PDES1_HUMAN
ID PDES1_HUMAN Reviewed; 270 AA.
AC A5PLL7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Plasmanylethanolamine desaturase {ECO:0000303|PubMed:31604315, ECO:0000303|PubMed:32209662};
DE EC=1.14.19.77 {ECO:0000269|PubMed:31604315, ECO:0000269|PubMed:32209662};
DE AltName: Full=Plasmanylethanolamine desaturase 1 {ECO:0000312|HGNC:HGNC:16735};
DE AltName: Full=Transmembrane protein 189;
GN Name=PEDS1 {ECO:0000312|HGNC:HGNC:16735};
GN Synonyms=KUA {ECO:0000303|PubMed:11076860},
GN PDES {ECO:0000303|PubMed:32209662}, TMEM189 {ECO:0000312|EMBL:AAI42967.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND
RP IDENTIFICATION OF PEDS1-UBE2V1 FUSION PROTEIN.
RC TISSUE=Colon cancer {ECO:0000269|PubMed:11076860};
RX PubMed=11076860; DOI=10.1101/gr.gr-1405r;
RA Thomson T.M., Lozano J.J., Loukili N., Carrio R., Serras F., Cormand B.,
RA Valeri M., Diaz V.M., Abril J., Burset M., Merino J., Macaya A.,
RA Corominas M., Guigo R.;
RT "Fusion of the human gene for the polyubiquitination coeffector UEV1 with
RT Kua, a newly identified gene.";
RL Genome Res. 10:1743-1756(2000).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pancreatic cancer {ECO:0000269|PubMed:11280764};
RX PubMed=11280764;
RA Ito M., Shichijo S., Tsuda N., Ochi M., Harashima N., Saito N., Itoh K.;
RT "Molecular basis of T cell-mediated recognition of pancreatic cancer
RT cells.";
RL Cancer Res. 61:2038-2046(2001).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Teratocarcinoma {ECO:0000269|PubMed:14702039};
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5] {ECO:0000312|EMBL:AAI42967.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DOMAIN, PATHWAY, AND
RP MUTAGENESIS OF HIS-95; HIS-120; HIS-121; HIS-130; HIS-186; HIS-190;
RP HIS-206; HIS-213; HIS-214; HIS-217; HIS-218 AND HIS-222.
RX PubMed=31604315; DOI=10.1126/science.aay1436;
RA Gallego-Garcia A., Monera-Girona A.J., Pajares-Martinez E.,
RA Bastida-Martinez E., Perez-Castano R., Iniesta A.A., Fontes M.,
RA Padmanabhan S., Elias-Arnanz M.;
RT "A bacterial light response reveals an orphan desaturase for human
RT plasmalogen synthesis.";
RL Science 366:128-132(2019).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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 (PubMed:31604315,
CC PubMed:32209662). Plasmalogens are glycerophospholipids with a
CC hydrocarbon chain linked by a vinyl ether bond at the glycerol sn-1
CC position, and are involved in antioxidative and signaling mechanisms
CC (PubMed:31604315). {ECO:0000269|PubMed:31604315,
CC ECO:0000269|PubMed:32209662, ECO:0000303|PubMed:31604315}.
CC -!- CATALYTIC ACTIVITY: [Plasmanylethanolamine desaturase]:
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:31604315, ECO:0000269|PubMed:32209662};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22957;
CC Evidence={ECO:0000269|PubMed:31604315};
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:0000269|PubMed:31604315};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61961;
CC Evidence={ECO:0000269|PubMed:31604315};
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:0000269|PubMed:31604315};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61965;
CC Evidence={ECO:0000269|PubMed:31604315};
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:0000269|PubMed:31604315};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61969;
CC Evidence={ECO:0000269|PubMed:31604315};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000269|PubMed:31604315}.
CC -!- INTERACTION:
CC A5PLL7; P13473-2: LAMP2; NbExp=3; IntAct=EBI-11337896, EBI-21591415;
CC A5PLL7; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-11337896, EBI-2623095;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11076860, ECO:0000269|PubMed:31604315}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A5PLL7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A5PLL7-2; Sequence=VSP_054091;
CC -!- DOMAIN: Histidine box-1 and -2 together with other histidine residues
CC are essential for catalytic activity. {ECO:0000269|PubMed:31604315}.
