO:0000250|UniProtKB:O43813}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:O43813}.
CC   -!- SIMILARITY: Belongs to the LanC-like protein family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ278244; CAC39613.1; -; mRNA.
DR   RefSeq; NP_001009891.1; NM_001009891.1.
DR   AlphaFoldDB; Q90ZL2; -.
DR   SMR; Q90ZL2; -.
DR   STRING; 7955.ENSDARP00000018694; -.
DR   PaxDb; Q90ZL2; -.
DR   Ensembl; ENSDART00000016139; ENSDARP00000018694; ENSDARG00000013741.
DR   GeneID; 494154; -.
DR   KEGG; dre:494154; -.
DR   CTD; 10314; -.
DR   ZFIN; ZDB-GENE-040924-1; lancl1.
DR   eggNOG; KOG2787; Eukaryota.
DR   GeneTree; ENSGT00530000063186; -.
DR   HOGENOM; CLU_036244_0_0_1; -.
DR   InParanoid; Q90ZL2; -.
DR   OMA; YSLVFIN; -.
DR   OrthoDB; 681208at2759; -.
DR   PhylomeDB; Q90ZL2; -.
DR   TreeFam; TF300068; -.
DR   PRO; PR:Q90ZL2; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 1.
DR   Bgee; ENSDARG00000013741; Expressed in brain and 25 other tissues.
DR   ExpressionAtlas; Q90ZL2; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0043295; F:glutathione binding; ISS:UniProtKB.
DR   GO; GO:0004364; F:glutathione transferase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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   Pfam; PF05147; LANC_like; 1.
DR   PRINTS; PR01951; LANCEUKARYTE.
DR   PRINTS; PR01950; LANCSUPER.
DR   SMART; SM01260; LANC_like; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cytoplasm; Membrane; Metal-binding; Reference proteome;
KW   Transferase; Zinc.
FT   CHAIN           1..405
FT                   /note="Glutathione S-transferase LANCL1"
FT                   /id="PRO_0000191271"
FT   BINDING         282
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O43813"
FT   BINDING         323
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:O43813"
FT   BINDING         328
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O43813"
FT   BINDING         329
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O43813"
FT   BINDING         370..373
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:O43813"
SQ   SEQUENCE   405 AA;  45752 MW;  541D33E420047068 CRC64;
     MSEQRALKNP YPDYTGLGCA QDLFDMQGNL TQHFATSISS KISELLAILE NGLKNADPRD
     CTGYTGWAGI ALLYLHLHSV FGDPTFLQRA LDYVNRSLRS LTQRWVTFLC GDAGPLAIAA
     VVYHRLQKHQ ESDECLNRLL QLQPSVVQGK GRLPDELLYG RTGYLYSLIF VNQQFQQEKI
     PFQYIQQICD AILESGQILS QRNKIQDQSP LMYEWYQEEY VGAAHGLSGI YYYLMQPGLV
     AGQDRVFSLV KPSVNYVCQL KFPSGNYAPC VGDARDLLVH WCHGSPGVIY MLIQAFKVFG
     VRQYLEDALQ CGEVIWQRGL LKKGYGLCHG AAGNAYGFLA LYKITQDPKH LYRACMFADW
     CMNYGRHGCR TPDTPFSLFE GMAGTIYFLA DLLQPARAKF PCFEV