AAPT1_ARATH
ID AAPT1_ARATH Reviewed; 389 AA.
AC O82567;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Choline/ethanolaminephosphotransferase 1;
DE EC=2.7.8.1;
DE EC=2.7.8.2;
DE AltName: Full=Aminoalcohol phosphotransferase 1;
DE Short=AtAAPT1;
GN Name=AAPT1; OrderedLocusNames=At1g13560; ORFNames=F13B4.5;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
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=O82567-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000305}.
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DR EMBL; AF091843; AAC61768.1; -; mRNA.
DR EMBL; AC027134; AAF99823.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29034.1; -; Genomic_DNA.
DR EMBL; AY080725; AAL86327.1; -; mRNA.
DR EMBL; AY114062; AAM45110.1; -; mRNA.
DR PIR; F86268; F86268.
DR RefSeq; NP_172813.1; NM_101226.5. [O82567-1]
DR AlphaFoldDB; O82567; -.
DR BioGRID; 23157; 4.
DR IntAct; O82567; 4.
DR STRING; 3702.AT1G13560.1; -.
DR TCDB; 4.F.1.1.2; the choline/ethanolaminephosphotransferase 1 (cept1) family.
DR PaxDb; O82567; -.
DR PRIDE; O82567; -.
DR ProteomicsDB; 245119; -. [O82567-1]
DR EnsemblPlants; AT1G13560.1; AT1G13560.1; AT1G13560. [O82567-1]
DR GeneID; 837917; -.
DR Gramene; AT1G13560.1; AT1G13560.1; AT1G13560. [O82567-1]
DR KEGG; ath:AT1G13560; -.
DR Araport; AT1G13560; -.
DR TAIR; locus:2009947; AT1G13560.
DR eggNOG; KOG2877; Eukaryota.
DR HOGENOM; CLU_035066_0_1_1; -.
DR InParanoid; O82567; -.
DR PhylomeDB; O82567; -.
DR BioCyc; ARA:AT1G13560-MON; -.
DR BRENDA; 2.7.8.1; 399.
DR BRENDA; 2.7.8.2; 399.
DR UniPathway; UPA00558; UER00743.
DR UniPathway; UPA00753; UER00740.
DR PRO; PR:O82567; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O82567; baseline and differential.
DR Genevisible; O82567; AT.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
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 1"
FT /id="PRO_0000423344"
FT TRANSMEM 40..60
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 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 389 AA; 43542 MW; 2B91B905E14B9D17 CRC64;
MGYIGAHGVA ALHRYKYSGV DHSYLAKYVL QPFWTRFVKV FPLWMPPNMI TLMGFMFLVT
SSLLGYIYSP QLDSPPPRWV HFAHGLLLFL YQTFDAVDGK QARRTNSSSP LGELFDHGCD
ALACAFEAMA FGSTAMCGRD TFWFWVISAI PFYGATWEHY FTNTLILPVI NGPTEGLALI
FVSHFFTAIV GAEWWAQQLG QSIPLFSWVP FVNEIQTSRA VLYMMIAFAV IPTVAFNVTN
VYKVVRSRNG SMVLALAMLY PFVVLLGGVL IWDYLSPINL IATYPHLVVL GTGLAFGFLV
GRMILAHLCD EPKGLKTNMC MSLLYLPFAL ANALTARLNA GVPLVDELWV LLGYCIFTVS
LYLHFATSVI HEITEALGIY CFRITRKEA
