PEMT_RAT
ID PEMT_RAT Reviewed; 199 AA.
AC Q08388; Q5BK89;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Phosphatidylethanolamine N-methyltransferase {ECO:0000303|PubMed:3182818, ECO:0000303|PubMed:3680298, ECO:0000303|PubMed:8344945};
DE Short=PE N-methyltransferase {ECO:0000303|PubMed:3182818, ECO:0000303|PubMed:3680298, ECO:0000303|PubMed:8344945};
DE Short=PEAMT {ECO:0000255|HAMAP-Rule:MF_03216};
DE Short=PEMT {ECO:0000255|HAMAP-Rule:MF_03216};
DE EC=2.1.1.17 {ECO:0000305|PubMed:3182818, ECO:0000305|PubMed:3680298, ECO:0000305|PubMed:8344945};
DE EC=2.1.1.71 {ECO:0000305|PubMed:3182818, ECO:0000305|PubMed:3680298, ECO:0000305|PubMed:8344945};
DE AltName: Full=Phospholipid methyltransferase {ECO:0000255|HAMAP-Rule:MF_03216};
DE Short=PLMT {ECO:0000255|HAMAP-Rule:MF_03216};
GN Name=Pemt {ECO:0000255|HAMAP-Rule:MF_03216}; Synonyms=Pempt;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=8344945; DOI=10.1016/s0021-9258(19)85468-6;
RA Cui Z., Vance J.E., Chen M.H., Voelker D.R., Vance D.E.;
RT "Cloning and expression of a novel phosphatidylethanolamine N-
RT methyltransferase. A specific biochemical and cytological marker for a
RT unique membrane fraction in rat liver.";
RL J. Biol. Chem. 268:16655-16663(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 [3]
RP PROTEIN SEQUENCE OF 2-31.
RA Ridgway N.D.;
RL Thesis (1988), University of British Columbia, Canada.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=3680298; DOI=10.1016/s0021-9258(18)45514-7;
RA Ridgway N.D., Vance D.E.;
RT "Purification of phosphatidylethanolamine N-methyltransferase from rat
RT liver.";
RL J. Biol. Chem. 262:17231-17239(1987).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=3182818; DOI=10.1016/s0021-9258(18)37470-2;
RA Ridgway N.D., Vance D.E.;
RT "Specificity of rat hepatic phosphatidylethanolamine N-methyltransferase
RT for molecular species of diacyl phosphatidylethanolamine.";
RL J. Biol. Chem. 263:16856-16863(1988).
CC -!- FUNCTION: Catalyzes the three sequential steps of the methylation
CC pathway for the biosynthesis of phosphatidylcholine, a critical and
CC essential component for membrane structure (Probable) (PubMed:8344945).
CC Uses S-adenosylmethionine (S-adenosyl-L-methionine, SAM or AdoMet) as
CC the methyl group donor for the methylation of phosphatidylethanolamine
CC (1,2-diacyl-sn-glycero-3-phosphoethanolamine, PE) to
CC phosphatidylmonomethylethanolamine (1,2-diacyl-sn-glycero-3-phospho-N-
CC methylethanolamine, PMME), PMME to phosphatidyldimethylethanolamine
CC (1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine, PDME), and
CC PDME to phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine,
CC PC), producing S-adenosyl-L-homocysteine in each step (Probable)
CC (PubMed:8344945). {ECO:0000269|PubMed:8344945,
CC ECO:0000305|PubMed:3182818, ECO:0000305|PubMed:3680298}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-
CC methionine = 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine +
CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11164,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:64573, ChEBI:CHEBI:64612; EC=2.1.1.17;
CC Evidence={ECO:0000305|PubMed:3182818, ECO:0000305|PubMed:3680298,
CC ECO:0000305|PubMed:8344945};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11165;
CC Evidence={ECO:0000305|PubMed:3182818, ECO:0000305|PubMed:3680298,
CC ECO:0000305|PubMed:8344945};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + S-
CC adenosyl-L-methionine = 1,2-diacyl-sn-glycero-3-phospho-N,N-
CC dimethylethanolamine + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:32735, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:64572, ChEBI:CHEBI:64573; EC=2.1.1.71;
CC Evidence={ECO:0000305|PubMed:3182818, ECO:0000305|PubMed:3680298,
CC ECO:0000305|PubMed:8344945};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32736;
CC Evidence={ECO:0000305|PubMed:3182818, ECO:0000305|PubMed:3680298,
CC ECO:0000305|PubMed:8344945};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine + S-
CC adenosyl-L-methionine = a 1,2-diacyl-sn-glycero-3-phosphocholine +
CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:32739,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57643, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:64572; EC=2.1.1.71;
CC Evidence={ECO:0000305|PubMed:3182818, ECO:0000305|PubMed:3680298,
CC ECO:0000305|PubMed:8344945};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32740;
CC Evidence={ECO:0000305|PubMed:3182818, ECO:0000305|PubMed:3680298,
CC ECO:0000305|PubMed:8344945};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + S-
CC adenosyl-L-methionine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phospho-N-methylethanolamine + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:70619, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:74986, ChEBI:CHEBI:85679;
CC Evidence={ECO:0000305|PubMed:3182818};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70620;
CC Evidence={ECO:0000305|PubMed:3182818};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho-N-
CC methylethanolamine + S-adenosyl-L-methionine = 1,2-di-(9Z-
CC octadecenoyl)-sn-glycero-3-phospho-N,N-dimethylethanolamine + H(+) +
CC S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:46112, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:85679,
