CHO21_VANPO
ID CHO21_VANPO Reviewed; 838 AA.
AC A7TNI7;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Phosphatidylethanolamine N-methyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_03217};
DE Short=PE methyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_03217};
DE Short=PEAMT 1 {ECO:0000255|HAMAP-Rule:MF_03217};
DE Short=PEMT 1 {ECO:0000255|HAMAP-Rule:MF_03217};
DE EC=2.1.1.17 {ECO:0000255|HAMAP-Rule:MF_03217};
GN Name=CHO2-1; ORFNames=Kpol_1026p17;
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC Y-8283 / UCD 57-17;
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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}.
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 -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03217}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03217}; Multi-pass membrane protein
CC {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; DS480431; EDO16170.1; -; Genomic_DNA.
DR RefSeq; XP_001644028.1; XM_001643978.1.
DR AlphaFoldDB; A7TNI7; -.
DR STRING; 436907.A7TNI7; -.
DR EnsemblFungi; EDO16170; EDO16170; Kpol_1026p17.
DR GeneID; 5544308; -.
DR KEGG; vpo:Kpol_1026p17; -.
DR eggNOG; ENOG502QRGH; Eukaryota.
DR HOGENOM; CLU_005987_0_1_1; -.
DR InParanoid; A7TNI7; -.
DR OMA; LAWEQTE; -.
DR OrthoDB; 170424at2759; -.
DR PhylomeDB; A7TNI7; -.
DR UniPathway; UPA00753; -.
DR Proteomes; UP000000267; Unassembled WGS sequence.
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; 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 Pfam; PF04191; PEMT; 2.
DR PIRSF; PIRSF000383; PEAMT; 1.
DR PROSITE; PS51598; SAM_CHO2; 1.
PE 3: Inferred from homology;
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..838
FT /note="Phosphatidylethanolamine N-methyltransferase 1"
FT /id="PRO_0000405922"
FT TOPO_DOM 1..48
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 70..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 95..157
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 179..184
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 206..236
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 258..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 283..328
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 350..356
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 378..403
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 404..424
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 425..435
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 457..517
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 518..538
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 539..838
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
SQ SEQUENCE 838 AA; 97170 MW; 77E3412434F01038 CRC64;
MATEIITEKK EIVARTRSSG ITFNPPVTHD MVRSLFDPTI KKSFLECCIT LTILANFVLC
YYLINWFGLS QAKLIFLIQY VYWRLAYNLG IGIILHYQSH YESLTKYANQ NKLFKKESAK
TNWIASFFQF EIKSKMPNDY NLHSYPDELN CWLLFRQFVD LILMQDFTTY IIYVYLSLPT
DVSSLINWKS LIGIAMILFN IWVKIDAHRV VKDYAWYWGD FFFLQDAELT FDGVFNISPH
PMYSIGYLGY YGLSLICGDY RVLLVSVGGH FLQFLFLKYV ESPHIERTYG SDSPSNSTQH
QIDDLIAKEN YDYSRPLINT GILFENFQFL RFSDYFTVST ILVLFSWFFT SKPSNNFLFV
LTLLTKLTTW LLTSWILFQQ SNRKWFTRLF LKNGYTQIYS YQQWQFLYNY SLIVTNTLLF
LHTLSELYSI QSSDGLNNSH VIFGLLLCAI QIWCNVETRD AISDFGWFYG DFFLTNYITT
RKLTSQGIYR YLNNPEAILG VAGIWGSVLM TNFSKTNVTL AVLWTVTNLI FVKLIEEPHV
SKVYGNGTRV SGVQQTLLAL KPFRWISDLI DDWGNKMMKS LHGFDSDSDS ESISSGKKGN
LSSLKLSKKS KLKNRVQSDN KLAPNSKFEI EDLEDEIVYL PNSVTISWKL PISMFNEKDW
IGLYNVLETG SDRTQTKIPS LGHWSAVDAT GYPHDSINTN SITEFKKGSK NVSGRVTFDA
NLLYFKPGIY EFRYHSKNSH KVLLISSPFQ ISFPEFDNEA QVDIKNEIMK FLDAISCMKN
EKYFANDNKY FTADAFSNYI KDSFGIELST DYIRRVNGDV EVISRRVHDI KEVLDSLN
