ID I3LEI1_PIG Unreviewed; 146 AA.
AC I3LEI1; A0A4X1VVE8;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Leukotriene C4 synthase {ECO:0000256|ARBA:ARBA00039419};
DE EC=4.4.1.20 {ECO:0000256|ARBA:ARBA00039056};
DE AltName: Full=Glutathione S-transferase LTC4 {ECO:0000256|ARBA:ARBA00041943};
DE AltName: Full=Leukotriene-C(4) synthase {ECO:0000256|ARBA:ARBA00041224};
GN Name=LTC4S {ECO:0000313|Ensembl:ENSSSCP00000022469.1,
GN ECO:0000313|VGNC:VGNC:89890};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000022469.1, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000022469.1, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000022469.1,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HDA48771.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30723633; DOI=.7717/peerj.6374;
RA Gilbert D.G.;
RT "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL PeerJ 7:E6374-E6374(2019).
RN [3] {ECO:0000313|Ensembl:ENSSSCP00000022469.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(13S,14S)-epoxy-(4Z,7Z,9E,11E,16Z,19Z)-docosahexaenoate +
CC glutathione = (13R)-S-glutathionyl-(14S)-hydroxy-
CC (4Z,7Z,9E,11E,16Z,19Z)-docosahexaenoate; Xref=Rhea:RHEA:53508,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:131958, ChEBI:CHEBI:137407;
CC Evidence={ECO:0000256|ARBA:ARBA00036460};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53509;
CC Evidence={ECO:0000256|ARBA:ARBA00036460};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=leukotriene C4 = glutathione + leukotriene A4;
CC Xref=Rhea:RHEA:17617, ChEBI:CHEBI:57463, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:57973; EC=4.4.1.20;
CC Evidence={ECO:0000256|ARBA:ARBA00036712};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17619;
CC Evidence={ECO:0000256|ARBA:ARBA00036712};
CC -!- PATHWAY: Lipid metabolism; leukotriene C4 biosynthesis.
CC {ECO:0000256|ARBA:ARBA00037884}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Nucleus outer membrane
CC {ECO:0000256|ARBA:ARBA00037823}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00037823}.
CC -!- SIMILARITY: Belongs to the MAPEG family.
CC {ECO:0000256|ARBA:ARBA00010459}.
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DR EMBL; DQIR01093295; HDA48771.1; -; Transcribed_RNA.
DR RefSeq; XP_003123693.2; XM_003123645.4.
DR STRING; 9823.ENSSSCP00000022469; -.
DR PaxDb; 9823-ENSSSCP00000022469; -.
DR Ensembl; ENSSSCT00000024428.2; ENSSSCP00000022469.1; ENSSSCG00000028488.4.
DR Ensembl; ENSSSCT00005011813.1; ENSSSCP00005006877.1; ENSSSCG00005007799.1.
DR GeneID; 100520063; -.
DR KEGG; ssc:100520063; -.
DR CTD; 4056; -.
DR VGNC; VGNC:89890; LTC4S.
DR eggNOG; ENOG502RZYY; Eukaryota.
DR GeneTree; ENSGT00940000160738; -.
DR HOGENOM; CLU_110291_3_0_1; -.
DR OMA; AGIYFHE; -.
DR OrthoDB; 5396066at2759; -.
DR TreeFam; TF105328; -.
DR Reactome; R-SSC-2142688; Synthesis of 5-eicosatetraenoic acids.
DR Reactome; R-SSC-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
DR Reactome; R-SSC-2142700; Synthesis of Lipoxins (LX).
DR Reactome; R-SSC-9026762; Biosynthesis of maresin conjugates in tissue regeneration (MCTR).
DR Reactome; R-SSC-9026766; Biosynthesis of protectin and resolvin conjugates in tissue regeneration (PCTR and RCTR).
DR Proteomes; UP000008227; Chromosome 2.
DR Bgee; ENSSSCG00000028488; Expressed in liver and 37 other cell types or tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR GO; GO:0005640; C:nuclear outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008047; F:enzyme activator activity; IEA:InterPro.
DR GO; GO:0004602; F:glutathione peroxidase activity; IBA:GO_Central.
DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0004464; F:leukotriene-C4 synthase activity; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; IEA:Ensembl.
DR GO; GO:0019370; P:leukotriene biosynthetic process; IBA:GO_Central.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IEA:Ensembl.
DR Gene3D; 1.20.120.550; Membrane associated eicosanoid/glutathione metabolism-like domain; 1.
DR InterPro; IPR001446; 5_LipOase_AP.
DR InterPro; IPR018295; FLAP/GST2/LTC4S_CS.
DR InterPro; IPR023352; MAPEG-like_dom_sf.
DR InterPro; IPR001129; Membr-assoc_MAPEG.
DR PANTHER; PTHR10250:SF4; LEUKOTRIENE C4 SYNTHASE; 1.
DR PANTHER; PTHR10250; MICROSOMAL GLUTATHIONE S-TRANSFERASE; 1.
DR Pfam; PF01124; MAPEG; 1.
DR PRINTS; PR00488; 5LPOXGNASEAP.
DR SUPFAM; SSF161084; MAPEG domain-like; 1.
DR PROSITE; PS01297; FLAP_GST2_LTC4S; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Leukotriene biosynthesis {ECO:0000256|ARBA:ARBA00022751};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Proteomics identification {ECO:0007829|PeptideAtlas:I3LEI1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 67..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 109..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 146 AA; 16255 MW; A6C9165CB6E55435 CRC64;
MKDEVALLAT VTLLGVLLQA YFSLQVISAR RAFRVSPPLT TGPPEFERVY RAQVNCSEYF
PLLLATLWVA GIYFHEGAAA LCGLIYLYAR FRYFQGYARS AQQRLAPMYA SACALWLLLA
LAALGLLAHF LPAALRTELQ ELLPRA
//
