PDES1_MOUSE
ID PDES1_MOUSE Reviewed; 271 AA.
AC Q99LQ7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Plasmanylethanolamine desaturase {ECO:0000250|UniProtKB:A5PLL7};
DE EC=1.14.19.77 {ECO:0000269|PubMed:32209662};
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:0000303|PubMed:32209662},
GN Tmem189 {ECO:0000312|MGI:MGI:2142624};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000312|EMBL:BAC40204.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE30306.1}, and
RC NOD {ECO:0000312|EMBL:BAC40204.1};
RC TISSUE=Bone marrow {ECO:0000312|EMBL:BAE30306.1}, and
RC Thymus {ECO:0000312|EMBL:BAC40204.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000312|EMBL:AAH02270.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor {ECO:0000312|EMBL:AAH02270.1};
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].
RC TISSUE=Brain, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-96; HIS-121; HIS-122;
RP HIS-131; HIS-187; HIS-191; HIS-215; HIS-218 AND HIS-219, DISRUPTION
RP PHENOTYPE, SUBCELLULAR LOCATION, AND PATHWAY.
RX PubMed=32209662; DOI=10.1073/pnas.1917461117;
RA Werner E.R., Keller M.A., Sailer S., Lackner K., Koch J., Hermann M.,
RA Coassin S., Golderer G., Werner-Felmayer G., Zoeller R.A., Hulo N.,
RA Berger J., Watschinger K.;
RT "The TMEM189 gene encodes plasmanylethanolamine desaturase which introduces
RT the characteristic vinyl ether double bond into plasmalogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 117:7792-7798(2020).
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:0000269|PubMed:32209662}.
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:0000269|PubMed:32209662};
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:0000269|PubMed:32209662}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:32209662}; 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:0000269|PubMed:32209662}.
CC -!- DISRUPTION PHENOTYPE: Body weight is reduced in homozygous deficient
CC male and female. Deficient mice lack plasmanylethanolamine desaturase
CC activity and have dramatically lowered plasmalogen levels in their
CC tissues. {ECO:0000269|PubMed:32209662}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase CarF family.
CC {ECO:0000305}.
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DR EMBL; AK088196; BAC40204.1; -; mRNA.
DR EMBL; AK151326; BAE30306.1; -; mRNA.
DR EMBL; AL589870; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR626861; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002270; AAH02270.1; -; mRNA.
DR CCDS; CCDS17104.1; -.
DR RefSeq; NP_663513.1; NM_145538.2.
DR AlphaFoldDB; Q99LQ7; -.
DR STRING; 10090.ENSMUSP00000006587; -.
DR PhosphoSitePlus; Q99LQ7; -.
DR EPD; Q99LQ7; -.
DR MaxQB; Q99LQ7; -.
DR PaxDb; Q99LQ7; -.
DR PeptideAtlas; Q99LQ7; -.
DR PRIDE; Q99LQ7; -.
DR ProteomicsDB; 259467; -.
DR Antibodypedia; 35022; 40 antibodies from 16 providers.
DR DNASU; 407243; -.
DR Ensembl; ENSMUST00000006587; ENSMUSP00000006587; ENSMUSG00000090213.
DR GeneID; 407243; -.
DR KEGG; mmu:407243; -.
DR UCSC; uc008oad.1; mouse.
DR CTD; 387521; -.
DR MGI; MGI:2142624; Tmem189.
DR VEuPathDB; HostDB:ENSMUSG00000090213; -.
DR eggNOG; KOG3011; Eukaryota.
DR GeneTree; ENSGT00940000162354; -.
DR HOGENOM; CLU_065233_1_1_1; -.
DR InParanoid; Q99LQ7; -.
DR OMA; CITNGWL; -.
DR OrthoDB; 1421561at2759; -.
DR PhylomeDB; Q99LQ7; -.
DR TreeFam; TF106147; -.
DR UniPathway; UPA00199; -.
