AT2L1_MOUSE
ID AT2L1_MOUSE Reviewed; 499 AA.
AC Q8BWU8; Q811K4; Q9DBB3;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Ethanolamine-phosphate phospho-lyase;
DE EC=4.2.3.2;
DE AltName: Full=Alanine--glyoxylate aminotransferase 2-like 1;
GN Name=Etnppl; Synonyms=Agxt2l1;
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 STRAIN=C57BL/6J; TISSUE=Hippocampus, and Liver;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Eye, and Liver;
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: Catalyzes the pyridoxal-phosphate-dependent breakdown of
CC phosphoethanolamine, converting it to ammonia, inorganic phosphate and
CC acetaldehyde. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + phosphoethanolamine = acetaldehyde + NH4(+) + phosphate;
CC Xref=Rhea:RHEA:17889, ChEBI:CHEBI:15343, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:43474, ChEBI:CHEBI:58190; EC=4.2.3.2;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- CAUTION: Does not seem to possess aminotransferase activity.
CC {ECO:0000250|UniProtKB:Q8TBG4}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK005060; BAB23784.1; -; mRNA.
DR EMBL; AK049937; BAC33993.1; -; mRNA.
DR EMBL; BC043680; AAH43680.2; -; mRNA.
DR EMBL; BC058592; AAH58592.1; -; mRNA.
DR CCDS; CCDS38638.1; -.
DR RefSeq; NP_001157059.1; NM_001163587.1.
DR RefSeq; NP_082183.2; NM_027907.3.
DR AlphaFoldDB; Q8BWU8; -.
DR SMR; Q8BWU8; -.
DR IntAct; Q8BWU8; 1.
DR STRING; 10090.ENSMUSP00000072121; -.
DR iPTMnet; Q8BWU8; -.
DR PhosphoSitePlus; Q8BWU8; -.
DR jPOST; Q8BWU8; -.
DR MaxQB; Q8BWU8; -.
DR PaxDb; Q8BWU8; -.
DR PRIDE; Q8BWU8; -.
DR ProteomicsDB; 265128; -.
DR Antibodypedia; 45175; 59 antibodies from 22 providers.
DR DNASU; 71760; -.
DR Ensembl; ENSMUST00000072271; ENSMUSP00000072121; ENSMUSG00000019232.
DR Ensembl; ENSMUST00000166187; ENSMUSP00000131294; ENSMUSG00000019232.
DR GeneID; 71760; -.
DR KEGG; mmu:71760; -.
DR UCSC; uc008rjb.2; mouse.
DR CTD; 64850; -.
DR MGI; MGI:1919010; Etnppl.
DR VEuPathDB; HostDB:ENSMUSG00000019232; -.
DR eggNOG; KOG1403; Eukaryota.
DR GeneTree; ENSGT00940000157910; -.
DR HOGENOM; CLU_016922_8_0_1; -.
DR InParanoid; Q8BWU8; -.
DR OMA; MVPNYNP; -.
DR OrthoDB; 145181at2759; -.
DR PhylomeDB; Q8BWU8; -.
DR TreeFam; TF320468; -.
DR Reactome; R-MMU-1483213; Synthesis of PE.
DR BioGRID-ORCS; 71760; 2 hits in 75 CRISPR screens.
DR PRO; PR:Q8BWU8; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8BWU8; protein.
DR Bgee; ENSMUSG00000019232; Expressed in lumbar subsegment of spinal cord and 98 other tissues.
DR ExpressionAtlas; Q8BWU8; baseline and differential.
DR Genevisible; Q8BWU8; MM.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0050459; F:ethanolamine-phosphate phospho-lyase activity; ISO:MGI.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 2: Evidence at transcript level;
KW Lyase; Mitochondrion; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..499
FT /note="Ethanolamine-phosphate phospho-lyase"
FT /id="PRO_0000287664"
FT MOD_RES 278
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 12
FT /note="A -> V (in Ref. 2; AAH43680)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="N -> D (in Ref. 1; BAB23784)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 499 AA; 55496 MW; 8CC1EDD075AAFDD1 CRC64;
MCELYSKQDT LALRERHIGP SCKIFFAADP IKIMRAQGQY MFDEKGERYL DCINNVAHVG
HCHPEVVKAA AKQMELLNTN SRFLHDNIIE FAKRLTATLP QELSVCYFTN SGSEANDLAL
RLARQFRGHQ DVITLDHAYH GHLSSLIEIS PYKFQKGKDV KRETVHVAPA PDTYRGKYRE
DHEDPSTAYA DEVKKIIEEA HSSGRKIAAF IAESMQSCGG QIIPPAGYFQ KVAEHIHKAG
GVFIADEVQV GFGRVGRYFW SFQMYGEDFV PDIVTMGKPM GNGHPISCVV TTKEIAEAFS
SSGMEYFNTY GGNPVSCAVG LAVLDVIEKE NLQGNAVRVG TYLMELLSEQ KAKHPLIGDI
RGVGLFIGID LVKDREKRTP ATAEAQHIIY EMKGKGVLLS ADGPHRNVLK IKPPMCFTED
DAKFLVDHLD GILTVLEEAM DSKSGTVFSE NTAYRTKMPK EIQVELPNLS ATEAREIPRG
KRNGVCSDQQ ALLSKRLKT
