PDES1_BOVIN
ID PDES1_BOVIN Reviewed; 271 AA.
AC A6QLM0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Plasmanylethanolamine desaturase {ECO:0000250|UniProtKB:A5PLL7};
DE EC=1.14.19.77 {ECO:0000250|UniProtKB:A5PLL7};
DE AltName: Full=Plasmanylethanolamine desaturase 1 {ECO:0000250|UniProtKB:A5PLL7};
DE AltName: Full=Transmembrane protein 189;
GN Name=PEDS1 {ECO:0000250|UniProtKB:A5PLL7};
GN Synonyms=PDES {ECO:0000250|UniProtKB:A5PLL7},
GN TMEM189 {ECO:0000250|UniProtKB:A5PLL7};
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;
RN [1] {ECO:0000312|EMBL:AAI48013.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford {ECO:0000312|EMBL:AAI48013.1};
RC TISSUE=Basal ganglia {ECO:0000312|EMBL:AAI48013.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plasmanylethanolamine desaturase involved in plasmalogen
CC biogenesis in the endoplasmic reticulum membrane. Plasmalogens are
CC glycerophospholipids with a hydrocarbon chain linked by a vinyl ether
CC bond at the glycerol sn-1 position, and are involved in antioxidative
CC and signaling mechanisms. {ECO:0000250|UniProtKB:A5PLL7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(1,2-saturated alkyl)-2-acyl-sn-glycero-3-
CC phosphoethanolamine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = 1-O-
CC (1Z-alkenyl)-2-acyl-sn-glycero-3-phosphoethanolamine + 2 Fe(III)-
CC [cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:22956, Rhea:RHEA-COMP:10438,
CC Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:75028, ChEBI:CHEBI:77290; EC=1.14.19.77;
CC Evidence={ECO:0000250|UniProtKB:A5PLL7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22957;
CC Evidence={ECO:0000250|UniProtKB:A5PLL7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-O-hexadecyl-2-acyl-sn-glycero-3-phosphoethanolamine + 2
CC Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a 1-O-(1Z-hexadecenyl)-2-acyl-
CC sn-glycero-3-phosphoethanolamine + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:61960, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:145181,
CC ChEBI:CHEBI:145186; Evidence={ECO:0000250|UniProtKB:A5PLL7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61961;
CC Evidence={ECO:0000250|UniProtKB:A5PLL7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-O-octadecyl-2-acyl-sn-glycero-3-phosphoethanolamine + 2
CC Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a 1-O-(1Z-octadecenyl)-2-acyl-
CC sn-glycero-3-phosphoethanolamine + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:61964, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:145182,
CC ChEBI:CHEBI:145187; Evidence={ECO:0000250|UniProtKB:A5PLL7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61965;
CC Evidence={ECO:0000250|UniProtKB:A5PLL7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-O-(9Z-octadecenyl)-2-acyl-sn-glycero-3-phosphoethanolamine
CC + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a 1-O-(1Z,9Z-
CC octadecadienyl)-2-acyl-sn-glycero-3-phosphoethanolamine + 2 Fe(III)-
CC [cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:61968, Rhea:RHEA-COMP:10438,
CC Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:145183, ChEBI:CHEBI:145188;
CC Evidence={ECO:0000250|UniProtKB:A5PLL7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61969;
CC Evidence={ECO:0000250|UniProtKB:A5PLL7};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000250|UniProtKB:A5PLL7}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:A5PLL7}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: Histidine box-1 and -2 together with other histidine residues
CC are essential for catalytic activity. {ECO:0000250|UniProtKB:A5PLL7}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase CarF family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC148012; AAI48013.1; -; mRNA.
DR RefSeq; NP_001093785.1; NM_001100315.1.
DR AlphaFoldDB; A6QLM0; -.
DR STRING; 9913.ENSBTAP00000013376; -.
DR PaxDb; A6QLM0; -.
DR Ensembl; ENSBTAT00000013376; ENSBTAP00000013376; ENSBTAG00000010135.
DR GeneID; 507694; -.
DR KEGG; bta:507694; -.
DR CTD; 387521; -.
DR VEuPathDB; HostDB:ENSBTAG00000010135; -.
DR VGNC; VGNC:57030; PEDS1.
DR eggNOG; KOG3011; Eukaryota.
DR GeneTree; ENSGT00940000162354; -.
DR HOGENOM; CLU_065233_1_1_1; -.
DR InParanoid; A6QLM0; -.
DR OMA; CITNGWL; -.
DR OrthoDB; 1421561at2759; -.
DR UniPathway; UPA00199; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000010135; Expressed in floor plate of diencephalon and 104 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0050207; F:plasmanylethanolamine desaturase activity; ISS:UniProtKB.
DR GO; GO:0008611; P:ether lipid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR019547; Lipid_desat.
DR Pfam; PF10520; Lipid_desat; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Fatty acid metabolism; Lipid metabolism; Membrane;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..271
FT /note="Plasmanylethanolamine desaturase"
FT /id="PRO_0000319992"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 187..191
FT /note="Histidine box-1"
FT /evidence="ECO:0000250|UniProtKB:A5PLL7"
FT MOTIF 214..218
FT /note="Histidine box-2"
FT /evidence="ECO:0000250|UniProtKB:A5PLL7"
FT SITE 96
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:A5PLL7"
FT SITE 121
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:A5PLL7"
FT SITE 122
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:A5PLL7"
FT SITE 187
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q99LQ7"
FT SITE 191
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q99LQ7"
FT SITE 215
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q99LQ7"
FT SITE 218
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q99LQ7"
FT SITE 219
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q99LQ7"
SQ SEQUENCE 271 AA; 31285 MW; 46A1FBEB92D619B6 CRC64;
MAGAEDGPGQ QPELEDDEAA SCRRWGAQHA GARELAALYS PGKRFQEWCC VVLCFSLIAH
NMAHLLLLAR WEHTPLVMLG MVAGALLADF LSGLVHWGAD TWGSVELPIV GKAFIRPFRE
HHIDPTAITR HDFIETNGDN CLLTLLPLLN MAYKFRTQSP EVLEQLYPWE CFVFCLIIFG
TFTNQIHKWS HTYFGLPCWV VFLQDWHVIL PRKHHRIHHV SPHETYFCIT TGWLNYPLER
MGFWRRLEDI IQALTGEKPR ADDMKWAQKI K
