LANC1_RAT
ID LANC1_RAT Reviewed; 399 AA.
AC Q9QX69; Q9ER29;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Glutathione S-transferase LANCL1 {ECO:0000250|UniProtKB:O89112};
DE EC=2.5.1.18 {ECO:0000250|UniProtKB:O89112};
DE AltName: Full=40 kDa erythrocyte membrane protein;
DE Short=p40 {ECO:0000303|PubMed:10944443};
DE AltName: Full=LanC-like protein 1 {ECO:0000250|UniProtKB:O43813};
GN Name=Lancl1 {ECO:0000312|RGD:69416};
GN Synonyms=Gpr69a {ECO:0000303|PubMed:10944443};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=10944443; DOI=10.1006/bbrc.2000.3260;
RA Bauer H., Mayer H., Marchler-Bauer A., Salzer U., Prohaska R.;
RT "Characterization of p40/GPR69A as a peripheral membrane protein related to
RT the lantibiotic synthetase component C.";
RL Biochem. Biophys. Res. Commun. 275:69-74(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=11376939; DOI=10.1016/s0378-1119(01)00463-2;
RA Mayer H., Bauer H., Breuss J., Ziegler S., Prohaska R.;
RT "Characterization of rat LANCL1, a novel member of the lanthionine
RT synthetase C-like protein family, highly expressed in testis and brain.";
RL Gene 269:73-80(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. Mitigates neuronal
CC oxidative stress during normal postnatal development and in response to
CC oxidative stresses probably through GSH antioxidant defense mechanism
CC (By similarity). May play a role in EPS8 signaling. Binds glutathione
CC (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 -!- 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: Strongly expressed in the brain, testis and
CC skeletal muscle. Expressed in the neurons of the cerebellum, the
CC germinal cells of the seminiferous tubules in testis, in liver
CC hepoatocytes and in cardiac myocytes. {ECO:0000269|PubMed:11376939}.
CC -!- SIMILARITY: Belongs to the LanC-like protein family. {ECO:0000305}.
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DR EMBL; AJ131111; CAB63943.1; -; mRNA.
DR EMBL; AJ295233; CAC16089.1; -; mRNA.
DR EMBL; BC085811; AAH85811.1; -; mRNA.
DR RefSeq; NP_446175.1; NM_053723.1.
DR AlphaFoldDB; Q9QX69; -.
DR SMR; Q9QX69; -.
DR BioGRID; 250361; 2.
DR IntAct; Q9QX69; 4.
DR MINT; Q9QX69; -.
DR STRING; 10116.ENSRNOP00000018293; -.
DR iPTMnet; Q9QX69; -.
DR PhosphoSitePlus; Q9QX69; -.
DR jPOST; Q9QX69; -.
DR PaxDb; Q9QX69; -.
DR PRIDE; Q9QX69; -.
DR GeneID; 114515; -.
DR KEGG; rno:114515; -.
DR UCSC; RGD:69416; rat.
DR CTD; 10314; -.
DR RGD; 69416; Lancl1.
DR VEuPathDB; HostDB:ENSRNOG00000013557; -.
DR eggNOG; KOG2787; Eukaryota.
DR HOGENOM; CLU_036244_0_0_1; -.
DR InParanoid; Q9QX69; -.
DR OMA; YSLVFIN; -.
DR OrthoDB; 681208at2759; -.
DR PhylomeDB; Q9QX69; -.
DR TreeFam; TF300068; -.
DR PRO; PR:Q9QX69; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000013557; Expressed in testis and 19 other tissues.
DR Genevisible; Q9QX69; RN.
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:0050750; F:low-density lipoprotein particle receptor binding; ISO:RGD.
DR GO; GO:0017124; F:SH3 domain binding; ISO:RGD.
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; ISS:UniProtKB.
DR GO; GO:1903203; P:regulation of oxidative stress-induced neuron death; ISS: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_0000191270"
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"
SQ SEQUENCE 399 AA; 45240 MW; F7D4968CB2CFE257 CRC64;
MAQRAFPNPY ADYNKSLAEN YFDSTGRLTP EFSHRLTNKI RELLQQMERG LKSADPQDGT
GYTGWAGIAV LYLHLHNVFG DPAYLQMAHS YVKHSLNCLS RRSITFLCGD AGPLAVAAVL
YHKMNSGKQA EDCITRLIHL NKIDPHVPNE MLYGRIGYIF ALLFVNKNFG EEKIPQSHIQ
QICETILTSG EKLSRKRNFT TKSPLMYEWY QEYYVGAAHG LAGIYYYLMQ PSLHVSQGKL
HSLVKPSVDF VCQLKFPSGN YPSCLDDTRD LLVHWCHGAP GVIYMLIQAY KVFKEEHYLC
DAQQCADVIW QYGLLKKGYG LCHGAAGNAY AFLALYNLTQ DAKYLYRACK FAEWCLDYGE
HGCRTPDTPF SLFEGMAGTI YFLADLLVPT KAKFPAFEL
