LANC1_BOVIN
ID LANC1_BOVIN Reviewed; 399 AA.
AC F1MVX2; Q1LZH8;
DT 31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 67.
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 {ECO:0000250|UniProtKB:Q9QX69};
DE Short=p40 {ECO:0000250|UniProtKB:Q9QX69};
DE AltName: Full=LanC-like protein 1 {ECO:0000250|UniProtKB:O43813};
GN Name=LANCL1 {ECO:0000312|VGNC:VGNC:30783};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000312|Proteomes:UP000009136};
RN [1] {ECO:0000312|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000312|Proteomes:UP000009136};
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2] {ECO:0000312|EMBL:AAI15992.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Hereford {ECO:0000312|EMBL:AAI15992.1};
RC TISSUE=Hypothalamus {ECO:0000312|EMBL:AAI15992.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
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).
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 (By similarity).
CC Binds glutathione (PubMed:17305318). {ECO:0000250|UniProtKB:O43813,
CC ECO:0000250|UniProtKB:O89112, ECO:0000269|PubMed:17305318}.
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 (By similarity). Interaction with
CC EPS8 is inhibited by glutathione binding (By similarity).
CC {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: Expressed in brain. {ECO:0000269|PubMed:17305318}.
CC -!- SIMILARITY: Belongs to the LanC-like protein family. {ECO:0000305}.
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DR EMBL; BC115991; AAI15992.1; -; mRNA.
DR RefSeq; NP_001069695.1; NM_001076227.1.
DR RefSeq; XP_010800568.1; XM_010802266.2.
DR RefSeq; XP_010800569.1; XM_010802267.2.
DR AlphaFoldDB; F1MVX2; -.
DR SMR; F1MVX2; -.
DR STRING; 9913.ENSBTAP00000020055; -.
DR PaxDb; F1MVX2; -.
DR PRIDE; F1MVX2; -.
DR Ensembl; ENSBTAT00000020055; ENSBTAP00000020055; ENSBTAG00000015066.
DR Ensembl; ENSBTAT00000072448; ENSBTAP00000069976; ENSBTAG00000015066.
DR GeneID; 540559; -.
DR KEGG; bta:540559; -.
DR CTD; 10314; -.
DR VEuPathDB; HostDB:ENSBTAG00000015066; -.
DR VGNC; VGNC:30783; LANCL1.
DR eggNOG; KOG2787; Eukaryota.
DR GeneTree; ENSGT00530000063186; -.
DR HOGENOM; CLU_036244_0_0_1; -.
DR InParanoid; F1MVX2; -.
DR OMA; YSLVFIN; -.
DR OrthoDB; 681208at2759; -.
DR TreeFam; TF300068; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000015066; Expressed in occipital lobe and 104 other tissues.
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; IEA:Ensembl.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IEA:Ensembl.
DR GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0043523; P:regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:1903203; P:regulation of oxidative stress-induced neuron death; IEA:Ensembl.
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_0000447675"
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 CONFLICT 145
FT /note="P -> R (in Ref. 2; AAI15992)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="K -> E (in Ref. 2; AAI15992)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 399 AA; 45309 MW; B47EBEFA14A521C0 CRC64;
MAQRAFPNPY ADYNKSLAEG YFDSAGRLTP EFSQRLNNKI RELLQQMERG LKSADPRDST
VYTGWAGIAV LYLHLYDVFG DPNYLQMAHG YVKQSLNSLS KHSITFLCGD GGPLAVAAVV
HHKMNNEKQA EECITRLIHL NKIDPHAPSE MLYGRMGYIS ALLFVNKNFG EEKIPQSHIQ
QICETVLTSG EDLARKRRFT GKTPLMYEWY QEYYVGAAHG LAGIYYYLMQ PSLQVSHAKL
HNLVKPSVDY VCQLKFPSGN YPPCVDDSRD LLIHWCHGAP GVIYMLTQAY KVFKEERYLN
DAYQCADVIW QYGLLKKGYG LCHGTAGNAY AFLSLYSLTQ DAKYLYRACK FAEWCLDYGE
HGCRTPDTPF SLFEGMAGTI YFLADLLVPT KARFPAFEL
