AT2L1_HUMAN
ID AT2L1_HUMAN Reviewed; 499 AA.
AC Q8TBG4; B7Z1Y0; E9PBY0; Q9H174;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Ethanolamine-phosphate phospho-lyase;
DE EC=4.2.3.2 {ECO:0000269|PubMed:22241472};
DE AltName: Full=Alanine--glyoxylate aminotransferase 2-like 1;
GN Name=ETNPPL; Synonyms=AGXT2L1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=7592550; DOI=10.1093/oxfordjournals.jbchem.a124787;
RA Matsui-Lee I.S., Muragaki Y., Ideguchi T., Hase T., Tsuji M., Ooshima A.,
RA Okuno E., Kido R.;
RT "Molecular cloning and sequencing of a cDNA encoding alanine-glyoxylate
RT aminotransferase 2 from rat kidney.";
RL J. Biochem. 117:856-862(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain cortex, and Kidney;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22241472; DOI=10.1074/jbc.m111.323485;
RA Veiga-da-Cunha M., Hadi F., Balligand T., Stroobant V., Van Schaftingen E.;
RT "Molecular identification of hydroxylysine kinase and of
RT ammoniophospholyases acting on 5-phosphohydroxy-L-lysine and
RT phosphoethanolamine.";
RL J. Biol. Chem. 287:7246-7255(2012).
CC -!- FUNCTION: Catalyzes the pyridoxal-phosphate-dependent breakdown of
CC phosphoethanolamine, converting it to ammonia, inorganic phosphate and
CC acetaldehyde. {ECO:0000269|PubMed:22241472}.
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 Evidence={ECO:0000269|PubMed:22241472};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:22241472};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=680 uM for phosphoethanolamine (at pH 7.4)
CC {ECO:0000269|PubMed:22241472};
CC Vmax=1.46 umol/min/mg enzyme (at pH 7.4)
CC {ECO:0000269|PubMed:22241472};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8TBG4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TBG4-2; Sequence=VSP_025583;
CC Name=3;
CC IsoId=Q8TBG4-3; Sequence=VSP_046097;
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:0000305|PubMed:22241472}.
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DR EMBL; AJ298293; CAC22253.1; -; mRNA.
DR EMBL; AK091888; BAC03766.1; -; mRNA.
DR EMBL; AK294072; BAH11666.1; -; mRNA.
DR EMBL; AC097473; AAY40946.1; -; Genomic_DNA.
DR EMBL; BC022526; AAH22526.1; -; mRNA.
DR CCDS; CCDS3682.1; -. [Q8TBG4-1]
DR CCDS; CCDS54792.1; -. [Q8TBG4-3]
DR CCDS; CCDS54793.1; -. [Q8TBG4-2]
DR RefSeq; NP_001140062.1; NM_001146590.1. [Q8TBG4-2]
DR RefSeq; NP_001140099.1; NM_001146627.1. [Q8TBG4-3]
DR RefSeq; NP_001317960.1; NM_001331031.1.
DR RefSeq; NP_001317961.1; NM_001331032.1.
DR RefSeq; NP_001317962.1; NM_001331033.1.
DR RefSeq; NP_112569.2; NM_031279.3. [Q8TBG4-1]
DR PDB; 6TOR; X-ray; 2.05 A; A/B=1-499.
DR PDBsum; 6TOR; -.
DR AlphaFoldDB; Q8TBG4; -.
DR SMR; Q8TBG4; -.
DR BioGRID; 122323; 5.
DR IntAct; Q8TBG4; 3.
DR STRING; 9606.ENSP00000296486; -.
DR iPTMnet; Q8TBG4; -.
DR PhosphoSitePlus; Q8TBG4; -.
DR BioMuta; ETNPPL; -.
DR DMDM; 74751376; -.
DR jPOST; Q8TBG4; -.
DR MassIVE; Q8TBG4; -.
DR MaxQB; Q8TBG4; -.
DR PaxDb; Q8TBG4; -.
DR PeptideAtlas; Q8TBG4; -.
DR PRIDE; Q8TBG4; -.
DR ProteomicsDB; 19316; -.
DR ProteomicsDB; 74014; -. [Q8TBG4-1]
DR ProteomicsDB; 74015; -. [Q8TBG4-2]
DR Antibodypedia; 45175; 59 antibodies from 22 providers.
DR DNASU; 64850; -.
DR Ensembl; ENST00000296486.8; ENSP00000296486.3; ENSG00000164089.9. [Q8TBG4-1]
DR Ensembl; ENST00000411864.6; ENSP00000392269.2; ENSG00000164089.9. [Q8TBG4-2]
DR Ensembl; ENST00000512646.5; ENSP00000427065.1; ENSG00000164089.9. [Q8TBG4-3]
DR GeneID; 64850; -.
DR KEGG; hsa:64850; -.
DR MANE-Select; ENST00000296486.8; ENSP00000296486.3; NM_031279.4; NP_112569.2.
DR UCSC; uc003hzc.4; human. [Q8TBG4-1]
DR CTD; 64850; -.
DR DisGeNET; 64850; -.
DR GeneCards; ETNPPL; -.
DR HGNC; HGNC:14404; ETNPPL.
DR HPA; ENSG00000164089; Group enriched (brain, liver).
DR MIM; 614682; gene.
DR neXtProt; NX_Q8TBG4; -.
