LANC1_MOUSE
ID LANC1_MOUSE Reviewed; 399 AA.
AC O89112;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Glutathione S-transferase LANCL1 {ECO:0000305|PubMed:25158856};
DE EC=2.5.1.18 {ECO:0000269|PubMed:25158856};
DE AltName: Full=40 kDa erythrocyte membrane protein;
DE Short=p40 {ECO:0000250|UniProtKB:Q9QX69};
DE AltName: Full=LanC-like protein 1 {ECO:0000250|UniProtKB:O43813};
GN Name=Lancl1 {ECO:0000312|MGI:MGI:1336997};
GN Synonyms=Gpr69a {ECO:0000250|UniProtKB:Q9QX69};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Brain, Diaphragm, and Fetal brain;
RX PubMed=9714732; DOI=10.1016/s0167-4781(98)00091-8;
RA Mayer H., Breuss J., Ziegler S., Prohaska R.;
RT "Molecular characterization and tissue-specific expression of a murine
RT putative G-protein-coupled receptor.";
RL Biochim. Biophys. Acta 1399:51-56(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Brain, and Testis;
RX PubMed=11474189; DOI=10.1159/000056958;
RA Mayer H., Bauer H., Prohaska R.;
RT "Organization and chromosomal localization of the human and mouse genes
RT coding for LanC-like protein 1 (LANCL1).";
RL Cytogenet. Cell Genet. 93:100-104(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland, and Olfactory epithelium;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
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).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=17305318; DOI=10.1021/bi061888s;
RA Chung C.H.Y., Kurien B.T., Mehta P., Mhatre M., Mou S., Pye Q.N.,
RA Stewart C., West M., Williamson K.S., Post J., Liu L., Wang R., Hensley K.;
RT "Identification of lanthionine synthase C-like protein-1 as a prominent
RT glutathione binding protein expressed in the mammalian central nervous
RT system.";
RL Biochemistry 46:3262-3269(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, DISRUPTION PHENOTYPE, MUTAGENESIS
RP OF ARG-4, AND CATALYTIC ACTIVITY.
RX PubMed=25158856; DOI=10.1016/j.devcel.2014.06.011;
RA Huang C., Chen M., Pang D., Bi D., Zou Y., Xia X., Yang W., Luo L.,
RA Deng R., Tan H., Zhou L., Yu S., Guo L., Du X., Cui Y., Hu J., Mao Q.,
RA Worley P.F., Xiao B.;
RT "Developmental and activity-dependent expression of LanCL1 confers
RT antioxidant activity required for neuronal survival.";
RL Dev. Cell 30:479-487(2014).
CC -!- FUNCTION: Functions as glutathione transferase (PubMed:25158856).
CC Catalyzes conjugation of the glutathione (GSH) to artificial substrates
CC 1-chloro-2,4-dinitrobenzene (CDNB) and p-nitrophenyl acetate
CC (PubMed:25158856). Mitigates neuronal oxidative stress during normal
CC postnatal development and in response to oxidative stresses probably
CC through GSH antioxidant defense mechanism (PubMed:25158856). May play a
CC role in EPS8 signaling. Binds glutathione (By similarity).
CC {ECO:0000250|UniProtKB:O43813, ECO:0000269|PubMed:25158856}.
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:0000269|PubMed:25158856};
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:0000269|PubMed:25158856};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.93 mM for 1-chloro-2,4-dinitrobenzene
CC {ECO:0000269|PubMed:25158856};
CC Vmax=1087 nmol/min/mg enzyme {ECO:0000269|PubMed:25158856};
CC -!- SUBUNIT: Interacts with the C-terminal of STOM (By similarity).
CC Interacts with the EPS8 SH3 domain. Interaction with EPS8 is inhibited
CC by glutathione binding (By similarity). {ECO:0000250|UniProtKB:O43813}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O43813}. Cell
CC membrane {ECO:0000250|UniProtKB:O43813}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O43813}.
CC -!- TISSUE SPECIFICITY: Detected in spinal cord (at protein level).
CC Ubiquitous. Strongly expressed in brain, testis, alveolar macrophages
CC and epithelial cells of the lung, kidney and intestine
CC (PubMed:17305318, PubMed:9714732). Expression in brain increases during
CC the first postnatal month and remaining high in adult
CC (PubMed:25158856). {ECO:0000269|PubMed:17305318,
CC ECO:0000269|PubMed:25158856, ECO:0000269|PubMed:9714732}.
CC -!- INDUCTION: Induced by oxidative stress. {ECO:0000269|PubMed:25158856}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice are viable. During later postnatal
CC development, mice demonstrate prominent neuronal degeneration.
CC {ECO:0000269|PubMed:25158856}.
CC -!- MISCELLANEOUS: Was originally thought to be a G-protein coupled
CC receptor. {ECO:0000305|PubMed:9714732}.
CC -!- SIMILARITY: Belongs to the LanC-like protein family. {ECO:0000305}.
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DR EMBL; Y11550; CAA72314.1; -; mRNA.
