AAPT2_ARATH
ID AAPT2_ARATH Reviewed; 389 AA.
AC O82568;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Choline/ethanolaminephosphotransferase 2;
DE EC=2.7.8.1;
DE EC=2.7.8.2;
DE AltName: Full=Aminoalcohol phosphotransferase 2;
DE Short=AtAAPT2;
GN Name=AAPT2; OrderedLocusNames=At3g25585; ORFNames=MWL2, T5M7;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RA Dewey R.E., Goode J.H.;
RT "Characterization of aminoalcoholphosphotransferases from Arabidopsis
RT thaliana and soybean.";
RL Plant Physiol. Biochem. 37:445-445(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
CC -!- FUNCTION: Catalyzes both phosphatidylcholine and
CC phosphatidylethanolamine biosynthesis from CDP-choline and CDP-
CC ethanolamine, respectively. Has a higher cholinephosphotransferase
CC activity than ethanolaminephosphotransferase activity.
CC {ECO:0000269|Ref.1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + CDP-ethanolamine = a 1,2-diacyl-sn-
CC glycero-3-phosphoethanolamine + CMP + H(+); Xref=Rhea:RHEA:32943,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:57876,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:64612; EC=2.7.8.1;
CC Evidence={ECO:0000269|Ref.1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + CDP-choline = a 1,2-diacyl-sn-
CC glycero-3-phosphocholine + CMP + H(+); Xref=Rhea:RHEA:32939,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:57643,
CC ChEBI:CHEBI:58779, ChEBI:CHEBI:60377; EC=2.7.8.2;
CC Evidence={ECO:0000269|Ref.1};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from ethanolamine: step 3/3.
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis;
CC phosphatidylcholine from phosphocholine: step 2/2.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O82568-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000305}.
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DR EMBL; AF091844; AAC61769.1; -; mRNA.
DR EMBL; AB025639; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001313; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002686; AEE77035.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77036.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77038.1; -; Genomic_DNA.
DR EMBL; AF360151; AAK25861.1; -; mRNA.
DR EMBL; AY054269; AAL06928.1; -; mRNA.
DR EMBL; AY142609; AAN13178.1; -; mRNA.
DR RefSeq; NP_001030767.1; NM_001035690.1. [O82568-1]
DR RefSeq; NP_189186.1; NM_113456.4. [O82568-1]
DR RefSeq; NP_850744.1; NM_180413.2. [O82568-1]
DR AlphaFoldDB; O82568; -.
DR BioGRID; 10843; 3.
DR IntAct; O82568; 3.
DR STRING; 3702.AT3G25585.4; -.
DR PaxDb; O82568; -.
DR PRIDE; O82568; -.
DR ProteomicsDB; 245142; -. [O82568-1]
DR EnsemblPlants; AT3G25585.1; AT3G25585.1; AT3G25585. [O82568-1]
DR EnsemblPlants; AT3G25585.2; AT3G25585.2; AT3G25585. [O82568-1]
DR EnsemblPlants; AT3G25585.4; AT3G25585.4; AT3G25585. [O82568-1]
DR GeneID; 825529; -.
DR Gramene; AT3G25585.1; AT3G25585.1; AT3G25585. [O82568-1]
DR Gramene; AT3G25585.2; AT3G25585.2; AT3G25585. [O82568-1]
DR Gramene; AT3G25585.4; AT3G25585.4; AT3G25585. [O82568-1]
DR KEGG; ath:AT3G25585; -.
DR Araport; AT3G25585; -.
DR TAIR; locus:2094513; AT3G25585.
DR eggNOG; KOG2877; Eukaryota.
DR HOGENOM; CLU_035066_0_1_1; -.
DR InParanoid; O82568; -.
DR OMA; PWGYDAS; -.
DR PhylomeDB; O82568; -.
DR BioCyc; ARA:AT3G25585-MON; -.
DR BRENDA; 2.7.8.1; 399.
DR UniPathway; UPA00558; UER00743.
DR UniPathway; UPA00753; UER00740.
DR PRO; PR:O82568; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; O82568; baseline and differential.
DR Genevisible; O82568; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004142; F:diacylglycerol cholinephosphotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004307; F:ethanolaminephosphotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.120.1760; -; 1.
DR InterPro; IPR000462; CDP-OH_P_trans.
DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR InterPro; IPR014472; CHOPT.
DR PANTHER; PTHR10414; PTHR10414; 1.
DR Pfam; PF01066; CDP-OH_P_transf; 1.
DR PIRSF; PIRSF015665; CHOPT; 1.
DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Lipid biosynthesis; Lipid metabolism; Magnesium;
KW Manganese; Membrane; Metal-binding; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..389
FT /note="Choline/ethanolaminephosphotransferase 2"
FT /id="PRO_0000423345"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 389 AA; 43639 MW; 8289E7671D2BAC55 CRC64;
MGYIGAHGVA ALKKHKYSGV DHSYLAKYVL QPFWNRFVKI FPLWMPPNMI TLMGFMFLLT
SALLGYIYSP KLDSPPPRWV HFAHGLLLFL YQTFDAVDGK QARRTNSSSP LGELFDHGCD
ALGCALETMA YGSTAMCGRD TFWFWVISAV PFFGATWEHY FTNTLTLPVV NGPTEGLALI
YCGHFFTAIV GAEWWAQPFG KSIPLFSWVP FLNEMQMSRI ILFSMIFFAV IPTLAINTSN
VYKVVHSRNG SMLLALAMLY PLVTLIAGVL IWDYLSPIDL IRNYPHLVVL GTGLAFGFLV
GRMILAHLCD EPKGLKTNMC MSLLYLPFAL ANALTARLND GVPLVDEFWV LLGYCIFTLS
LYAHFATSVI HEITTALGIY CFRITRKEA