DR OpenTargets; ENSG00000164089; -.
DR PharmGKB; PA24635; -.
DR VEuPathDB; HostDB:ENSG00000164089; -.
DR eggNOG; KOG1403; Eukaryota.
DR GeneTree; ENSGT00940000157910; -.
DR InParanoid; Q8TBG4; -.
DR OMA; MVPNYNP; -.
DR OrthoDB; 145181at2759; -.
DR PhylomeDB; Q8TBG4; -.
DR TreeFam; TF320468; -.
DR PathwayCommons; Q8TBG4; -.
DR Reactome; R-HSA-1483213; Synthesis of PE.
DR SignaLink; Q8TBG4; -.
DR BioGRID-ORCS; 64850; 12 hits in 1027 CRISPR screens.
DR GenomeRNAi; 64850; -.
DR Pharos; Q8TBG4; Tbio.
DR PRO; PR:Q8TBG4; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q8TBG4; protein.
DR Bgee; ENSG00000164089; Expressed in cranial nerve II and 151 other tissues.
DR ExpressionAtlas; Q8TBG4; baseline and differential.
DR Genevisible; Q8TBG4; HS.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0050459; F:ethanolamine-phosphate phospho-lyase activity; IDA:FlyBase.
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 SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Lyase; Mitochondrion;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..499
FT /note="Ethanolamine-phosphate phospho-lyase"
FT /id="PRO_0000287663"
FT REGION 468..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 278
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..59
FT /note="MCELYSKRDTLGLRKKHIGPSCKVFFASDPIKIVRAQRQYMFDENGEQYLDC
FT INNVAHV -> M (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046097"
FT VAR_SEQ 59..64
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7592550"
FT /id="VSP_025583"
FT VARIANT 185
FT /note="S -> P (in dbSNP:rs1377210)"
FT /id="VAR_032342"
FT CONFLICT 105
FT /note="V -> A (in Ref. 2; BAH11666)"
FT /evidence="ECO:0000305"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:6TOR"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:6TOR"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:6TOR"
FT HELIX 64..74
FT /evidence="ECO:0007829|PDB:6TOR"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:6TOR"
FT HELIX 86..97
FT /evidence="ECO:0007829|PDB:6TOR"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:6TOR"
FT HELIX 112..127
FT /evidence="ECO:0007829|PDB:6TOR"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:6TOR"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:6TOR"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:6TOR"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:6TOR"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:6TOR"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:6TOR"
FT HELIX 185..202
FT /evidence="ECO:0007829|PDB:6TOR"
FT STRAND 207..216
FT /evidence="ECO:0007829|PDB:6TOR"
FT TURN 217..220
FT /evidence="ECO:0007829|PDB:6TOR"
FT HELIX 228..238
FT /evidence="ECO:0007829|PDB:6TOR"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:6TOR"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:6TOR"
FT TURN 252..255
FT /evidence="ECO:0007829|PDB:6TOR"
FT HELIX 261..265
FT /evidence="ECO:0007829|PDB:6TOR"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:6TOR"
FT HELIX 278..281
FT /evidence="ECO:0007829|PDB:6TOR"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:6TOR"
FT HELIX 293..300
FT /evidence="ECO:0007829|PDB:6TOR"
FT HELIX 314..329
FT /evidence="ECO:0007829|PDB:6TOR"
FT HELIX 332..353
FT /evidence="ECO:0007829|PDB:6TOR"
FT STRAND 357..363
FT /evidence="ECO:0007829|PDB:6TOR"
FT STRAND 366..373
FT /evidence="ECO:0007829|PDB:6TOR"
FT TURN 375..377
FT /evidence="ECO:0007829|PDB:6TOR"
FT HELIX 382..394
FT /evidence="ECO:0007829|PDB:6TOR"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:6TOR"
FT TURN 403..406
FT /evidence="ECO:0007829|PDB:6TOR"
FT STRAND 408..411
FT /evidence="ECO:0007829|PDB:6TOR"
FT HELIX 419..440
FT /evidence="ECO:0007829|PDB:6TOR"
SQ SEQUENCE 499 AA; 55671 MW; 3C610898060474B4 CRC64;
MCELYSKRDT LGLRKKHIGP SCKVFFASDP IKIVRAQRQY MFDENGEQYL DCINNVAHVG
HCHPGVVKAA LKQMELLNTN SRFLHDNIVE YAKRLSATLP EKLSVCYFTN SGSEANDLAL
RLARQFRGHQ DVITLDHAYH GHLSSLIEIS PYKFQKGKDV KKEFVHVAPT PDTYRGKYRE
DHADSASAYA DEVKKIIEDA HNSGRKIAAF IAESMQSCGG QIIPPAGYFQ KVAEYVHGAG
GVFIADEVQV GFGRVGKHFW SFQMYGEDFV PDIVTMGKPM GNGHPVACVV TTKEIAEAFS
SSGMEYFNTY GGNPVSCAVG LAVLDIIENE DLQGNAKRVG NYLTELLKKQ KAKHTLIGDI
RGIGLFIGID LVKDHLKRTP ATAEAQHIIY KMKEKRVLLS ADGPHRNVLK IKPPMCFTEE
DAKFMVDQLD RILTVLEEAM GTKTESVTSE NTPCKTKMLK EAHIELLRDS TTDSKENPSR
KRNGMCTDTH SLLSKRLKT