CC -!- MISCELLANEOUS: In human, PESD1 and UBE2V1 are adjacent genes which can
CC produce independent proteins and can also be fused to form a PESD1-
CC UBE2V1 hybrid protein. {ECO:0000269|PubMed:11076860}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase CarF family.
CC {ECO:0000305}.
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DR EMBL; AF155120; AAF08702.1; -; mRNA.
DR EMBL; AB044550; BAB18652.1; -; mRNA.
DR EMBL; AK023028; BAB14364.1; -; mRNA.
DR EMBL; AL034423; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC142966; AAI42967.1; -; mRNA.
DR CCDS; CCDS13428.1; -. [A5PLL7-1]
DR CCDS; CCDS54473.1; -. [A5PLL7-2]
DR RefSeq; NP_001155977.1; NM_001162505.1. [A5PLL7-2]
DR RefSeq; NP_954580.1; NM_199129.2. [A5PLL7-1]
DR RefSeq; NP_954673.1; NM_199203.2.
DR AlphaFoldDB; A5PLL7; -.
DR BioGRID; 132320; 30.
DR BioGRID; 132321; 34.
DR IntAct; A5PLL7; 4.
DR MINT; A5PLL7; -.
DR STRING; 9606.ENSP00000360715; -.
DR SwissLipids; SLP:000001973; -.
DR iPTMnet; A5PLL7; -.
DR PhosphoSitePlus; A5PLL7; -.
DR SwissPalm; A5PLL7; -.
DR BioMuta; TMEM189; -.
DR EPD; A5PLL7; -.
DR jPOST; A5PLL7; -.
DR MassIVE; A5PLL7; -.
DR MaxQB; A5PLL7; -.
DR PeptideAtlas; A5PLL7; -.
DR PRIDE; A5PLL7; -.
DR ProteomicsDB; 739; -. [A5PLL7-1]
DR Antibodypedia; 35022; 40 antibodies from 16 providers.
DR DNASU; 387522; -.
DR Ensembl; ENST00000371650.9; ENSP00000360713.5; ENSG00000240849.11. [A5PLL7-2]
DR Ensembl; ENST00000371652.9; ENSP00000360715.4; ENSG00000240849.11. [A5PLL7-1]
DR GeneID; 387521; -.
DR GeneID; 387522; -.
DR KEGG; hsa:387521; -.
DR KEGG; hsa:387522; -.
DR MANE-Select; ENST00000371652.9; ENSP00000360715.4; NM_199129.4; NP_954580.2.
DR UCSC; uc002xvg.3; human. [A5PLL7-1]
DR CTD; 387521; -.
DR CTD; 387522; -.
DR DisGeNET; 387521; -.
DR DisGeNET; 387522; -.
DR GeneCards; PEDS1; -.
DR HGNC; HGNC:16735; PEDS1.
DR HPA; ENSG00000240849; Low tissue specificity.
DR MIM; 610994; gene.
DR neXtProt; NX_A5PLL7; -.
DR OpenTargets; ENSG00000240849; -.
DR PharmGKB; PA162406226; -.
DR VEuPathDB; HostDB:ENSG00000240849; -.
DR eggNOG; KOG3011; Eukaryota.
DR GeneTree; ENSGT00940000162354; -.
DR HOGENOM; CLU_065233_1_1_1; -.
DR InParanoid; A5PLL7; -.
DR OMA; RTQECIC; -.
DR OrthoDB; 1462707at2759; -.
DR PhylomeDB; A5PLL7; -.
DR BioCyc; MetaCyc:G66-30744-MON; -.
DR BRENDA; 1.14.19.77; 2681.
DR PathwayCommons; A5PLL7; -.
DR SignaLink; A5PLL7; -.
DR UniPathway; UPA00199; -.
DR BioGRID-ORCS; 387521; 68 hits in 1067 CRISPR screens.
DR BioGRID-ORCS; 387522; 70 hits in 918 CRISPR screens.
DR GeneWiki; Kua-UEV; -.
DR Pharos; A5PLL7; Tdark.
DR PRO; PR:A5PLL7; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; A5PLL7; protein.
DR Bgee; ENSG00000240849; Expressed in lower esophagus mucosa and 160 other tissues.
