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CHO2_YEAS6
ID   CHO2_YEAS6              Reviewed;         869 AA.
AC   B5VJA0;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Phosphatidylethanolamine N-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03217};
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};
GN   Name=CHO2; ORFNames=AWRI1631_73790;
OS   Saccharomyces cerevisiae (strain AWRI1631) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=545124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AWRI1631;
RX   PubMed=18778279; DOI=10.1111/j.1567-1364.2008.00434.x;
RA   Borneman A.R., Forgan A.H., Pretorius I.S., Chambers P.J.;
RT   "Comparative genome analysis of a Saccharomyces cerevisiae wine strain.";
RL   FEMS Yeast Res. 8:1185-1195(2008).
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; ABSV01000974; EDZ72001.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5VJA0; -.
DR   UniPathway; UPA00753; -.
DR   Proteomes; UP000008988; 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   Acetylation; Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism;
KW   Membrane; Methyltransferase; Phospholipid biosynthesis;
KW   Phospholipid metabolism; S-adenosyl-L-methionine; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P05374"
FT   CHAIN           2..869
FT                   /note="Phosphatidylethanolamine N-methyltransferase"
FT                   /id="PRO_0000405912"
FT   TOPO_DOM        2..55
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        77..86
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        108..187
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        188..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        209..212
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        213..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        234..258
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        259..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        280..291
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        292..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        311..362
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        363..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        384..389
FT                   /note="Cytoplasmic"
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..439
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        440..460
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        461..463
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        464..484
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        485..534
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        535..555
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        556..869
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P05374"
SQ   SEQUENCE   869 AA;  101252 MW;  A6598AB6B817C112 CRC64;
     MSSCKTTLSE MVGSVTKDRG TINVKARTRS SNVTFKPPVT HDMVRSLFDP TLKKSLLEKC
     IALAIISNFF ICYWVFQRFG LQFTKYFFLV QYLFWRIAYN LGIGLVLHYQ SHYETLTNCA
     KTHAIFSKIP HNKDANSNFS TNSNSFSEKF WNFIRKFCQY EIRSKMPKEY DLFAYPEEIN
     VWLIFRQFVD LILMQDFVTY IIYVYLSIPY SWVQIFNWRS LLGVILILFN IWVKLDAHRV
     VKDYAWYWGD FFFLEESELI FDGVFNISPH PMYSIGYLGY YGLSLICNDY KVLLVSVFGH
     YSQFLFLKYV ENPHIERTYG DGTDSDSQMN SRIDDLISKE NYDYSRPLIN MGLSFNNFNK
     LRFTDYFTIG TVAALMLGTI MNARFINLNY LFITVFVTKL VSWLFISTIL YKQSQSKWFT
     RLFLENGYTQ VYSYEQWQFI YNYYLVLTYT LMIIYTGLQI WSNFSNINNS QLIFGLILVA
     LQTWCDKETR LAISDFGWFY GDFFLSNYIS TRKLTSQGIY RYLNHPEAVL GVVGVWGTVL
     MTNFAVTNII LAVLWTLTNF ILVKFIETPH VNKIYGKTKR VSGVGKTLLG LKPLRQVSDI
     VNRIENIIIK SLVDESKNSN GGAELLPKNY QDNKEWNILI QEAMDSVATR LSPYCELKIE
     NEQIETNFVL PTPVTLNWKM PIELYNGDDW IGLYKVIDTR ADREKTRVGS GGHWSATSKD
     SYMNHGLRHK ESVTEIKATE KYVQGKVTFD TSLLYFENGI YEFRYHSGNS HKVLLISTPF
     EISLPVLNTT TPELFEKDLT EFLTKVNVLK DGKFRPLGNK FFGMDSLKQL IKNSIGVELS
     SEYMRRVNGD AHVISHRAWD IKQTLDSLA
 
 
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