DR EMBL; Y16518; CAA76269.1; -; mRNA.
DR EMBL; AJ294535; CAC69241.1; -; mRNA.
DR EMBL; AJ289603; CAC40153.1; -; Genomic_DNA.
DR EMBL; AJ289604; CAC40153.1; JOINED; Genomic_DNA.
DR EMBL; AJ289605; CAC40153.1; JOINED; Genomic_DNA.
DR EMBL; AJ289606; CAC40153.1; JOINED; Genomic_DNA.
DR EMBL; AJ289607; CAC40153.1; JOINED; Genomic_DNA.
DR EMBL; AJ289608; CAC40153.1; JOINED; Genomic_DNA.
DR EMBL; BC058560; AAH58560.1; -; mRNA.
DR CCDS; CCDS15025.1; -.
DR RefSeq; NP_001177913.1; NM_001190984.1.
DR RefSeq; NP_001177914.1; NM_001190985.1.
DR RefSeq; NP_067270.1; NM_021295.3.
DR AlphaFoldDB; O89112; -.
DR SMR; O89112; -.
DR BioGRID; 200033; 9.
DR IntAct; O89112; 4.
DR STRING; 10090.ENSMUSP00000109612; -.
DR iPTMnet; O89112; -.
DR PhosphoSitePlus; O89112; -.
DR SwissPalm; O89112; -.
DR EPD; O89112; -.
DR MaxQB; O89112; -.
DR PaxDb; O89112; -.
DR PeptideAtlas; O89112; -.
DR PRIDE; O89112; -.
DR ProteomicsDB; 290007; -.
DR Antibodypedia; 34207; 115 antibodies from 20 providers.
DR DNASU; 14768; -.
DR Ensembl; ENSMUST00000027149; ENSMUSP00000027149; ENSMUSG00000026000.
DR Ensembl; ENSMUST00000113979; ENSMUSP00000109612; ENSMUSG00000026000.
DR Ensembl; ENSMUST00000119559; ENSMUSP00000113080; ENSMUSG00000026000.
DR GeneID; 14768; -.
DR KEGG; mmu:14768; -.
DR UCSC; uc007biv.1; mouse.
DR CTD; 10314; -.
DR MGI; MGI:1336997; Lancl1.
DR VEuPathDB; HostDB:ENSMUSG00000026000; -.
DR eggNOG; KOG2787; Eukaryota.
DR GeneTree; ENSGT00530000063186; -.
DR HOGENOM; CLU_036244_0_0_1; -.
DR InParanoid; O89112; -.
DR OMA; YSLVFIN; -.
DR OrthoDB; 681208at2759; -.
DR PhylomeDB; O89112; -.
DR TreeFam; TF300068; -.
DR BioGRID-ORCS; 14768; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Lancl1; mouse.
DR PRO; PR:O89112; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; O89112; protein.
DR Bgee; ENSMUSG00000026000; Expressed in seminiferous tubule of testis and 280 other tissues.
DR ExpressionAtlas; O89112; baseline and differential.
DR Genevisible; O89112; MM.
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; IMP:UniProtKB.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0043523; P:regulation of neuron apoptotic process; IMP:UniProtKB.
DR GO; GO:1903203; P:regulation of oxidative stress-induced neuron death; IMP:UniProtKB.
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 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cytoplasm; Membrane; Metal-binding;
KW Reference proteome; Transferase; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O43813"
FT CHAIN 2..399
FT /note="Glutathione S-transferase LANCL1"
FT /id="PRO_0000191269"
FT BINDING 276
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O43813"
FT BINDING 317
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O43813"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O43813"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O43813"
FT BINDING 364..367
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O43813"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O43813"
FT MOD_RES 142
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O43813"
FT MUTAGEN 4
FT /note="R->A: Does not increase glutathione transferase
FT activity and reduces cellular protection."
FT /evidence="ECO:0000269|PubMed:25158856"
SQ SEQUENCE 399 AA; 45341 MW; 542A628818C30B89 CRC64;
MAQRAFPNPY ADYNKSLAEN YFDSTGRLTP EFSHRLTNKI RELLQQMERG LKSADPRDGT
GYTGWAGIAV LYLHLHNVFG DPAYLQMAHS YVKQSLNCLS RRSITFLCGD AGPLAVAAVL
YHKMNSEKQA EECITRLIHL NKIDPHVPNE MLYGRIGYIF ALLFVNKNFG EEKIPQSHIQ
QICENILTSG ENLSRKRNLA AKSPLMYEWY QEYYVGAAHG LAGIYYYLMQ PSLQVNQGKL
HSLVKPSVDF VCRLKFPSGN YPPCLDDTRD LLVHWCHGAP GVIYMLIQAY KVFKEERYLC
DAQQCADVIW QYGLLKKGYG LCHGAAGNAY AFLALYNLTQ DLKYLYRACK FAEWCLDYGE
HGCRTADTPF SLFEGMAGTI YFLADLLVPT KAKFPAFEL
