ID A0A1S3MTJ9_SALSA Unreviewed; 408 AA.
AC A0A1S3MTJ9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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};
GN Name=LOC106574849 {ECO:0000313|RefSeq:XP_014006430.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014006430.1};
RN [1] {ECO:0000313|RefSeq:XP_014006430.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014006430.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_014006430.1; XM_014150955.1.
DR AlphaFoldDB; A0A1S3MTJ9; -.
DR STRING; 8030.ENSSSAP00000034267; -.
DR PaxDb; 8030-ENSSSAP00000034267; -.
DR GeneID; 106574849; -.
DR KEGG; sasa:106574849; -.
DR OMA; YSLVFIN; -.
DR OrthoDB; 1377744at2759; -.
DR Proteomes; UP000087266; Chromosome ssa16.
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 Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ SEQUENCE 408 AA; 45806 MW; B3DE9E13CABBBCE2 CRC64;
MDQRAWKNPY ADYDGNPASV QELFDSQGKL TAEFAGRLSN AISQLLMHME NGLKSADPRD
CTGYTGWAGI ALLYLHLHGV FGEPSFLQKA LDYVGHSLTC PTRRRDVTFL CGDAGPLAVA
AVVYHRVQRA QESDECLSRL LQLHQSVVMG SGASGLPDEL LYGRMGYLYA LTFINQQFGH
DKIPIQYIQQ ICEAVLISGE AQSQRFRCQD QSPLMYEWYQ EQYVGPAHGL AGIYYFLMQP
GYVAGDERVH RLVRPSVDHV CRLRFPTGNY PPCIGDNRDL LVHWCHGAPG IIYMLLQAYK
VFGVGQYLEE ALQCGEVVWH RGLLKKGYGL CHGAAGNAYA FLALYKLTHD PKHLYRACMF
ADWCMNYGKH GCRTPDTPFS LFEGMAGTIY FLADLLQPLK SKFPAFEV
//