EPT1_MOUSE
ID EPT1_MOUSE Reviewed; 398 AA.
AC Q80TA1; Q3KQQ5; Q8BG08;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 125.
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:0000312|MGI:MGI:107898};
GN Synonyms=D5Wsu178e {ECO:0000312|EMBL:AAI06098.2},
GN Ept1 {ECO:0000312|MGI:MGI:107898}, Kiaa1724 {ECO:0000312|EMBL:BAC65826.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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=BAC33214.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC37608.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC65826.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK122544; BAC65826.1; ALT_SEQ; mRNA.
DR EMBL; AK048011; BAC33214.1; ALT_SEQ; mRNA.
DR EMBL; AK079325; BAC37608.1; ALT_SEQ; mRNA.
DR EMBL; BC106097; AAI06098.2; -; mRNA.
DR EMBL; BC115783; AAI15784.2; -; mRNA.
DR EMBL; BC117551; AAI17552.2; -; mRNA.
DR CCDS; CCDS51451.1; -.
DR RefSeq; NP_081928.2; NM_027652.3.
DR BioGRID; 205731; 1.
DR STRING; 10090.ENSMUSP00000118368; -.
DR iPTMnet; Q80TA1; -.
DR PhosphoSitePlus; Q80TA1; -.
DR EPD; Q80TA1; -.
DR jPOST; Q80TA1; -.
DR MaxQB; Q80TA1; -.
DR PaxDb; Q80TA1; -.
DR PeptideAtlas; Q80TA1; -.
DR PRIDE; Q80TA1; -.
DR ProteomicsDB; 275874; -.
DR Antibodypedia; 60801; 13 antibodies from 6 providers.
DR DNASU; 28042; -.
DR Ensembl; ENSMUST00000145167; ENSMUSP00000118368; ENSMUSG00000075703.
DR GeneID; 28042; -.
DR KEGG; mmu:28042; -.
DR UCSC; uc008wvh.1; mouse.
DR CTD; 85465; -.
DR MGI; MGI:107898; Selenoi.
DR VEuPathDB; HostDB:ENSMUSG00000075703; -.
DR eggNOG; KOG2877; Eukaryota.
DR GeneTree; ENSGT00950000183117; -.
DR HOGENOM; CLU_035066_2_0_1; -.
DR InParanoid; Q80TA1; -.
DR OMA; FPYQNVL; -.
DR OrthoDB; 847100at2759; -.
DR PhylomeDB; Q80TA1; -.
DR TreeFam; TF313270; -.
DR Reactome; R-MMU-1483213; Synthesis of PE.
DR UniPathway; UPA00558; UER00743.
DR BioGRID-ORCS; 28042; 15 hits in 75 CRISPR screens.
DR ChiTaRS; Selenoi; mouse.
DR PRO; PR:Q80TA1; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q80TA1; protein.
DR Bgee; ENSMUSG00000075703; Expressed in superior cervical ganglion and 213 other tissues.
DR ExpressionAtlas; Q80TA1; baseline and differential.
DR Genevisible; Q80TA1; MM.
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..398
FT /note="Ethanolaminephosphotransferase 1"
FT /id="PRO_0000056814"
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 319..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT NON_STD 388
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 398 AA; 45346 MW; 9DE0703774583D23 CRC64;
MAGYEYVSPE QLSGFDKYKY SALDTNPLSL YIMHPFWNTI VKVFPTWLAP NLITFSGFML
LVFNFLLLTY FDPDFYASAP GHKHVPDWVW IVVGILNFAA YTLDGVDGKQ ARRTNSSTPL
GELFDHGLDS WSCVYFVVTV YSIFGRGPTG VSVFVLYLLL WVVLFSFILS HWEKYNTGVL
FLPWGYDISQ VTISFVYIVT AVVGVEAWYE PFLFNFLYRD LFTAMIIGCA LCVTLPMSLL
NFFRSYKSNT LKHKSVYEAM VPFFSPCLLF TLCTVWILWS PSDILEIHPR IFYFMVGTAF
ANITCQLIVC QMSSTRCPTL NWLLLPLLLV VAAVIVGAAT SRLESALLYT LTAAFTLAHI
HYGVQVVKQL SRHFQIYPFS LRKPNSDULG MEEQNIGL
