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Database: UniProt
Entry: Q8CHW0_MOUSE
LinkDB: Q8CHW0_MOUSE
Original site: Q8CHW0_MOUSE 
ID   Q8CHW0_MOUSE            Unreviewed;       148 AA.
AC   Q8CHW0;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 66.
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};
DE   Flags: Fragment;
GN   Name=Lancl1 {ECO:0000313|EMBL:AAH38649.1,
GN   ECO:0000313|MGI:MGI:1336997};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|EMBL:AAH38649.1};
RN   [1] {ECO:0000313|EMBL:AAH38649.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:AAH38649.1};
RC   TISSUE=Mammary gland {ECO:0000313|EMBL:AAH38649.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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   EMBL; BC038649; AAH38649.1; -; mRNA.
DR   AlphaFoldDB; Q8CHW0; -.
DR   PeptideAtlas; Q8CHW0; -.
DR   AGR; MGI:1336997; -.
DR   MGI; MGI:1336997; Lancl1.
DR   ChiTaRS; Lancl1; mouse.
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   SUPFAM; SSF158745; LanC-like; 1.
PE   2: Evidence at transcript level;
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}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAH38649.1"
SQ   SEQUENCE   148 AA;  17123 MW;  ED831481247D1802 CRC64;
     QAEECITRLI HLNKIDPHVP NEMLYGRIGY IFALLFVNKN FGEEKIPQSH IQQICENILT
     SGENLSRKRN FAAKSPLMYE WYQEYYVGAA HGLAGIYYYL MQPSLQVNQG KLHSLVKPSV
     DFVCRLKFPS GNYPPCLDDT RDLLVHWC
//
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