DR ExpressionAtlas; A5PLL7; baseline and differential.
DR Genevisible; A5PLL7; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
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 Alternative splicing; Endoplasmic reticulum; Fatty acid metabolism;
KW Lipid metabolism; Membrane; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..270
FT /note="Plasmanylethanolamine desaturase"
FT /id="PRO_0000319993"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 186..190
FT /note="Histidine box-1"
FT /evidence="ECO:0000269|PubMed:31604315"
FT MOTIF 213..217
FT /note="Histidine box-2"
FT /evidence="ECO:0000269|PubMed:31604315"
FT SITE 95
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000269|PubMed:31604315"
FT SITE 120
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000269|PubMed:31604315"
FT SITE 121
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000269|PubMed:31604315"
FT SITE 186
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q99LQ7"
FT SITE 190
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q99LQ7"
FT SITE 214
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q99LQ7"
FT SITE 217
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 VAR_SEQ 109..111
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11076860"
FT /id="VSP_054091"
FT VARIANT 7
FT /note="W -> G (in dbSNP:rs2026757)"
FT /id="VAR_059732"
FT MUTAGEN 95
FT /note="H->A: Loss of plasmanylethanolamine desaturase
FT activity."
FT /evidence="ECO:0000269|PubMed:31604315"
FT MUTAGEN 120
FT /note="H->A: Loss of plasmanylethanolamine desaturase
FT activity."
FT /evidence="ECO:0000269|PubMed:31604315"
FT MUTAGEN 121
FT /note="H->A: Loss of plasmanylethanolamine desaturase
FT activity."
FT /evidence="ECO:0000269|PubMed:31604315"
FT MUTAGEN 130
FT /note="H->A: Loss of plasmanylethanolamine desaturase
FT activity."
FT /evidence="ECO:0000269|PubMed:31604315"
FT MUTAGEN 186
FT /note="H->A: Loss of plasmanylethanolamine desaturase
FT activity."
FT /evidence="ECO:0000269|PubMed:31604315"
FT MUTAGEN 190
FT /note="H->A: Loss of plasmanylethanolamine desaturase
FT activity."
FT /evidence="ECO:0000269|PubMed:31604315"
FT MUTAGEN 206
FT /note="H->A: No effect on plasmanylethanolamine desaturase
FT activity."
FT /evidence="ECO:0000269|PubMed:31604315"
FT MUTAGEN 213
FT /note="H->A: No effect on plasmanylethanolamine desaturase
FT activity."
FT /evidence="ECO:0000269|PubMed:31604315"
FT MUTAGEN 214
FT /note="H->A: Loss of plasmanylethanolamine desaturase
FT activity."
FT /evidence="ECO:0000269|PubMed:31604315"
FT MUTAGEN 217
FT /note="H->A: Loss of plasmanylethanolamine desaturase
FT activity."
FT /evidence="ECO:0000269|PubMed:31604315"
FT MUTAGEN 218
FT /note="H->A: Loss of plasmanylethanolamine desaturase
FT activity."
FT /evidence="ECO:0000269|PubMed:31604315"
FT MUTAGEN 222
FT /note="H->A: No effect on desaturase plasmanylethanolamine
FT activity."
FT /evidence="ECO:0000269|PubMed:31604315"
FT CONFLICT 6
FT /note="N -> D (in Ref. 1; AAF08702, 2; BAB18652, 4;
FT BAB14364 and 5; AAI42967)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="H -> N (in Ref. 5; AAI42967)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="P -> H (in Ref. 5; AAI42967)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 270 AA; 31135 MW; 960E639B6F1B55ED CRC64;
MAGAENWPGQ QLELDEDEAS CCRWGAQHAG ARELAALYSP GKRLQEWCSV ILCFSLIAHN
LVHLLLLARW EDTPLVILGV VAGALIADFL SGLVHWGADT WGSVELPIVG KAFIRPFREH
HIDPTAITRH DFIETNGDNC LVTLLPLLNM AYKFRTHSPE ALEQLYPWEC FVFCLIIFGT
FTNQIHKWSH TYFGLPRWVT LLQDWHVILP RKHHRIHHVS PHETYFCITT GWLNYPLEKI
GFWRRLEDLI QGLTGEKPRA DDMKWAQKIK
