CHO22_VANPO
ID CHO22_VANPO Reviewed; 843 AA.
AC A7TLA7;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Phosphatidylethanolamine N-methyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_03217};
DE Short=PE methyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_03217};
DE Short=PEAMT 2 {ECO:0000255|HAMAP-Rule:MF_03217};
DE Short=PEMT 2 {ECO:0000255|HAMAP-Rule:MF_03217};
DE EC=2.1.1.17 {ECO:0000255|HAMAP-Rule:MF_03217};
GN Name=CHO2-2; ORFNames=Kpol_1041p40;
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; DS480413; EDO16982.1; -; Genomic_DNA.
DR RefSeq; XP_001644840.1; XM_001644790.1.
DR AlphaFoldDB; A7TLA7; -.
DR STRING; 436907.A7TLA7; -.
DR EnsemblFungi; EDO16982; EDO16982; Kpol_1041p40.
DR GeneID; 5545168; -.
DR KEGG; vpo:Kpol_1041p40; -.
DR eggNOG; ENOG502QRGH; Eukaryota.
DR HOGENOM; CLU_005987_0_1_1; -.
DR InParanoid; A7TLA7; -.
DR OMA; DWVGLYM; -.
DR OrthoDB; 170424at2759; -.
DR PhylomeDB; A7TLA7; -.
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..843
FT /note="Phosphatidylethanolamine N-methyltransferase 2"
FT /id="PRO_0000405923"
FT TOPO_DOM 1..58
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 80..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 111..171
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 193..201
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 202..219
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 220..254
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 255..271
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 272..277
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 278..294
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 295..343
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 365..372
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 394..418
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 440..444
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 445..465
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 466..516
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 517..537
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 538..843
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
SQ SEQUENCE 843 AA; 97906 MW; DF5D35A64385ED82 CRC64;
MSVNYSETIC SFQDTAINNI GTGKKYQTMA HTRSSNIRFV PAVTHDMVRS LFDPTIKKSF
LECCITLSIF ANFGLCYLFN LKFGQSLTKV FYLFQYILWR LSYNLGIGIL LHYQSKNESL
TSFAKLNKLF DKKSTSKLAK FCQFEISTKM ANDYNMHNYP EEFNIWLLFR QFVDLILMQD
FTTYILFVYC SLPSEGIDFK NWRILVGTSM ILFNIWVKVD AHRVVKDYAW YWGDFFFLQD
SELTFDGVFN ISPHPMYSIG YLGYYGISLI CGDYKVLLIS IWGHILQFLF LKYVENPHIE
EIYGSESDTN QLSNSYIDDL IVKENYDYSR PLISTGLRWK HYDLLRFSDH FTILSILAVV
LIAIKTKPTE KALFIITITA KIFSASFTSY ILFKQSKDKW FTKIFLKNGY TQIYCYQQWQ
FIYNYSFVLP TTLLILQTTS KIYNLYPNIE YTQIIFGGIL CAIQMWCNSE IRAAISDFGW
FYGDFFLINY ISERRLTSQG IYRYLNNPEA ILGTAGIWGT ALMTNFCYEN IILAIIWTST
NFIFVKFIEK PHVSKIYGNE TRISGVGKTL QGLKPLRMIY DIFDDIGSLF LRNLIASNKH
ALNHSAASPL HLEFSIQEAL ENANAKLAPN CKFNLEPKPN DEYVLPESIK ISWQLPIELY
NNRDWIGLYN VLDTRTNRYR TKVSSSGHWC GTSREGYKSD KQNTMAIKEF HKNSKVVKGV
VVFDYNLLIF EPGIYEVRYH SNGGHNVIMS SQPFQIKFPK FEITDQEILH SNLVNFLTKV
NSINDGKFVE NGSKYFNTRT FSCLLKKSTG IDISIEFIKK VSGDLKIISH RLCEIKKILD
SLD
