ID A8NIB6_COPC7 Unreviewed; 1047 AA.
AC A8NIB6;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 2.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Phosphatidylethanolamine N-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03217, ECO:0000256|RuleBase:RU361122};
DE Short=PE methyltransferase {ECO:0000256|HAMAP-Rule:MF_03217};
DE Short=PEAMT {ECO:0000256|HAMAP-Rule:MF_03217, ECO:0000256|RuleBase:RU361122};
DE Short=PEMT {ECO:0000256|HAMAP-Rule:MF_03217};
DE EC=2.1.1.17 {ECO:0000256|HAMAP-Rule:MF_03217, ECO:0000256|RuleBase:RU361122};
GN ORFNames=CC1G_01636 {ECO:0000313|EMBL:EAU87989.2};
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176 {ECO:0000313|EMBL:EAU87989.2, ECO:0000313|Proteomes:UP000001861};
RN [1] {ECO:0000313|EMBL:EAU87989.2, ECO:0000313|Proteomes:UP000001861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC {ECO:0000313|Proteomes:UP000001861};
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
CC -!- FUNCTION: Catalyzes the first step of the methylation pathway of
CC phosphatidylcholine biosynthesis, the SAM-dependent methylation of
CC phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine
CC (PMME). {ECO:0000256|HAMAP-Rule:MF_03217,
CC ECO:0000256|RuleBase:RU361122}.
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:0000256|HAMAP-Rule:MF_03217,
CC ECO:0000256|RuleBase:RU361122};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_03217, ECO:0000256|RuleBase:RU361122}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|HAMAP-Rule:MF_03217, ECO:0000256|RuleBase:RU361122};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_03217,
CC ECO:0000256|RuleBase:RU361122}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the class VI-like SAM-binding methyltransferase
CC superfamily. CHO2 family. {ECO:0000256|HAMAP-Rule:MF_03217,
CC ECO:0000256|RuleBase:RU361122}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03217,
CC ECO:0000256|RuleBase:RU361122}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAU87989.2}.
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DR EMBL; AACS02000010; EAU87989.2; -; Genomic_DNA.
DR RefSeq; XP_001833959.2; XM_001833907.2.
DR AlphaFoldDB; A8NIB6; -.
DR STRING; 240176.A8NIB6; -.
DR GeneID; 6010463; -.
DR KEGG; cci:CC1G_01636; -.
DR VEuPathDB; FungiDB:CC1G_01636; -.
DR eggNOG; ENOG502QRGH; Eukaryota.
DR HOGENOM; CLU_005987_0_1_1; -.
DR InParanoid; A8NIB6; -.
DR OMA; RIWYSVG; -.
DR OrthoDB; 1561at2759; -.
DR UniPathway; UPA00753; -.
DR Proteomes; UP000001861; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004608; F:phosphatidylethanolamine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_03217; PEMT; 1.
DR InterPro; IPR007318; Phopholipid_MeTrfase.
DR InterPro; IPR016219; Phosphatid-EA_MeTrfase_fun.
DR PANTHER; PTHR32138; PHOSPHATIDYLETHANOLAMINE N-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR32138:SF0; PHOSPHATIDYLETHANOLAMINE N-METHYLTRANSFERASE; 1.
DR Pfam; PF04191; PEMT; 2.
DR PIRSF; PIRSF000383; PEAMT; 2.
DR PROSITE; PS51598; SAM_CHO2; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824, ECO:0000256|HAMAP-
KW Rule:MF_03217};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_03217};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_03217};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_03217};
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_03217,
KW ECO:0000256|RuleBase:RU361122};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209,
KW ECO:0000256|HAMAP-Rule:MF_03217};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264, ECO:0000256|HAMAP-
KW Rule:MF_03217}; Reference proteome {ECO:0000313|Proteomes:UP000001861};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03217,
KW ECO:0000256|RuleBase:RU361122};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03217,
KW ECO:0000256|RuleBase:RU361122};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_03217};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_03217}.
FT TRANSMEM 83..100
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03217,
FT ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 106..128
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03217,
FT ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03217,
FT ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 477..495
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03217,
FT ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 501..523
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03217,
FT ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 655..675
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03217,
FT ECO:0000256|RuleBase:RU361122"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 959..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..976
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1047 AA; 117841 MW; 183A5DED1E3C8731 CRC64;
MSKSQNGLRQ RKGNTTPKGA QRSRSPATDS DKTVNGEHVS NGTRAEEVVW GKTPSGEVFR
VPTTHDVLTT LFDPRYPKSH LDMLNLGLLG LQLVLFFWLP RNLGRIFFFF YFAFWRAAYD
AGLGWVLTKQ SKRKWIVKEV QRRGWLDEKR RPLVRDWIRK QLQDKMGKDY SFDELPLEYN
TWLLFRQLVD VILVNDFLSY CMFAFSCFRT PEGLSFIVHV MRWLGGIALI GFNLWVKTEA
HNVVKDYGWY WGDVFFQRGN LVFDGVFELA PHPMYSVGYA GYYGLSLISG SYAVLFVSLA
AHAAQFAFLV FFENPHIERM YGKPKAIAKR TPITTPARSG LNAVASSSTT TGSSTPVVED
ESTPAITEGD TATTETELET EIEDTVVSNG AAFPNVTKPS STLGSKHLKQ RQLSISSTGS
SIGELDEELH RPQAFKAPPQ PQRKKQKILS QHDLLNKYFR RDAVVLRNVD LFRATDAMLV
LIIFYAAVIT FIPSVGPRVM LALHFIHALT WLGIHYVGLG LLLRAQSQSK FLVRHFLKNY
HYPEKDAVQG PIIEAFSNWK AIYNLSLCMK YVSCLGVVWK TYSLPSDWAV GNELLCHTLG
TLLVGLHIWA TMESFEVLGV FGWFFGDFFM EEFPAHLEYT GIYRYLNNPE AMGGAAWFGL
SLISGSKLVL ALAVVRHLVN WWFLTTVENP HMRKLYGDSL RKDAGFVKVI KNVANKNAKI
LESRAGKHVP ELKRVVKEVK GTIDKVFEET AEAVEDFLAK SGPKFSEVVQ DTKVLLQQSR
EKLVITRVAN DISSYDATKY NVSIVPSSTT GTLAFHLGEP ITVKWEAPHN HSRKDWIGLY
RVGANKDTLV TKTSAMGMWL PVHDEEWDGD VPLGLERAPC SNRESQTGTI TFKGNTLPWL
VGRYEIRYHH DGKYNVMSLD GPLEIYVDKP SDTTFSSVRE TLMRVVPLCL DSDPSLMPAS
CKRTSAPSSS SVPSTPAAEG DHDPEVEDRD PDDFTFWSER QAKRISAAIK QIFGVDYAPE
VIVADANLTI LANRILASTE LLGRPET
//
