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Q8TBG4 (AT2L1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ethanolamine-phosphate phospho-lyase

EC=4.2.3.2
Alternative name(s):
Alanine--glyoxylate aminotransferase 2-like 1
Gene names
Name:ETNPPL
Synonyms:AGXT2L1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length499 AA.
Sequence statusComplete.
Protein existenceEvidence 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 componentMitochondrion
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandPyridoxal phosphate
   Molecular functionAminotransferase
Lyase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionethanolamine-phosphate phospho-lyase activity

Inferred from electronic annotation. Source: UniProtKB-EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

transaminase activity

Inferred from electronic annotation. Source: UniProtKB-KW

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 499499Ethanolamine-phosphate phospho-lyase
PRO_0000287663

Amino acid modifications

Modified residue2781N6-(pyridoxal phosphate)lysine By similarity

Natural variations

Alternative sequence1 – 5959MCELY…NVAHV → M in isoform 3.
VSP_046097
Alternative sequence59 – 646Missing in isoform 2.
VSP_025583
Natural variant1851S → P.
Corresponds to variant rs1377210 [ dbSNP | Ensembl ].
VAR_032342

Experimental info

Sequence conflict1051V → A in BAH11666. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 3C610898060474B4

FASTA49955,671
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 550C3D17990588B3
Show »

FASTA49355,040
Isoform 3 [UniParc].

Checksum: 922846180BD29061
Show »

FASTA44148,942

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
CCDSCCDS3682.1. [Q8TBG4-1]
CCDS54792.1. [Q8TBG4-3]
CCDS54793.1. [Q8TBG4-2]
RefSeqNP_001140062.1. NM_001146590.1. [Q8TBG4-2]
NP_001140099.1. NM_001146627.1. [Q8TBG4-3]
NP_112569.2. NM_031279.3. [Q8TBG4-1]
UniGeneHs.106576.

3D structure databases

ProteinModelPortalQ8TBG4.
SMRQ8TBG4. Positions 15-433.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122323. 2 interactions.
STRING9606.ENSP00000296486.

PTM databases

PhosphoSiteQ8TBG4.

Polymorphism databases

DMDM74751376.

Proteomic databases

MaxQBQ8TBG4.
PaxDbQ8TBG4.
PRIDEQ8TBG4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296486; ENSP00000296486; ENSG00000164089. [Q8TBG4-1]
ENST00000411864; ENSP00000392269; ENSG00000164089. [Q8TBG4-2]
ENST00000512646; ENSP00000427065; ENSG00000164089. [Q8TBG4-3]
GeneID64850.
KEGGhsa:64850.
UCSCuc003hzc.3. human. [Q8TBG4-1]
uc010imc.3. human. [Q8TBG4-2]

Organism-specific databases

CTD64850.
GeneCardsGC04M109664.
HGNCHGNC:14404. ETNPPL.
HPAHPA044546.
MIM614682. gene.
neXtProtNX_Q8TBG4.
PharmGKBPA24635.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0160.
HOGENOMHOG000020206.
HOVERGENHBG004196.
InParanoidQ8TBG4.
KOK14286.
OMAAMCAFEV.
OrthoDBEOG79KPF2.
PhylomeDBQ8TBG4.
TreeFamTF320468.

Gene expression databases

ArrayExpressQ8TBG4.
BgeeQ8TBG4.
CleanExHS_AGXT2L1.
GenevestigatorQ8TBG4.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
InterProIPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR11986. PTHR11986. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
PIRSFPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi64850.
NextBio66972.
PROQ8TBG4.
SOURCESearch...

Entry information

Entry nameAT2L1_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM