ID A0A3P8XUM3_ESOLU Unreviewed; 479 AA.
AC A0A3P8XUM3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=S-formylglutathione hydrolase {ECO:0000256|ARBA:ARBA00016774, ECO:0000256|RuleBase:RU363068};
DE EC=3.1.2.12 {ECO:0000256|ARBA:ARBA00012479, ECO:0000256|RuleBase:RU363068};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000008146.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000008146.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000008146.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Serine hydrolase involved in the detoxification of
CC formaldehyde. {ECO:0000256|ARBA:ARBA00002608,
CC ECO:0000256|RuleBase:RU363068}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-formylglutathione = formate + glutathione + H(+);
CC Xref=Rhea:RHEA:14961, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:57688, ChEBI:CHEBI:57925; EC=3.1.2.12;
CC Evidence={ECO:0000256|RuleBase:RU363068};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC {ECO:0000256|ARBA:ARBA00004541}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000256|RuleBase:RU000688}.
CC -!- SIMILARITY: Belongs to the esterase D family.
CC {ECO:0000256|ARBA:ARBA00005622, ECO:0000256|RuleBase:RU363068}.
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DR AlphaFoldDB; A0A3P8XUM3; -.
DR Ensembl; ENSELUT00000006059.2; ENSELUP00000008146.2; ENSELUG00000008859.2.
DR GeneTree; ENSGT00390000011864; -.
DR InParanoid; A0A3P8XUM3; -.
DR Proteomes; UP000265140; LG16.
DR Bgee; ENSELUG00000008859; Expressed in stomach and 14 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0018738; F:S-formylglutathione hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0046294; P:formaldehyde catabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000801; Esterase-like.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR014186; S-formylglutathione_hydrol.
DR NCBIfam; TIGR02821; fghA_ester_D; 1.
DR PANTHER; PTHR10061; S-FORMYLGLUTATHIONE HYDROLASE; 1.
DR PANTHER; PTHR10061:SF0; S-FORMYLGLUTATHIONE HYDROLASE; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR Pfam; PF00756; Esterase; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU363068};
KW G-protein coupled receptor {ECO:0000256|RuleBase:RU000688};
KW Hydrolase {ECO:0000256|RuleBase:RU363068};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|RuleBase:RU000688};
KW Reference proteome {ECO:0000313|Proteomes:UP000265140};
KW Serine esterase {ECO:0000256|RuleBase:RU363068};
KW Transducer {ECO:0000256|RuleBase:RU000688};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000688};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 65..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 100..119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 139..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 80..193
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
FT ACT_SITE 346
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT ACT_SITE 423
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
FT ACT_SITE 457
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR614186-1"
SQ SEQUENCE 479 AA; 52505 MW; F84C3C072FAB7B32 CRC64;
MGTDIMNLHG NVSEGLLGNG GRNGCNGNDI LSGNLTQGGG GYSEETKILA SSQCATGMTA
VDKNWAALLI LAVIAITVTG NILVIIAVSL EKKLQNATNY FLMSLAVADM LLGILVMPVS
MVTILYEYRW PLPSDLCPIW IYLDVLFSTA SIMHLCAISL DRYIAIRNPL HHSRFNSRTK
ARLKIMAVWT ISVGNGKMSL TQVTSNKCSG GYQKVFEHDS TELKCKMKFA IYLPPKAENG
KCPVFYWLSG LTCTEQNFIT KAGSQQAASE HGLIIVAPDT SPRGCNIEGE DESWDFGTGA
GFYVNATQEP WKTNYRMYAY VTEELPSLIN ANFPADPEKM SISGHSMGGH GALICALKNP
GKYKAVSAFA PICNPMQCAW GQKAFTGYLG EDKKDWESYD ATVLAGSYCG PQLDILIDQG
RDDQFLSASQ LLPDNLIAAC SEKKIPVVFR LQPGYDHSYY FIYSFINDHI KHHAKFLNA
//
