Q8TBG4 (AT2L1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ethanolamine-phosphate phospho-lyase
EC=4.2.3.2

Alternative name(s):
Alanine--glyoxylate aminotransferase 2-like 1

Gene names

Name:

AGXT2L1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	499 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the pyridoxal-phosphate-dependent breakdown of phosphoethanolamine, converting it to ammonia, inorganic phosphate and acetaldehyde. Ref.5
Catalytic activity	Ethanolamine phosphate + H2O = acetaldehyde + NH3 + phosphate. Ref.5
Cofactor	Pyridoxal phosphate. Ref.5
Subunit structure	Homotetramer By similarity.
Subcellular location	Mitochondrion Potential.
Sequence similarities	Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.
Caution	Does not seem to possess aminotransferase activity (Ref.5).
Biophysicochemical properties	Kinetic parameters: KM=680 µM for phosphoethanolamine (at pH 7.4) Ref.5 Vmax=1.46 µmol/min/mg enzyme (at pH 7.4)

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Lyase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular amino acid metabolic process Non-traceable author statement. Source: UniProtKB
Cellular_component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	alanine-glyoxylate transaminase activity Non-traceable author statement. Source: UniProtKB ethanolamine-phosphate phospho-lyase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8TBG4-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q8TBG4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     59-64: Missing.

Isoform 3 (identifier: Q8TBG4-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-59: MCELYSKRDTLGLRKKHIGPSCKVFFASDPIKIVRAQRQYMFDENGEQYLDCINNVAHV → M

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 499	499	Ethanolamine-phosphate phospho-lyase		PRO_0000287663
Amino acid modifications
	Modified residue	278	1	N6-(pyridoxal phosphate)lysine By similarity
Natural variations
	Alternative sequence	1 – 59	59	MCELY…NVAHV → M in isoform 3.		VSP_046097
	Alternative sequence	59 – 64	6	Missing in isoform 2.		VSP_025583
	Natural variant	185	1	S → P. Corresponds to variant rs1377210 [ dbSNP | Ensembl ].		VAR_032342
Experimental info
	Sequence conflict	105	1	V → A in BAH11666. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 3C610898060474B4	FASTA	499	55,671
	10 20 30 40 50 60 MCELYSKRDT LGLRKKHIGP SCKVFFASDP IKIVRAQRQY MFDENGEQYL DCINNVAHVG 70 80 90 100 110 120 HCHPGVVKAA LKQMELLNTN SRFLHDNIVE YAKRLSATLP EKLSVCYFTN SGSEANDLAL 130 140 150 160 170 180 RLARQFRGHQ DVITLDHAYH GHLSSLIEIS PYKFQKGKDV KKEFVHVAPT PDTYRGKYRE 190 200 210 220 230 240 DHADSASAYA DEVKKIIEDA HNSGRKIAAF IAESMQSCGG QIIPPAGYFQ KVAEYVHGAG 250 260 270 280 290 300 GVFIADEVQV GFGRVGKHFW SFQMYGEDFV PDIVTMGKPM GNGHPVACVV TTKEIAEAFS 310 320 330 340 350 360 SSGMEYFNTY GGNPVSCAVG LAVLDIIENE DLQGNAKRVG NYLTELLKKQ KAKHTLIGDI 370 380 390 400 410 420 RGIGLFIGID LVKDHLKRTP ATAEAQHIIY KMKEKRVLLS ADGPHRNVLK IKPPMCFTEE 430 440 450 460 470 480 DAKFMVDQLD RILTVLEEAM GTKTESVTSE NTPCKTKMLK EAHIELLRDS TTDSKENPSR 490 KRNGMCTDTH SLLSKRLKT
	Isoform 2 [UniParc]. Checksum: 550C3D17990588B3	FASTA	493	55,040
	10 20 30 40 50 60 MCELYSKRDT LGLRKKHIGP SCKVFFASDP IKIVRAQRQY MFDENGEQYL DCINNVAHGV 70 80 90 100 110 120 VKAALKQMEL LNTNSRFLHD NIVEYAKRLS ATLPEKLSVC YFTNSGSEAN DLALRLARQF 130 140 150 160 170 180 RGHQDVITLD HAYHGHLSSL IEISPYKFQK GKDVKKEFVH VAPTPDTYRG KYREDHADSA 190 200 210 220 230 240 SAYADEVKKI IEDAHNSGRK IAAFIAESMQ SCGGQIIPPA GYFQKVAEYV HGAGGVFIAD 250 260 270 280 290 300 EVQVGFGRVG KHFWSFQMYG EDFVPDIVTM GKPMGNGHPV ACVVTTKEIA EAFSSSGMEY 310 320 330 340 350 360 FNTYGGNPVS CAVGLAVLDI IENEDLQGNA KRVGNYLTEL LKKQKAKHTL IGDIRGIGLF 370 380 390 400 410 420 IGIDLVKDHL KRTPATAEAQ HIIYKMKEKR VLLSADGPHR NVLKIKPPMC FTEEDAKFMV 430 440 450 460 470 480 DQLDRILTVL EEAMGTKTES VTSENTPCKT KMLKEAHIEL LRDSTTDSKE NPSRKRNGMC 490 TDTHSLLSKR LKT
	Isoform 3 [UniParc]. Checksum: 922846180BD29061	FASTA	441	48,942
	10 20 30 40 50 60 MGHCHPGVVK AALKQMELLN TNSRFLHDNI VEYAKRLSAT LPEKLSVCYF TNSGSEANDL 70 80 90 100 110 120 ALRLARQFRG HQDVITLDHA YHGHLSSLIE ISPYKFQKGK DVKKEFVHVA PTPDTYRGKY 130 140 150 160 170 180 REDHADSASA YADEVKKIIE DAHNSGRKIA AFIAESMQSC GGQIIPPAGY FQKVAEYVHG 190 200 210 220 230 240 AGGVFIADEV QVGFGRVGKH FWSFQMYGED FVPDIVTMGK PMGNGHPVAC VVTTKEIAEA 250 260 270 280 290 300 FSSSGMEYFN TYGGNPVSCA VGLAVLDIIE NEDLQGNAKR VGNYLTELLK KQKAKHTLIG 310 320 330 340 350 360 DIRGIGLFIG IDLVKDHLKR TPATAEAQHI IYKMKEKRVL LSADGPHRNV LKIKPPMCFT 370 380 390 400 410 420 EEDAKFMVDQ LDRILTVLEE AMGTKTESVT SENTPCKTKM LKEAHIELLR DSTTDSKENP 430 440 SRKRNGMCTD THSLLSKRLK T