CC ChEBI:CHEBI:85680; Evidence={ECO:0000305|PubMed:3182818};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46113;
CC Evidence={ECO:0000305|PubMed:3182818};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho-N,N-
CC dimethylethanolamine + S-adenosyl-L-methionine = 1,2-di-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphocholine + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:70623, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74669,
CC ChEBI:CHEBI:85680; Evidence={ECO:0000305|PubMed:3182818};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70624;
CC Evidence={ECO:0000305|PubMed:3182818};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphoethanolamine + S-adenosyl-L-methionine = 1,2-di-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phospho-N-methylethanolamine + H(+) +
CC S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:70739, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:172403,
CC ChEBI:CHEBI:189848; Evidence={ECO:0000305|PubMed:3182818};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70740;
CC Evidence={ECO:0000305|PubMed:3182818};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho-N-
CC methylethanolamine + S-adenosyl-L-methionine = 1,2-di-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phospho-N,N-dimethylethanolamine + H(+)
CC + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:70743, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:189848,
CC ChEBI:CHEBI:189849; Evidence={ECO:0000305|PubMed:3182818};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70744;
CC Evidence={ECO:0000305|PubMed:3182818};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho-N,N-
CC dimethylethanolamine + S-adenosyl-L-methionine = 1,2-di-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phosphocholine + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:70747, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:42027, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:189849; Evidence={ECO:0000305|PubMed:3182818};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70748;
CC Evidence={ECO:0000305|PubMed:3182818};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z,12Z,15Z-octadecatrienoyl)-sn-glycero-3-
CC phosphoethanolamine + S-adenosyl-L-methionine = 1,2-di-(9Z,12Z,15Z-
CC octadecatrienoyl)-sn-glycero-3-phospho-N-methylethanolamine + H(+) +
CC S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:70751, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:189858,
CC ChEBI:CHEBI:189859; Evidence={ECO:0000305|PubMed:3182818};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70752;
CC Evidence={ECO:0000305|PubMed:3182818};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z,12Z,15Z-octadecatrienoyl)-sn-glycero-3-phospho-N-
CC methylethanolamine + S-adenosyl-L-methionine = 1,2-di-(9Z,12Z,15Z-
CC octadecatrienoyl)-sn-glycero-3-phospho-N,N-dimethylethanolamine +
CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:70755,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:189859, ChEBI:CHEBI:189860;
CC Evidence={ECO:0000305|PubMed:3182818};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70756;
CC Evidence={ECO:0000305|PubMed:3182818};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z,12Z,15Z-octadecatrienoyl)-sn-glycero-3-phospho-N,N-
CC dimethylethanolamine + S-adenosyl-L-methionine = 1,2-di-(9Z,12Z,15Z-
CC octadecatrienoyl)-sn-glycero-3-phosphocholine + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:70759, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:86161,
CC ChEBI:CHEBI:189860; Evidence={ECO:0000305|PubMed:3182818};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70760;
CC Evidence={ECO:0000305|PubMed:3182818};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycero-3-phosphoethanolamine + S-adenosyl-L-methionine = 1-
CC hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-
CC phospho-N-methylethanolamine + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:70763, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:78261, ChEBI:CHEBI:189861;
CC Evidence={ECO:0000305|PubMed:3182818};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70764;
CC Evidence={ECO:0000305|PubMed:3182818};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycero-3-phospho-N-methylethanolamine + S-adenosyl-L-methionine = 1-
CC hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-
CC phospho-N,N-dimethylethanolamine + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:70767, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:189861, ChEBI:CHEBI:189862;
CC Evidence={ECO:0000305|PubMed:3182818};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70768;
CC Evidence={ECO:0000305|PubMed:3182818};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycero-3-phospho-N,N-dimethylethanolamine + S-adenosyl-L-methionine
CC = 1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycero-3-phosphocholine + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:70771, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:74963, ChEBI:CHEBI:189862;
CC Evidence={ECO:0000305|PubMed:3182818};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70772;
CC Evidence={ECO:0000305|PubMed:3182818};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 10. {ECO:0000305|PubMed:3680298};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis.
