EPT1_BOVIN
ID EPT1_BOVIN Reviewed; 397 AA.
AC Q17QM4;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 90.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Brain cortex;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI18274.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC118273; AAI18274.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001068725.2; NM_001075257.1.
DR STRING; 9913.ENSBTAP00000010310; -.
DR PaxDb; Q17QM4; -.
DR Ensembl; ENSBTAT00000010310; ENSBTAP00000010310; ENSBTAG00000007837.
DR GeneID; 506381; -.
DR KEGG; bta:506381; -.
DR CTD; 85465; -.
DR VEuPathDB; HostDB:ENSBTAG00000007837; -.
DR VGNC; VGNC:97309; SELENOI.
DR eggNOG; KOG2877; Eukaryota.
DR GeneTree; ENSGT00950000183117; -.
DR HOGENOM; CLU_035066_2_0_1; -.
DR InParanoid; Q17QM4; -.
DR OMA; FPYQNVL; -.
DR OrthoDB; 847100at2759; -.
DR TreeFam; TF313270; -.
DR Reactome; R-BTA-1483213; Synthesis of PE.
DR UniPathway; UPA00558; UER00743.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000007837; Expressed in conceptus and 106 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
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_0000289258"
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; 45214 MW; A393118B091D26F3 CRC64;
MASYEYVSPE QLAGFDKYKY SAVDTNPLSL YVMHPFWNTV VKVFPTWLAP NLITFSGFLL
VVFNFLLLAY FDPDFYASAP GHKHVPDWVW IVVGILNFMA YTLDGVDGKQ ARRTNSSTPL
GELFDHGLDS WSCVYFVVTV YSIFGRGSSG VSVFVLYLLL WVVLFSFILS HWEKYNTGIL
FLPWGYDISQ VTISFVYIVT AVVGVEAWYE PFLFNFLYRD LFTAMIFGCA LCVTLPMSLL
NFFRSYKNNT LKHNSVYEAV VPFFSPCLLF ILSTAWILLS PSDILELHPR VFYLMVGTAF
ANSTCQLIVC QMSSTRCPTL NWLLLPLFVI VMVVNVGVTP YVESILLFTL TAAFTLAHIH
YGVRVVKQLS NHFHIYPFSL RKPNSDULGV EEKNIGL