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and sequencing of a cDNA encoding alanine-glyoxylate aminotransferase 2 from rat kidney." Matsui-Lee I.S., Muragaki Y., Ideguchi T., Hase T., Tsuji M., Ooshima A., Okuno E., Kido R. J. Biochem. 117:856-862(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). Tissue: Brain cortex and Kidney.
[3]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[5]	"Molecular identification of hydroxylysine kinase and of ammoniophospholyases acting on 5-phosphohydroxy-L-lysine and phosphoethanolamine." Veiga-da-Cunha M., Hadi F., Balligand T., Stroobant V., Van Schaftingen E. J. Biol. Chem. 287:7246-7255(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ298293 mRNA. Translation: CAC22253.1. AK091888 mRNA. Translation: BAC03766.1. AK294072 mRNA. Translation: BAH11666.1. AC097473 Genomic DNA. Translation: AAY40946.1. BC022526 mRNA. Translation: AAH22526.1.
IPI	IPI00152204. IPI00845332. IPI00929120.
RefSeq	NP_001140062.1. NM_001146590.1. NP_001140099.1. NM_001146627.1. NP_112569.2. NM_031279.3.
UniGene	Hs.106576.
3D structure databases
HSSP	HSSP built from PDB template 1QJ3 based on UniProtKB P12995.
ProteinModelPortal	Q8TBG4.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000296486.
PTM databases
PhosphoSite	Q8TBG4.
Polymorphism databases
DMDM	74751376.
Proteomic databases
PaxDb	Q8TBG4.
PRIDE	Q8TBG4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000296486; ENSP00000296486; ENSG00000164089. ENST00000411864; ENSP00000392269; ENSG00000164089. ENST00000512646; ENSP00000427065; ENSG00000164089.
GeneID	64850.
KEGG	hsa:64850.
UCSC	uc003hzc.3. human. uc010imc.3. human.
Organism-specific databases
CTD	64850.
GeneCards	GC04M109663.
HGNC	HGNC:14404. AGXT2L1.
HPA	HPA044546.
MIM	614682. gene.
neXtProt	NX_Q8TBG4.
PharmGKB	PA24635.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0160.
HOGENOM	HOG000020206.
HOVERGEN	HBG004196.
InParanoid	Q8TBG4.
KO	K14286.
OMA	KIIEDAH.
OrthoDB	EOG4TTGHM.
PhylomeDB	Q8TBG4.
Gene expression databases
ArrayExpress	Q8TBG4.
Bgee	Q8TBG4.
CleanEx	HS_AGXT2L1.
Genevestigator	Q8TBG4.
Family and domain databases
Gene3D	3.40.640.10. 1 hit. 3.90.1150.10. 1 hit.
InterPro	IPR005814. Aminotrans_3. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
PANTHER	PTHR11986. PTHR11986. 1 hit.
Pfam	PF00202. Aminotran_3. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
PROSITE	PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	64850.
NextBio	66972.
SOURCE	Search...

Entry information

Entry name

AT2L1_HUMAN

Accession

Primary (citable) accession number: Q8TBG4
Secondary accession number(s): B7Z1Y0, E9PBY0, Q9H174

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 15, 2007
Last sequence update:	June 1, 2002
Last modified:	May 1, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.