CHO2_NEUCR
ID CHO2_NEUCR Reviewed; 965 AA.
AC Q7SAJ6;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Phosphatidylethanolamine N-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03217, ECO:0000303|PubMed:6016609};
DE Short=PE methyltransferase {ECO:0000255|HAMAP-Rule:MF_03217};
DE Short=PEAMT {ECO:0000255|HAMAP-Rule:MF_03217};
DE Short=PEMT {ECO:0000255|HAMAP-Rule:MF_03217};
DE EC=2.1.1.17 {ECO:0000255|HAMAP-Rule:MF_03217, ECO:0000269|PubMed:6016609};
DE AltName: Full=Cholineless {ECO:0000303|Ref.3};
GN Name=chol-1 {ECO:0000303|Ref.4}; Synonyms=cho2;
GN ORFNames=B2E7.130, NCU08045;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [3]
RP PATHWAY.
RA Horowitz N.H., Beadle G.W.;
RT "A microbiological method for the determination of choline by use of a
RT mutant of Neurospora.";
RL J. Biol. Chem. 150:325-333(1943).
RN [4]
RP PATHWAY.
RA Horowitz N.H., Bonner D., Houlahan M.B.;
RT "The utilization of choline analogues by cholineless mutants of
RT Neurospora.";
RL J. Biol. Chem. 159:145-151(1945).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=6016609; DOI=10.1016/s0021-9258(19)81455-2;
RA Scarborough G.A., Nyc J.F.;
RT "Methylation of ethanolamine phosphatides by microsomes from normal and
RT mutant strains of Neurospora crassa.";
RL J. Biol. Chem. 242:238-242(1967).
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:0000255|HAMAP-Rule:MF_03217, ECO:0000269|PubMed:6016609}.
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:0000255|HAMAP-Rule:MF_03217,
CC ECO:0000269|PubMed:6016609};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03217, ECO:0000305|Ref.3,
CC ECO:0000305|Ref.4}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03217, ECO:0000269|PubMed:6016609}; Multi-
CC pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03217}.
CC -!- SIMILARITY: Belongs to the class VI-like SAM-binding methyltransferase
CC superfamily. CHO2 family. {ECO:0000255|HAMAP-Rule:MF_03217}.
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DR EMBL; BX897675; CAE85544.1; -; Genomic_DNA.
DR EMBL; CM002239; EAA33479.1; -; Genomic_DNA.
DR RefSeq; XP_962715.1; XM_957622.2.
DR AlphaFoldDB; Q7SAJ6; -.
DR SMR; Q7SAJ6; -.
DR STRING; 5141.EFNCRP00000008237; -.
DR PRIDE; Q7SAJ6; -.
DR EnsemblFungi; EAA33479; EAA33479; NCU08045.
DR GeneID; 3878822; -.
DR KEGG; ncr:NCU08045; -.
DR VEuPathDB; FungiDB:NCU08045; -.
DR HOGENOM; CLU_005987_0_0_1; -.
DR InParanoid; Q7SAJ6; -.
DR OMA; DWVGLYM; -.
DR UniPathway; UPA00753; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004608; F:phosphatidylethanolamine N-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IBA:GO_Central.
DR HAMAP; MF_03217; PEMT; 1.
DR InterPro; IPR007318; Phopholipid_MeTrfase.
DR InterPro; IPR016219; Phosphatid-EA_MeTrfase_fun.
DR Pfam; PF04191; PEMT; 2.
DR PIRSF; PIRSF000383; PEAMT; 1.
DR PROSITE; PS51598; SAM_CHO2; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Methyltransferase; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..965
FT /note="Phosphatidylethanolamine N-methyltransferase"
FT /id="PRO_0000405900"
FT TOPO_DOM 1..91
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 113..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 137..201
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 223..229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 251..279
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 301..306
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 328..389
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 411..417
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 439..467
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 468..488
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 489..496
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 497..517
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 518..573
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 574..594
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 595..965
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 965 AA; 109552 MW; EAA3EF9E29E795FE CRC64;
MSSSAADPFA ARLNSDVRQR HPTASATSKN VEGTSQQKQQ QQQQQSEANA AASRVKKTYG
KTPDGTVFVV PTTHDMVTQL LDPREPKNLS DVAVLAIIAL HFLAAYYLPW GVKRPLFAAI
FMFWRLAYNV GIGYLLTIQS KYKLLVTWAK RWKLFENPAT GKNPRPWLYN LLKKELETKI
PQDYKFEEAP IEYNTWLTFR RVVDLILMCD FISYCLFAIV CAHKPDGEGL FMCFARWAAG
ITLVGFNLWV KLDAHRVVKD YAWYWGDFFY LIEQELTFDG VFELAPHPMY SIGYAGYYGI
SMMAASYDVL FISIIAHAAQ FAFLVIVENP HIEKTYNPPQ PRVRCESEAG SQLQEFASEY
SVPSTTGRHD NTPLPVHNLI GLKNLDFFRI TDVAIVLLCA YLAVVTMVTP NTRFYQALFV
LHALAWRLWY SAGLGVILTM QSEEKMFTRH FLKYGESVGE AWRQWKGIYH LSNCLCHASF
IAASYKMYEF PADWTYGWAL LKHVVGLSLI ALQVWTATSI YESLGEFGWF YGDFFFDSKR
QLTYTSIYRF LNNPERVFGT AGLWGAALIT WSRAIFLMAL AGHFLTLAFL AYVEKPHMQK
VYGRNLRDDA GVTKFIKRSL PPPVTEWQQS IDKVLDETKH FIDEFVDAAR SRLATGSSTI
VKDTSALFNK YPARLTLSKI SPDLAGYDPK HYGLSLAGTR VVGTNEKATG KESPNARVLK
DVKTQAFEYG APIRVKWTAP ANHSKKDWVG LYMVTDNRSR EVTEVPSLGR WVPTNPGEYD
TTTDQGILVW DQPVEKKSED TDLVEGEMVF EGDKLWWTQG VFEFRYHHGG GHHVMSISEP
FEIQIPKFDD EHMGVDISGE VGERAVEAAL LPVIRNCLDR DPDIAPSNAE ERFGGHVERD
GKYARRVVYA IRHMFGIDFA PAVVLADGNV RRLAWRICHA KEVLAPFSMS HTNGRTTPVD
SKFSE