CC {ECO:0000305|PubMed:3680298}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9UBM1}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03216}. Mitochondrion membrane
CC {ECO:0000255|HAMAP-Rule:MF_03216}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03216}. Note=Found in endoplasmic reticulum
CC where most PEMT activity is generated and in mitochondria (By
CC similarity). Located in a unique membrane in the hepatocyte, which is
CC not recognizable as any known subcellular structure (PubMed:8344945).
CC {ECO:0000250|UniProtKB:Q9UBM1, ECO:0000269|PubMed:8344945}.
CC -!- TISSUE SPECIFICITY: Expressed in liver (at protein level).
CC {ECO:0000269|PubMed:8344945}.
CC -!- SIMILARITY: Belongs to the class VI-like SAM-binding methyltransferase
CC superfamily. PEMT/PEM2 methyltransferase family. {ECO:0000255|HAMAP-
CC Rule:MF_03216}.
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DR EMBL; L14441; AAA03154.1; -; mRNA.
DR EMBL; BC091162; AAH91162.1; -; mRNA.
DR PIR; A47353; A47353.
DR RefSeq; NP_037135.1; NM_013003.1.
DR AlphaFoldDB; Q08388; -.
DR STRING; 10116.ENSRNOP00000004488; -.
DR PaxDb; Q08388; -.
DR GeneID; 25511; -.
DR KEGG; rno:25511; -.
DR CTD; 10400; -.
DR RGD; 3297; Pemt.
DR VEuPathDB; HostDB:ENSRNOG00000054423; -.
DR eggNOG; KOG4142; Eukaryota.
DR HOGENOM; CLU_086119_0_1_1; -.
DR InParanoid; Q08388; -.
DR OMA; VITSTWA; -.
DR OrthoDB; 1395721at2759; -.
DR PhylomeDB; Q08388; -.
DR BioCyc; MetaCyc:MON-16675; -.
DR BRENDA; 2.1.1.17; 5301.
DR Reactome; R-RNO-1483191; Synthesis of PC.
DR UniPathway; UPA00753; -.
DR PRO; PR:Q08388; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000054423; Expressed in liver and 19 other tissues.
DR Genevisible; Q08388; RN.
DR GO; GO:0031526; C:brush border membrane; IDA:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; IDA:RGD.
DR GO; GO:0080101; F:phosphatidyl-N-dimethylethanolamine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000773; F:phosphatidyl-N-methylethanolamine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008429; F:phosphatidylethanolamine binding; IDA:RGD.
DR GO; GO:0004608; F:phosphatidylethanolamine N-methyltransferase activity; IDA:RGD.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:RGD.
DR GO; GO:0001835; P:blastocyst hatching; ISO:RGD.
DR GO; GO:0006650; P:glycerophospholipid metabolic process; IMP:RGD.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IDA:RGD.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0050747; P:positive regulation of lipoprotein metabolic process; IMP:RGD.
DR GO; GO:0043200; P:response to amino acid; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0033273; P:response to vitamin; IDA:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:RGD.
DR GO; GO:0046498; P:S-adenosylhomocysteine metabolic process; IDA:RGD.
DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; IDA:RGD.
DR GO; GO:0006686; P:sphingomyelin biosynthetic process; ISO:RGD.
DR HAMAP; MF_03216; PLMT; 1.
DR InterPro; IPR024960; PEMT/MFAP.
DR InterPro; IPR007318; Phopholipid_MeTrfase.
DR PANTHER; PTHR15458; PTHR15458; 1.
DR Pfam; PF04191; PEMT; 1.
DR PIRSF; PIRSF005444; PEMT; 1.
DR PROSITE; PS51599; SAM_PEMT_PEM2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Endoplasmic reticulum; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Methyltransferase; Mitochondrion;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3"
FT CHAIN 2..199
FT /note="Phosphatidylethanolamine N-methyltransferase"
FT /id="PRO_0000193922"
FT TOPO_DOM 2..12
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT INTRAMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TOPO_DOM 34..45
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TOPO_DOM 67..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TOPO_DOM 115..157
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TOPO_DOM 179..199
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT BINDING 98..100
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT BINDING 180..181
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
SQ SEQUENCE 199 AA; 22486 MW; 8F1A938ED883B0FA CRC64;
MSWLLGYVDP TEPSFVAAVL TIVFNPLFWN VVARWEQRTR KLSRAFGSPY LACYSLGSII
LLLNILRSHC FTQAMMSQPK MEGLDSHTIY FLGLALLGWG LVFVLSSFYA LGFTGTFLGD
YFGILKESRV TTFPFSVLDN PMYWGSTANY LGWALMHASP TGLLLTVLVA LVYVVALLFE
EPFTAEIYRR KATRLHKRS
