EPT1_PONAB
ID EPT1_PONAB Reviewed; 397 AA.
AC Q5NV96;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 10-FEB-2021, entry version 69.
DE RecName: Full=Ethanolaminephosphotransferase 1 {ECO:0000305};
DE EC=2.7.8.1 {ECO:0000250|UniProtKB:Q9C0D9};
DE AltName: Full=Selenoprotein I {ECO:0000250|UniProtKB:Q9C0D9};
DE Short=SelI {ECO:0000250|UniProtKB:Q9C0D9};
GN Name=SELENOI {ECO:0000250|UniProtKB:Q9C0D9};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ethanolaminephosphotransferase that catalyzes the transfer of
CC phosphoethanolamine/PE from CDP-ethanolamine to lipid acceptors, the
CC final step in the synthesis of PE via the 'Kennedy' pathway. PE is the
CC second most abundant phospholipid of membranes in mammals and is
CC involved in various membrane-related cellular processes. The enzyme is
CC critical for the synthesis of several PE species and could also
CC catalyze the synthesis of ether-linked phospholipids like
CC plasmanyl- and plasmenyl-PE which could explain it is required for
CC proper myelination and neurodevelopment.
CC {ECO:0000250|UniProtKB:Q9C0D9}.
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:0000250|UniProtKB:Q9C0D9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32944;
CC Evidence={ECO:0000250|UniProtKB:Q9C0D9};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9C0D9};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9C0D9};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from ethanolamine: step 3/3.
CC {ECO:0000250|UniProtKB:Q9C0D9}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9C0D9}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9C0D9}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000305}.
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DR EMBL; CR926492; CAI30284.1; -; mRNA.
DR RefSeq; NP_001127136.1; NM_001133664.1.
DR STRING; 9601.ENSPPYP00000014048; -.
DR GeneID; 100174185; -.
DR KEGG; pon:100174185; -.
DR CTD; 85465; -.
DR eggNOG; KOG2877; Eukaryota.
DR InParanoid; Q5NV96; -.
DR OrthoDB; 847100at2759; -.
DR UniPathway; UPA00558; UER00743.
DR Proteomes; UP000001595; Unplaced.
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:0004307; F:ethanolaminephosphotransferase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Acetylation; Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism;
KW Magnesium; Manganese; Membrane; Metal-binding; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Selenocysteine; Transferase;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9C0D9"
FT CHAIN 2..397
FT /note="Ethanolaminephosphotransferase 1"
FT /id="PRO_0000056815"
FT TRANSMEM 47..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT NON_STD 387
FT /note="Selenocysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0D9"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0D9"
SQ SEQUENCE 397 AA; 45290 MW; A41A7285A3609209 CRC64;
MAGYEYVSPE QLAGFDKHKY SAVDTNPLSL YVMHPFWNTI VKVFPTWLAP NLITFSGFLL
VVFNFLLMAY FDPDFYASAP GHKHVPDWVW IVVGILNFVA YTLDGVDGKQ ARRTNSSTPL
GELFDHGLDN WSYVYFVVTV YSIFGRGSTG VSVFVLYLLL WVVLFSFILS HWEKYNTGIL
FLPWGYDISQ VTISFVYIVT AVVGVEAWYE PFLFNFLYRD LFTAMIIGCA LCVTLPMSLL
NFFRSYKNNT LKLNSVYEAM VPLFSPCLLF ILSTAWILWS PSDILELHPR VFYFMVGTAF
ANSTCQLIVC QMSSTRCPTL NWLLVPLFLV VLVVNLGVAS YVESILLYTL TTAFTLAHIH
YGVRVVKQLS SHFQIYPFSL RKPNSDULGM EEKNIGL