DR BioGRID-ORCS; 407243; 8 hits in 71 CRISPR screens.
DR ChiTaRS; Tmem189; mouse.
DR PRO; PR:Q99LQ7; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q99LQ7; protein.
DR Bgee; ENSMUSG00000090213; Expressed in right kidney and 73 other tissues.
DR Genevisible; Q99LQ7; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA: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; IDA:UniProtKB.
DR GO; GO:0008611; P:ether lipid biosynthetic process; IDA: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 1: Evidence at protein 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_0000319994"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 COMPBIAS 9..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 96
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000269|PubMed:32209662"
FT SITE 121
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000269|PubMed:32209662"
FT SITE 122
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000269|PubMed:32209662"
FT SITE 187
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000269|PubMed:32209662"
FT SITE 191
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000269|PubMed:32209662"
FT SITE 215
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000269|PubMed:32209662"
FT SITE 218
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000269|PubMed:32209662"
FT SITE 219
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000269|PubMed:32209662"
FT MUTAGEN 96
FT /note="H->A: Loss of plasmanylethanolamine desaturase
FT activity. Does not affect endoplasmic reticulum membrane
FT localization."
FT /evidence="ECO:0000269|PubMed:32209662"
FT MUTAGEN 121
FT /note="H->A: Loss of plasmanylethanolamine desaturase
FT activity. Does not affect endoplasmic reticulum membrane
FT localization."
FT /evidence="ECO:0000269|PubMed:32209662"
FT MUTAGEN 122
FT /note="H->A: Loss of plasmanylethanolamine desaturase
FT activity. Does not affect endoplasmic reticulum membrane
FT localization."
FT /evidence="ECO:0000269|PubMed:32209662"
FT MUTAGEN 131
FT /note="H->A: Strongly reduces plasmanylethanolamine
FT desaturase activity. Does not affect endoplasmic reticulum
FT membrane localization."
FT /evidence="ECO:0000269|PubMed:32209662"
FT MUTAGEN 187
FT /note="H->A: Loss of plasmanylethanolamine desaturase
FT activity. Does not affect endoplasmic reticulum membrane
FT localization."
FT /evidence="ECO:0000269|PubMed:32209662"
FT MUTAGEN 191
FT /note="H->A: Loss of plasmanylethanolamine desaturase
FT activity. Does not affect endoplasmic reticulum membrane
FT localization."
FT /evidence="ECO:0000269|PubMed:32209662"
FT MUTAGEN 215
FT /note="H->A: Loss of plasmanylethanolamine desaturase
FT activity. Does not affect endoplasmic reticulum membrane
FT localization."
FT /evidence="ECO:0000269|PubMed:32209662"
FT MUTAGEN 218
FT /note="H->A: Loss of plasmanylethanolamine desaturase
FT activity. Does not affect endoplasmic reticulum membrane
FT localization."
FT /evidence="ECO:0000269|PubMed:32209662"
FT MUTAGEN 219
FT /note="H->A: Loss of plasmanylethanolamine desaturase
FT activity. Does not affect endoplasmic reticulum membrane
FT localization."
FT /evidence="ECO:0000269|PubMed:32209662"
SQ SEQUENCE 271 AA; 31134 MW; 4C37C838DBE5E15B CRC64;
MAGAEDAPGR QPELDEDETA EGRRWGAQHA GARELAALYS PGKRFQEWCS VILCFSLIAH
NLVHLLLLAR WEHTPLVILG VVAGALVADF LSGLVHWGAD TWGSVDLPIV GKAFIRPFRE
HHIDPTAITR HDFIETNGDN CLVTLLPLLN MAYKFRTQSP ETLEQLYPWE CFVFCLTIFG
TFTNQIHKWS HTYLGLPYWV TVLQDWHVIL PRKHHRIHHV APHETYFCIT TGWLNYPLEV
IGFWRRLEDL IQGLTGEKPR ADDMKWAQKI K
